KALRN_HUMAN
ID KALRN_HUMAN Reviewed; 2986 AA.
AC O60229; A8MSI4; C9JQ37; J3QSW6; Q6ZN45; Q8TBQ5; Q9NSZ4; Q9Y2A5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Kalirin {ECO:0000250|UniProtKB:P97924};
DE EC=2.7.11.1;
DE AltName: Full=Huntingtin-associated protein-interacting protein;
DE AltName: Full=Protein Duo;
DE AltName: Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain;
GN Name=KALRN {ECO:0000312|HGNC:HGNC:4814}; Synonyms=DUET, DUO, HAPIP, TRAD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Frontal cortex;
RX PubMed=9285789; DOI=10.1093/hmg/6.9.1519;
RA Colomer V., Engelender S., Sharp A.H., Duan K., Cooper J.K., Lanahan A.,
RA Lyford G., Worley P., Ross C.A.;
RT "Huntingtin-associated protein 1 (HAP1) binds to a Trio-like polypeptide,
RT with a rac1 guanine nucleotide exchange factor domain.";
RL Hum. Mol. Genet. 6:1519-1525(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, MUTAGENESIS OF LYS-2713,
RP AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=10023074; DOI=10.1016/s0378-1119(98)00605-2;
RA Kawai T., Sanjo H., Akira S.;
RT "Duet is a novel serine/threonine kinase with Dbl-homology (DH) and
RT pleckstrin-homology (PH) domains.";
RL Gene 227:249-255(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 641-1464 (ISOFORM 1).
RC TISSUE=Amygdala, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1917 (ISOFORM 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2105-2986 (ISOFORM 5).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2017-2986 (ISOFORM 5).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1750; SER-1753; SER-1799;
RP SER-1817 AND SER-2262, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1799, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [11]
RP SPECTRIN REPEATS.
RX PubMed=22738176; DOI=10.1021/bi300583s;
RA Vishwanatha K.S., Wang Y.P., Keutmann H.T., Mains R.E., Eipper B.A.;
RT "Structural organization of the nine spectrin repeats of Kalirin.";
RL Biochemistry 51:5663-5673(2012).
RN [12]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-213 AND CYS-1897.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-196.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Promotes the exchange of GDP by GTP. Activates specific Rho
CC GTPase family members, thereby inducing various signaling mechanisms
CC that regulate neuronal shape, growth, and plasticity, through their
CC effects on the actin cytoskeleton. Induces lamellipodia independent of
CC its GEF activity. {ECO:0000269|PubMed:10023074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha-
CC amidating monooxygenase (PAM) and with the huntingtin-associated
CC protein 1 (HAP1) (By similarity). Interacts with FASLG. {ECO:0000250,
CC ECO:0000269|PubMed:19807924}.
CC -!- INTERACTION:
CC O60229; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-949233, EBI-25475920;
CC O60229; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-949233, EBI-25492395;
CC O60229-2; Q9Y6H5-1: SNCAIP; NbExp=3; IntAct=EBI-9075360, EBI-9075374;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10023074}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10023074}. Note=Associated
CC with the cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O60229-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60229-2; Sequence=VSP_028910, VSP_028911;
CC Name=4; Synonyms=DUET, TRAD;
CC IsoId=O60229-4; Sequence=VSP_028903, VSP_028912;
CC Name=5;
CC IsoId=O60229-5; Sequence=VSP_028904, VSP_028909, VSP_028913,
CC VSP_028914, VSP_028915;
CC Name=6;
CC IsoId=O60229-6; Sequence=VSP_028903, VSP_028912, VSP_028913;
CC -!- TISSUE SPECIFICITY: Isoform 2 is brain specific. Highly expressed in
CC cerebral cortex, putamen, amygdala, hippocampus and caudate nucleus.
CC Weakly expressed in brain stem and cerebellum. Isoform 4 is expressed
CC in skeletal muscle. {ECO:0000269|PubMed:10023074}.
CC -!- DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1 and
CC RhoA which are bound by DH1 and DH2 respectively. The two GEF domains
CC appear to play differing roles in neuronal development and axonal
CC outgrowth. SH3 1 binds to the first GEF domain inhibiting GEF activity
CC only when in the presence of a PXXP peptide, suggesting that the SH3
CC domain/peptide interaction mediates binding to GEF1. CRK1 SH3 domain
CC binds to and inhibits GEF1 activity (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated.
CC -!- MISCELLANEOUS: Called DUO because the encoded protein is closely
CC related to but shorter than TRIO.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58015.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAD18530.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U94190; AAC15791.1; -; mRNA.
DR EMBL; AB011422; BAA76314.1; -; mRNA.
DR EMBL; AK125979; BAC86373.1; -; mRNA.
DR EMBL; AK131379; BAD18530.1; ALT_SEQ; mRNA.
DR EMBL; AC022336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF457679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79410.1; -; Genomic_DNA.
DR EMBL; BC026865; AAH26865.1; -; mRNA.
DR EMBL; BC058015; AAH58015.1; ALT_SEQ; mRNA.
DR EMBL; AL137629; CAB70850.1; -; mRNA.
DR CCDS; CCDS3027.1; -. [O60229-2]
DR CCDS; CCDS3028.1; -. [O60229-4]
DR PIR; T46482; T46482.
DR RefSeq; NP_001019831.2; NM_001024660.4. [O60229-1]
DR RefSeq; NP_001309917.1; NM_001322988.1.
DR RefSeq; NP_001309918.1; NM_001322989.1.
DR RefSeq; NP_001309923.1; NM_001322994.1.
DR RefSeq; NP_001309924.1; NM_001322995.1.
DR RefSeq; NP_001309925.1; NM_001322996.1.
DR RefSeq; NP_001309926.1; NM_001322997.1.
DR RefSeq; NP_001309927.1; NM_001322998.1.
DR RefSeq; NP_001309928.1; NM_001322999.1.
DR RefSeq; NP_001309929.1; NM_001323000.1.
DR RefSeq; NP_001309930.1; NM_001323001.1.
DR RefSeq; NP_003938.1; NM_003947.5. [O60229-2]
DR RefSeq; NP_008995.2; NM_007064.4. [O60229-4]
DR PDB; 5QQD; X-ray; 1.91 A; B=1280-1459.
DR PDB; 5QQE; X-ray; 1.95 A; B=1280-1459.
DR PDB; 5QQF; X-ray; 2.26 A; B=1280-1459.
DR PDB; 5QQG; X-ray; 2.23 A; B=1280-1459.
DR PDB; 5QQH; X-ray; 2.09 A; B=1280-1459.
DR PDB; 5QQI; X-ray; 2.08 A; B=1280-1459.
DR PDB; 5QQJ; X-ray; 1.90 A; B=1280-1459.
DR PDB; 5QQK; X-ray; 2.24 A; B=1280-1459.
DR PDB; 5QQL; X-ray; 2.25 A; B=1280-1459.
DR PDB; 5QQM; X-ray; 2.02 A; B=1280-1459.
DR PDB; 5QQN; X-ray; 2.26 A; B=1280-1459.
DR PDB; 5QU9; X-ray; 2.00 A; B=1280-1459.
DR PDBsum; 5QQD; -.
DR PDBsum; 5QQE; -.
DR PDBsum; 5QQF; -.
DR PDBsum; 5QQG; -.
DR PDBsum; 5QQH; -.
DR PDBsum; 5QQI; -.
DR PDBsum; 5QQJ; -.
DR PDBsum; 5QQK; -.
DR PDBsum; 5QQL; -.
DR PDBsum; 5QQM; -.
DR PDBsum; 5QQN; -.
DR PDBsum; 5QU9; -.
DR SMR; O60229; -.
DR BioGRID; 114478; 26.
DR IntAct; O60229; 19.
DR MINT; O60229; -.
DR STRING; 9606.ENSP00000240874; -.
DR iPTMnet; O60229; -.
DR PhosphoSitePlus; O60229; -.
DR SwissPalm; O60229; -.
DR BioMuta; KALRN; -.
DR EPD; O60229; -.
DR jPOST; O60229; -.
DR MassIVE; O60229; -.
DR MaxQB; O60229; -.
DR PaxDb; O60229; -.
DR PeptideAtlas; O60229; -.
DR PRIDE; O60229; -.
DR ProteomicsDB; 11196; -.
DR ProteomicsDB; 49252; -. [O60229-1]
DR ProteomicsDB; 49253; -. [O60229-2]
DR ProteomicsDB; 49255; -. [O60229-4]
DR ProteomicsDB; 49256; -. [O60229-5]
DR ProteomicsDB; 49257; -. [O60229-6]
DR Antibodypedia; 2142; 177 antibodies from 33 providers.
DR DNASU; 8997; -.
DR Ensembl; ENST00000240874.7; ENSP00000240874.3; ENSG00000160145.16. [O60229-2]
DR Ensembl; ENST00000291478.9; ENSP00000291478.4; ENSG00000160145.16. [O60229-4]
DR Ensembl; ENST00000360013.7; ENSP00000353109.3; ENSG00000160145.16. [O60229-1]
DR GeneID; 8997; -.
DR KEGG; hsa:8997; -.
DR UCSC; uc003ehf.2; human. [O60229-1]
DR CTD; 8997; -.
DR DisGeNET; 8997; -.
DR GeneCards; KALRN; -.
DR HGNC; HGNC:4814; KALRN.
DR HPA; ENSG00000160145; Tissue enhanced (brain).
DR MalaCards; KALRN; -.
DR MIM; 604605; gene.
DR neXtProt; NX_O60229; -.
DR OpenTargets; ENSG00000160145; -.
DR PharmGKB; PA29189; -.
DR VEuPathDB; HostDB:ENSG00000160145; -.
DR eggNOG; KOG4240; Eukaryota.
DR GeneTree; ENSGT00940000155248; -.
DR HOGENOM; CLU_000373_0_1_1; -.
DR InParanoid; O60229; -.
DR OMA; AKXFIMA; -.
DR OrthoDB; 5761at2759; -.
DR PhylomeDB; O60229; -.
DR TreeFam; TF318080; -.
DR PathwayCommons; O60229; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; O60229; -.
DR SIGNOR; O60229; -.
DR BioGRID-ORCS; 8997; 10 hits in 1108 CRISPR screens.
DR ChiTaRS; KALRN; human.
DR GeneWiki; Kalirin; -.
DR GenomeRNAi; 8997; -.
DR Pharos; O60229; Tbio.
DR PRO; PR:O60229; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O60229; protein.
DR Bgee; ENSG00000160145; Expressed in secondary oocyte and 165 other tissues.
DR ExpressionAtlas; O60229; baseline and differential.
DR Genevisible; O60229; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:HGNC-UCL.
DR GO; GO:0007399; P:nervous system development; ISS:HGNC-UCL.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 4.
DR Gene3D; 1.20.900.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR028570; Kalirin/TRIO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF104; PTHR22826:SF104; 2.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 7.
DR SUPFAM; SSF48065; SSF48065; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Guanine-nucleotide releasing factor; Immunoglobulin domain;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; SH3 domain;
KW Transferase.
FT CHAIN 1..2986
FT /note="Kalirin"
FT /id="PRO_0000080955"
FT DOMAIN 35..180
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REPEAT 167..308
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 310..417
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 418..535
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 536..639
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 640..770
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 771..888
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 889..1004
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1005..1128
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1129..1234
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 1281..1456
FT /note="DH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1468..1580
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1646..1711
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1929..2104
FT /note="DH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 2116..2226
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 2321..2386
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 2471..2564
FT /note="Ig-like C2-type"
FT DOMAIN 2571..2665
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2684..2938
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 710..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2244..2310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2412..2454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2412..2434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2803
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 2690..2698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 1750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 1753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 1799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1812
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97924"
FT MOD_RES 1817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT MOD_RES 1913
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2CG49"
FT MOD_RES 2262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087"
FT DISULFID 2492..2548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..1697
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10023074"
FT /id="VSP_028903"
FT VAR_SEQ 1..1627
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_028904"
FT VAR_SEQ 1628..1643
FT /note="ISIASRTSQNTVDSDK -> MLKWISWRQSKANKAQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_028909"
FT VAR_SEQ 1644..1663
FT /note="LSGGCELTVVLQDFSAGHSS -> DGNLVPRWHLGPGDPFSTYV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9285789"
FT /id="VSP_028910"
FT VAR_SEQ 1664..2986
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9285789"
FT /id="VSP_028911"
FT VAR_SEQ 1698..1725
FT /note="EGLVPSSALCISHSRSSVEMDCFFPLVK -> MKGGDRAYTRGPSLGWLFAK
FT CCCCFPCR (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10023074"
FT /id="VSP_028912"
FT VAR_SEQ 1857..1888
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_028913"
FT VAR_SEQ 2314
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_028914"
FT VAR_SEQ 2399..2986
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_028915"
FT VARIANT 196
FT /note="S -> L"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041898"
FT VARIANT 213
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1187034389)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035976"
FT VARIANT 1326
FT /note="E -> D (in dbSNP:rs2289838)"
FT /id="VAR_020192"
FT VARIANT 1897
FT /note="S -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035625"
FT VARIANT 1930
FT /note="R -> M (in dbSNP:rs35298864)"
FT /id="VAR_057190"
FT MUTAGEN 2713
FT /note="K->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:10023074"
FT CONFLICT 2459
FT /note="E -> G (in Ref. 2; BAA76314)"
FT /evidence="ECO:0000305"
FT HELIX 1281..1305
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1307..1313
FT /evidence="ECO:0007829|PDB:5QQJ"
FT STRAND 1314..1316
FT /evidence="ECO:0007829|PDB:5QQJ"
FT TURN 1320..1324
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1326..1330
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1333..1342
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1344..1350
FT /evidence="ECO:0007829|PDB:5QQJ"
FT TURN 1351..1353
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1355..1358
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1359..1364
FT /evidence="ECO:0007829|PDB:5QQJ"
FT TURN 1365..1367
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1368..1370
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1371..1389
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1393..1401
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1407..1429
FT /evidence="ECO:0007829|PDB:5QQJ"
FT HELIX 1437..1455
FT /evidence="ECO:0007829|PDB:5QQJ"
SQ SEQUENCE 2986 AA; 340261 MW; EA7B559A9E4AFFA0 CRC64;
MTDRFWDQWY LWYLRLLRLL DRGSFRNDGL KASDVLPILK EKVAFVSGGR DKRGGPILTF
PARSNHDRIR QEDLRKLVTY LASVPSEDVC KRGFTVIIDM RGSKWDLIKP LLKTLQEAFP
AEIHVALIIK PDNFWQKQKT NFGSSKFIFE TSMVSVEGLT KLVDPSQLTE EFDGSLDYNH
EEWIELRLSL EEFFNSAVHL LSRLEDLQEM LARKEFPVDV EGSRRLIDEH TQLKKKVLKA
PVEELDREGQ RLLQCIRCSD GFSGRNCIPG SADFQSLVPK ITSLLDKLHS TRQHLHQMWH
VRKLKLDQCF QLRLFEQDAE KMFDWISHNK ELFLQSHTEI GVSYQYALDL QTQHNHFAMN
SMNAYVNINR IMSVASRLSE AGHYASQQIK QISTQLDQEW KSFAAALDER STILAMSAVF
HQKAEQFLSG VDAWCKMCSE GGLPSEMQDL ELAIHHHQTL YEQVTQAYTE VSQDGKALLD
VLQRPLSPGN SESLTATANY SKAVHQVLDV VHEVLHHQRR LESIWQHRKV RLHQRLQLCV
FQQDVQQVLD WIENHGEAFL SKHTGVGKSL HRARALQKRH DDFEEVAQNT YTNADKLLEA
AEQLAQTGEC DPEEIYKAAR HLEVRIQDFV RRVEQRKLLL DMSVSFHTHT KELWTWMEDL
QKEMLEDVCA DSVDAVQELI KQFQQQQTAT LDATLNVIKE GEDLIQQLRS APPSLGEPSE
ARDSAVSNNK TPHSSSISHI ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE
VTAELDAWNE DLLRQMNDFN TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIT
EVQASGIELI CEKDIDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK
QVLGWIRNGE SMLNASLVNA SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ KTHQSALQVQ
QKAEVLLQAG HYDADAIREC AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE
SLEQEYRRDE DWCGGRDKLG PAAEIDHVIP LISKHLEQKE AFLKACTLAR RNAEVFLKYI
HRNNVSMPSV ASHTRGPEQQ VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK
QALDWIQETG EFYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE
KGHIHATEIR KWVTTVDKHY RDFSLRMGKY RYSLEKALGV NTEDNKDLEL DIIPASLSDR
EVKLRDANHE VNEEKRKSAR KKEFIMAELL QTEKAYVRDL HECLETYLWE MTSGVEEIPP
GILNKEHIIF GNIQEIYDFH NNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP
DSNQLILEHA GTFFDEIQQR HGLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGELK
DGLEVMLSVP KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI RKGRERHLFL
FEISLVFSKE IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR TPSSDNKTVL
KASNIETKQE WIKNIREVIQ ERIIHLKGAL KEPLQLPKTP AKQRNNSKRD GVEDIDSQGD
GSSQPDTISI ASRTSQNTVD SDKLSGGCEL TVVLQDFSAG HSSELTIQVG QTVELLERPS
ERPGWCLVRT TERSPPLEGL VPSSALCISH SRSSVEMDCF FPLVKDAYSH SSSENGGKSE
SVANLQAQPS LNSIHSSPGP KRSTNTLKKW LTSPVRRLNS GKADGNIKKQ KKVRDGRKSF
DLGSPKPGDE TTPQGDSADE KSKKGWGEDE PDEESHTPLP PPMKIFDNDP TQDEMSSSLL
AARQASTEVP TAADLVNAIE KLVKNKLSLE GSSYRGSLKD PAGCLNEGMA PPTPPKNPEE
EQKAKALRGR MFVLNELVQT EKDYVKDLGI VVEGFMKRIE EKGVPEDMRG KDKIVFGNIH
QIYDWHKDFF LAELEKCIQE QDRLAQLFIK HERKLHIYVW YCQNKPRSEY IVAEYDAYFE
EVKQEINQRL TLSDFLIKPI QRITKYQLLL KDFLRYSEKA GLECSDIEKA VELMCLVPKR
CNDMMNLGRL QGFEGTLTAQ GKLLQQDTFY VIELDAGMQS RTKERRVFLF EQIVIFSELL
RKGSLTPGYM FKRSIKMNYL VLEENVDNDP CKFALMNRET SERVVLQAAN ADIQQAWVQD
INQVLETQRD FLNALQSPIE YQRKERSTAV MRSQPARLPQ ASPRPYSSVP AGSEKPPKGS
SYNPPLPPLK ISTSNGSPGF EYHQPGDKFE ASKQNDLGGC NGTSSMAVIK DYYALKENEI
CVSQGEVVQV LAVNQQNMCL VYQPASDHSP AAEGWVPGSI LAPLTKATAA ESSDGSIKKS
CSWHTLRMRK RAEVENTGKN EATGPRKPKD ILGNKVSVKE TNSSEESECD DLDPNTSMEI
LNPNFIQEVA PEFLVPLVDV TCLLGDTVIL QCKVCGRPKP TITWKGPDQN ILDTDNSSAT
YTVSSCDSGE ITLKICNLMP QDSGIYTCIA TNDHGTTSTS ATVKVQGVPA APNRPIAQER
SCTSVILRWL PPSSTGNCTI SGYTVEYREE GSQIWQQSVA STLDTYLVIE DLSPGCPYQF
RVSASNPWGI SLPSEPSEFV RLPEYDAAAD GATISWKENF DSAYTELNEI GRGRFSIVKK
CIHKATRKDV AVKFVSKKMK KKEQAAHEAA LLQHLQHPQY ITLHDTYESP TSYILILELM
DDGRLLDYLM NHDELMEEKV AFYIRDIMEA LQYLHNCRVA HLDIKPENLL IDLRIPVPRV
KLIDLEDAVQ ISGHFHIHHL LGNPEFAAPE VIQGIPVSLG TDIWSIGVLT YVMLSGVSPF
LDESKEETCI NVCRVDFSFP HEYFCGVSNA ARDFINVILQ EDFRRRPTAA TCLQHPWLQP
HNGSYSKIPL DTSRLACFIE RRKHQNDVRP IPNVKSYIVN RVNQGT
