KALRN_MOUSE
ID KALRN_MOUSE Reviewed; 2964 AA.
AC A2CG49; A2CG50; A2CG51; A2CG52; A2CG53; B2RXR5; D3Z559; Q3TXY8; Q3TYL1;
AC Q3UTA5; Q8BTT9; Q8C4Q2; Q9CVA9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Kalirin {ECO:0000250|UniProtKB:P97924};
DE EC=2.7.11.1;
DE AltName: Full=Protein Duo;
DE AltName: Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain;
GN Name=Kalrn {ECO:0000312|MGI:MGI:2685385};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB25925.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2108-2964 (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB25925.1}, and
RC NOD {ECO:0000312|EMBL:BAC40535.1};
RC TISSUE=Egg {ECO:0000312|EMBL:BAE24075.1},
RC Embryonic head {ECO:0000312|EMBL:BAC38239.1},
RC Stomach {ECO:0000312|EMBL:BAB25925.1},
RC Thymus {ECO:0000312|EMBL:BAC40535.1}, and
RC Visual cortex {ECO:0000312|EMBL:BAE34552.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC TISSUE=Brain;
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 [4] {ECO:0000312|EMBL:CAM18305.1}
RP PROTEIN SEQUENCE OF 2034-2042, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1722 AND SER-1771, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1722; SER-1771; SER-1789;
RP THR-1881 AND THR-1884, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250|UniProtKB:P97924}.
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 Evidence={ECO:0000250|UniProtKB:O60229};
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; Evidence={ECO:0000250|UniProtKB:O60229};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O60229};
CC -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha-
CC amidating monooxygenase (PAM) and with the huntingtin-associated
CC protein 1 (HAP1). Interacts with FASLG (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60229,
CC ECO:0000250|UniProtKB:P97924}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=10;
CC Name=1; Synonyms=Kalirin-12A {ECO:0000250|UniProtKB:P97924};
CC IsoId=A2CG49-1; Sequence=Displayed;
CC Name=2; Synonyms=Kalirin-9A {ECO:0000250|UniProtKB:P97924};
CC IsoId=A2CG49-2; Sequence=VSP_052576, VSP_052579;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=A2CG49-3; Sequence=VSP_052562;
CC Name=4 {ECO:0000269|PubMed:16141072};
CC IsoId=A2CG49-4; Sequence=VSP_052563, VSP_052570, VSP_052571,
CC VSP_052573, VSP_052577, VSP_052578;
CC Name=5 {ECO:0000269|PubMed:16141072};
CC IsoId=A2CG49-5; Sequence=VSP_052564, VSP_052567, VSP_052568,
CC VSP_052569;
CC Name=6 {ECO:0000269|PubMed:16141072};
CC IsoId=A2CG49-6; Sequence=VSP_052563, VSP_052570, VSP_052573,
CC VSP_052574, VSP_052575;
CC Name=7 {ECO:0000269|PubMed:16141072};
CC IsoId=A2CG49-7; Sequence=VSP_052565, VSP_052572;
CC Name=8 {ECO:0000269|PubMed:16141072};
CC IsoId=A2CG49-8; Sequence=VSP_052566, VSP_052567, VSP_052568,
CC VSP_052569;
CC Name=9 {ECO:0000269|PubMed:16141072}; Synonyms=Kalirin-7c
CC {ECO:0000250|UniProtKB:P97924};
CC IsoId=A2CG49-9; Sequence=VSP_052566, VSP_052568, VSP_052569;
CC Name=10; Synonyms=Delta Kalirin-7 {ECO:0000250|UniProtKB:P97924};
CC IsoId=A2CG49-10; Sequence=VSP_052564, VSP_052568, VSP_052569;
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).
CC {ECO:0000250|UniProtKB:P97924}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O60229}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative initiation at Met-
CC 624 of isoform 1. Inferred by similarity. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AK008844; BAB25925.1; -; mRNA.
DR EMBL; AK081504; BAC38239.1; -; mRNA.
DR EMBL; AK088732; BAC40535.1; -; mRNA.
DR EMBL; AK139581; BAE24075.1; -; mRNA.
DR EMBL; AK158544; BAE34552.1; -; mRNA.
DR EMBL; AK159031; BAE34776.1; -; mRNA.
DR EMBL; CT010573; CAM18305.1; -; Genomic_DNA.
DR EMBL; AC154524; CAM18305.1; JOINED; Genomic_DNA.
DR EMBL; AC155257; CAM18305.1; JOINED; Genomic_DNA.
DR EMBL; AC165079; CAM18305.1; JOINED; Genomic_DNA.
DR EMBL; CT010573; CAM18306.1; -; Genomic_DNA.
DR EMBL; AC154524; CAM18306.1; JOINED; Genomic_DNA.
DR EMBL; AC165079; CAM18306.1; JOINED; Genomic_DNA.
DR EMBL; CT010573; CAM18307.1; -; Genomic_DNA.
DR EMBL; AC154524; CAM18307.1; JOINED; Genomic_DNA.
DR EMBL; AC154588; CAM18307.1; JOINED; Genomic_DNA.
DR EMBL; CT010573; CAM18308.1; -; Genomic_DNA.
DR EMBL; AC154524; CAM18308.1; JOINED; Genomic_DNA.
DR EMBL; AC154588; CAM18308.1; JOINED; Genomic_DNA.
DR EMBL; CT010573; CAM18309.1; -; Genomic_DNA.
DR EMBL; AC154524; CAM18309.1; JOINED; Genomic_DNA.
DR EMBL; AC154588; CAM18309.1; JOINED; Genomic_DNA.
DR EMBL; BC157950; AAI57951.1; -; mRNA.
DR EMBL; BC172101; AAI72101.1; -; mRNA.
DR CCDS; CCDS49836.1; -. [A2CG49-9]
DR RefSeq; NP_001157740.1; NM_001164268.1. [A2CG49-9]
DR RefSeq; XP_006522445.1; XM_006522382.3. [A2CG49-8]
DR PDB; 1WFW; NMR; -; A=2295-2354.
DR PDBsum; 1WFW; -.
DR SMR; A2CG49; -.
DR BioGRID; 244011; 61.
DR IntAct; A2CG49; 61.
DR MINT; A2CG49; -.
DR STRING; 10090.ENSMUSP00000110611; -.
DR iPTMnet; A2CG49; -.
DR PhosphoSitePlus; A2CG49; -.
DR SwissPalm; A2CG49; -.
DR MaxQB; A2CG49; -.
DR PaxDb; A2CG49; -.
DR PeptideAtlas; A2CG49; -.
DR PRIDE; A2CG49; -.
DR ProteomicsDB; 301718; -. [A2CG49-1]
DR ProteomicsDB; 301719; -. [A2CG49-2]
DR ProteomicsDB; 301720; -. [A2CG49-3]
DR ProteomicsDB; 301721; -. [A2CG49-4]
DR ProteomicsDB; 301722; -. [A2CG49-5]
DR ProteomicsDB; 301723; -. [A2CG49-6]
DR ProteomicsDB; 301724; -. [A2CG49-7]
DR ProteomicsDB; 301725; -. [A2CG49-8]
DR ProteomicsDB; 301726; -. [A2CG49-9]
DR ProteomicsDB; 301727; -. [A2CG49-10]
DR Antibodypedia; 2142; 177 antibodies from 33 providers.
DR DNASU; 545156; -.
DR Ensembl; ENSMUST00000076810; ENSMUSP00000076088; ENSMUSG00000061751. [A2CG49-1]
DR Ensembl; ENSMUST00000089655; ENSMUSP00000087084; ENSMUSG00000061751. [A2CG49-8]
DR Ensembl; ENSMUST00000114949; ENSMUSP00000110599; ENSMUSG00000061751. [A2CG49-10]
DR Ensembl; ENSMUST00000114953; ENSMUSP00000110603; ENSMUSG00000061751. [A2CG49-5]
DR Ensembl; ENSMUST00000114954; ENSMUSP00000110604; ENSMUSG00000061751. [A2CG49-5]
DR Ensembl; ENSMUST00000114960; ENSMUSP00000110611; ENSMUSG00000061751. [A2CG49-9]
DR Ensembl; ENSMUST00000232157; ENSMUSP00000156147; ENSMUSG00000061751. [A2CG49-4]
DR GeneID; 545156; -.
DR KEGG; mmu:545156; -.
DR UCSC; uc007zar.2; mouse. [A2CG49-3]
DR UCSC; uc007zas.1; mouse. [A2CG49-6]
DR UCSC; uc007zat.1; mouse. [A2CG49-4]
DR UCSC; uc007zav.1; mouse. [A2CG49-5]
DR UCSC; uc007zax.2; mouse. [A2CG49-9]
DR UCSC; uc012aew.1; mouse. [A2CG49-1]
DR CTD; 8997; -.
DR MGI; MGI:2685385; Kalrn.
DR VEuPathDB; HostDB:ENSMUSG00000061751; -.
DR eggNOG; KOG4240; Eukaryota.
DR GeneTree; ENSGT00940000155248; -.
DR InParanoid; A2CG49; -.
DR OMA; AKXFIMA; -.
DR OrthoDB; 5761at2759; -.
DR PhylomeDB; A2CG49; -.
DR TreeFam; TF318080; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 545156; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Kalrn; mouse.
DR EvolutionaryTrace; A2CG49; -.
DR PRO; PR:A2CG49; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; A2CG49; protein.
DR Bgee; ENSMUSG00000061751; Expressed in cingulate cortex and 246 other tissues.
DR ExpressionAtlas; A2CG49; baseline and differential.
DR Genevisible; A2CG49; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
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; IEA:UniProtKB-KW.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0046959; P:habituation; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0042711; P:maternal behavior; IMP:MGI.
DR GO; GO:0060137; P:maternal process involved in parturition; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0060125; P:negative regulation of growth hormone secretion; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0050773; P:regulation of dendrite development; ISO:MGI.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 5.
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; IPR036179; Ig-like_dom_sf.
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; PF00018; SH3_1; 1.
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; SSF48726; SSF48726; 1.
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 initiation; Alternative splicing; ATP-binding;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond;
KW Guanine-nucleotide releasing factor; Immunoglobulin domain; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; SH3 domain;
KW Transferase.
FT CHAIN 1..2964
FT /note="Kalirin"
FT /id="PRO_0000308173"
FT DOMAIN 17..162
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REPEAT 149..290
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 292..399
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 400..517
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 518..621
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 622..752
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 753..870
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 871..977
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 978..1101
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1102..1207
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 1254..1429
FT /note="DH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1441..1553
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1619..1684
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1900..2075
FT /note="DH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 2087..2197
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 2292..2357
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 2443..2536
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT DOMAIN 2543..2637
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2656..2910
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 692..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2215..2285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2384..2426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2257..2271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2384..2406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2775
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 2662..2670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O60229,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60229"
FT MOD_RES 1771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1784
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97924"
FT MOD_RES 1789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1881
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1884
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60229"
FT DISULFID 2464..2520
FT /evidence="ECO:0000250|UniProtKB:O60229,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..2731
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052562"
FT VAR_SEQ 1..1669
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052563"
FT VAR_SEQ 1..623
FT /note="Missing (in isoform 5 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052564"
FT VAR_SEQ 1..4
FT /note="MVLS -> MNPPEGASEEGGAADSDVDAFFRT (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052565"
FT VAR_SEQ 1..4
FT /note="MVLS -> MTDRFWDQWYLWYLRLLRLLDR (in isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052566"
FT VAR_SEQ 923
FT /note="E -> ESLFHATSLQ (in isoform 5 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052567"
FT VAR_SEQ 1617..1636
FT /note="LSGGCELTVVLQDFSAGHSS -> DGNLVPRWHLGPGDPFSTYV (in
FT isoform 5, isoform 8, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052568"
FT VAR_SEQ 1637..2964
FT /note="Missing (in isoform 5, isoform 8, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052569"
FT VAR_SEQ 1670..1697
FT /note="QEGLVPSSALCISHSRSSVEMDCFFPLK -> MKGGDQAYTRGPSLGWLFAK
FT CCCCFPCR (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052570"
FT VAR_SEQ 1828..1858
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052571"
FT VAR_SEQ 1859..1898
FT /note="TLEGGSYRGSLKDPTGCLNEGMTPPTPPRNLEEEQKAKAL -> VSGHAGGS
FT SELPLTSVWLPGPQPGPRTGLPHPNFTNRNCI (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052572"
FT VAR_SEQ 2285
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052573"
FT VAR_SEQ 2357..2364
FT /note="KATAAAES -> QSQSRGRK (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052574"
FT VAR_SEQ 2365..2964
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052575"
FT VAR_SEQ 2371..2375
FT /note="KSCSW -> TLLKP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052576"
FT VAR_SEQ 2372..2374
FT /note="SCS -> EPY (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052577"
FT VAR_SEQ 2375..2964
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052578"
FT VAR_SEQ 2376..2964
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052579"
FT CONFLICT 1824
FT /note="Q -> H (in Ref. 1; BAC40535)"
FT /evidence="ECO:0000305"
FT CONFLICT 2316
FT /note="G -> S (in Ref. 1; BAB25925)"
FT /evidence="ECO:0000305"
FT CONFLICT 2344
FT /note="E -> K (in Ref. 1; BAB25925)"
FT /evidence="ECO:0000305"
FT CONFLICT 2355
FT /note="L -> F (in Ref. 1; BAB25925)"
FT /evidence="ECO:0000305"
FT STRAND 2296..2298
FT /evidence="ECO:0007829|PDB:1WFW"
FT STRAND 2307..2309
FT /evidence="ECO:0007829|PDB:1WFW"
FT STRAND 2318..2324
FT /evidence="ECO:0007829|PDB:1WFW"
FT STRAND 2328..2334
FT /evidence="ECO:0007829|PDB:1WFW"
FT STRAND 2338..2348
FT /evidence="ECO:0007829|PDB:1WFW"
FT HELIX 2349..2351
FT /evidence="ECO:0007829|PDB:1WFW"
FT CONFLICT A2CG49-5:711
FT /note="E -> K (in Ref. 1; BAE34776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2964 AA; 337000 MW; 76064FE06AA2BD9C CRC64;
MVLSGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL TFPARSNHDR IRQEDLRKLV
TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA FPAEIHVALI IKPDNFWQKQ
KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY NHEEWIELRL SLEEFFNSAV
HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVL KAPVEELDRE GQRLLQCIRC
SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM WHVRKLKLDQ CFQLRLFEQD
AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA MNSMNAYVNI NRIMSVASRL
SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA VFHQKAEQFL SGVDAWCKMC
SEGGLPSEMQ DLELAIHHHQ SLYEQVTQAY TEVSQDGKAL LDVLQRPLSP GNSESLTATA
NYSKAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL CVFQQDVQQV LDWIENHGEA
FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL EAAEQLAQTG ECDPEEIYKA
ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME DLQKEVLEDV CADSVDAVQE
LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP TEARDSAMSN NKTPHSSSIS
HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT IEVTAELDAW NEDLLRQMND
FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY IMEVQASGIE LICEKDLDLA
AQVQELLEFL HEKQHELELN AEQTHKRLEQ CLQLRHLQAE VKQVLGWIRN GESMLNASLV
NASSLSEAEQ LQREHEQFQL AIEKTHQSAL QVQQKAEALL QAGHYDADAI RECAEKVALH
WQQLMLKMED RLKLVNASVA FYKTSEQVCS VLESLEQEYR RDEDWCGGRD KLGPAAEMDH
VIPLLSKHLE QKEAFLKACT LARRNAEVFL KYIHRNNVSM PSVASHTRGP EQQVKAILSE
LLQRENRVLH FWTLKKRRLD QCQQYVVFER SAKQALDWIQ ETGEYYLSTH TSTGETTEET
QELLKEYGEF RVPAKQTKEK VKLLIQLADS FVEKGHIHAT EIRKWVTTVD KHYRDFSLRM
GKYRYSLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA NHEINEEKRK SARKKEFIMA
ELLQTEKAYV RDLHECLETY LWEMTSGVEE IPPGILNKEH IIFGNIQEIY DFHNNIFLKE
LEKYEQLPED VGHCFVTWAD KFQMYVTYCK NKPDSNQLIL EHAGTFFDEI QQRHGLANSI
SSYLIKPVQR VTKYQLLLKE LLTCCEEGKG ELKDGLEVML SVPKKANDAM HVSMLEGFDE
NLDVQGELIL QDAFQVWDPK SLIRKGRERH LFLFEISLVF SKEIKDSSGH TKYVYKNKLL
TSELGVTEHV EGDPCKFALW SGRTPSSDNK TVLKASNIET KQEWIKNIRE VIQERIIHLK
GALKEPIQLP KTPAKLRNNS KRDGVEDGDS QGDGSSQPDT ISIASRTSQN TVESDKLSGG
CELTVVLQDF SAGHSSELSI QVGQTVELLE RPSERPGWCL VRTTERSPPQ EGLVPSSALC
ISHSRSSVEM DCFFPLKDSY SHSSSENGGK SESVAHLQSQ PSLNSIHSSP GPKRSTNTLK
KWLTSPVRRL NSGKADGNIK KQKKVRDGRK SFDLGSPKPG DETTPQGDSA DEKSKKGWGE
DEPDEESHTP LPPPMKIFDN DPTQDEMSSL LAARQAPPDV PTAADLVSAI EKLVKNKLTL
EGGSYRGSLK DPTGCLNEGM TPPTPPRNLE EEQKAKALRG RMFVLNELVQ TEKDYVKDLG
IVVEGFMKRI EEKGVPEDMR GKEKIVFGNI HQIYDWHKDF FLAELEKCIQ EQDRLAQLFI
KHERKLHIYV WYCQNKPRSE YIVAEYDAYF EEVKQEINQR LTLSDFLIKP IQRITKYQLL
LKDFLRYSEK AGLECSDIEK AVELMCLVPK RCNDMMNLGR LQGFEGTLTA QGKLLQQDTF
YVIELDAGMQ SRTKERRVFL FEQIVIFSEL LRKGSLTPGY MFKRSIKMNY LVLEDNVDGD
PCKFALMNRE TSERVILQAA NSDIQQAWVQ DINQVLETQR DFLNALQSPI EYQRKERSTA
VIRSQPPRVP QASPRPYSSG PVGSEKPPKG SSYNPPLPPL KISTSNGSPG FDYHQPGDKF
DASKQNDLGG CNGTSTMTVI KDYYALKENE ICVSQGEVVQ VLAVNQQNMC LVYQPASDHS
PAAEGWVPGS ILAPLAKATA AAESSDGSIK KSCSWHTLRM RKRADVENSG KNEATGPRKP
KDILGNKVSV KETNSSEESE CDDLDPNTSM EILNPNFIQE VAPEFLVPLV DVTCLLGDTV
LLQCKACGRP KPSITWKGPD QNILDTDNSS ATYTISSCDS GESTLKICNL MPQDSGIYTC
IAANDHGTAS TSATVKVQGV PAAPNRPIAQ ERSCTSVILR WLPPASTGNC TISGYTVEYR
EEGSQVWQQS VASTLDTYLV IEDLSPGCPY QFRVSASNPW GISLPSEPSE FVRLPEYDAA
ADGATISWKE NFDSAYTELN EIGRGRFSIV KKCIHKATRK DVAVKFVSKK MKKKEQAAHE
AALLQHLQHP QYVTLHDTYE SPTSYILILE LMDDGRLLDY LMNHDELMEE KVAFYIRDIM
EALQYLHNCR VAHLDIKPEN LLIDLRIPVP RVKLIDLEDA VQISGHFHIH HLLGNPEFAA
PEVIQGIPVS LGTDIWSIGV LTYVMLSGVS PFLDESKEET CINVCRVDFS FPHEYFCGVS
NAARDFINVI LQEDFRRRPT AATCLQHPWL QPHNGSYSKI PLDTSRLACF IERRKHQNDV
RPIPNVKSYI VNRVNQGTSL SHNP
