CATE_HUMAN
ID CATE_HUMAN Reviewed; 396 AA.
AC P14091; Q5TZ01; Q5TZ02; Q9NY58; Q9UCE3; Q9UCE4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Cathepsin E;
DE EC=3.4.23.34;
DE Contains:
DE RecName: Full=Cathepsin E form I;
DE Contains:
DE RecName: Full=Cathepsin E form II;
DE Flags: Precursor;
GN Name=CTSE;
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 1).
RC TISSUE=Gastric mucosa;
RX PubMed=2674141; DOI=10.1016/s0021-9258(19)84768-3;
RA Azuma T., Pals G., Mohandas T.K., Couvreur J.M., Taggart R.T.;
RT "Human gastric cathepsin E. Predicted sequence, localization to chromosome
RT 1, and sequence homology with other aspartic proteinases.";
RL J. Biol. Chem. 264:16748-16753(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=1370478; DOI=10.1016/s0021-9258(18)45989-3;
RA Azuma T., Liu W.G., Vander Laan D.J., Bowcock A.M., Taggart R.T.;
RT "Human gastric cathepsin E gene. Multiple transcripts result from
RT alternative polyadenylation of the primary transcripts of a single gene
RT locus at 1q31-q32.";
RL J. Biol. Chem. 267:1609-1614(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RC TISSUE=Intestine;
RX PubMed=7983070; DOI=10.1016/s0021-9258(18)47417-0;
RA Finley E.M., Kornfeld S.;
RT "Subcellular localization and targeting of cathepsin E.";
RL J. Biol. Chem. 269:31259-31266(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=12531480; DOI=10.1016/s0167-4781(02)00595-x;
RA Tatnell P.J., Cook M., Kay J.;
RT "An alternatively spliced variant of cathepsin E in human gastric
RT adenocarcinoma cells.";
RL Biochim. Biophys. Acta 1625:203-206(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP PROTEIN SEQUENCE OF 20-38 AND 54-76, BIOPHYSICOCHEMICAL PROPERTIES,
RP AUTOCATALYTIC CLEAVAGE, AND GLYCOSYLATION.
RC TISSUE=Erythrocyte;
RX PubMed=8346912; DOI=10.1006/abbi.1993.1361;
RA Takeda-Ezaki M., Yamamoto K.;
RT "Isolation and biochemical characterization of procathepsin E from human
RT erythrocyte membranes.";
RL Arch. Biochem. Biophys. 304:352-358(1993).
RN [10]
RP PROTEIN SEQUENCE OF 54-68; 77-95; 141-154; 275-285 AND 389-396, AND
RP GLYCOSYLATION.
RC TISSUE=Gastric mucosa;
RX PubMed=2334440; DOI=10.1016/0006-291x(90)92403-m;
RA Athauda S.B.P., Matsuzaki O., Kgeyama T., Takahashi K.;
RT "Structural evidence for two isozymic forms and the carbohydrate attachment
RT site of human gastric cathepsin E.";
RL Biochem. Biophys. Res. Commun. 168:878-885(1990).
RN [11]
RP CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-60.
RX PubMed=7789521; DOI=10.1016/0014-5793(95)00501-y;
RA Fowler S.D., Kay J., Dunn B.M., Tatnell P.J.;
RT "Monomeric human cathepsin E.";
RL FEBS Lett. 366:72-74(1995).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=8765029; DOI=10.1002/eji.1830260826;
RA Sealy L., Mota F., Rayment N., Tatnell P.J., Kay J., Chain B.;
RT "Regulation of cathepsin E expression during human B cell differentiation
RT in vitro.";
RL Eur. J. Immunol. 26:1838-1843(1996).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=11322887; DOI=10.1046/j.1432-1327.2001.02159.x;
RA Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.;
RT "Regulation of human and mouse procathepsin E gene expression.";
RL Eur. J. Biochem. 268:2658-2668(2001).
CC -!- FUNCTION: May have a role in immune function. Probably involved in the
CC processing of antigenic peptides during MHC class II-mediated antigen
CC presentation. May play a role in activation-induced lymphocyte
CC depletion in the thymus, and in neuronal degeneration and glial cell
CC activation in the brain. {ECO:0000269|PubMed:8765029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to cathepsin D, but slightly broader specificity.;
CC EC=3.4.23.34; Evidence={ECO:0000269|PubMed:7789521,
CC ECO:0000269|PubMed:8765029};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for hemoglobin {ECO:0000269|PubMed:8346912};
CC KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu
CC {ECO:0000269|PubMed:8346912};
CC KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu
CC {ECO:0000269|PubMed:8346912};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:7789521}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:7983070}. Note=The
CC proenzyme is localized to the endoplasmic reticulum and Golgi
CC apparatus, while the mature enzyme is localized to the endosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P14091-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P14091-2; Sequence=VSP_059426;
CC Name=3;
CC IsoId=P14091-3; Sequence=VSP_059425;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the stomach, the Clara
CC cells of the lung and activated B-lymphocytes, and at lower levels in
CC lymph nodes, skin and spleen. Not expressed in resting B-lymphocytes.
CC {ECO:0000269|PubMed:11322887, ECO:0000269|PubMed:1370478,
CC ECO:0000269|PubMed:8765029}.
CC -!- PTM: Glycosylated. The nature of the carbohydrate chain varies between
CC cell types. In fibroblasts, the proenzyme contains a high mannose-type
CC oligosaccharide, while the mature enzyme contains a complex-type
CC oligosaccharide. In erythrocyte membranes, both the proenzyme and
CC mature enzyme contain a complex-type oligosaccharide.
CC {ECO:0000269|PubMed:2334440, ECO:0000269|PubMed:7983070,
CC ECO:0000269|PubMed:8346912}.
CC -!- PTM: Two forms are produced by autocatalytic cleavage, form I begins at
CC Ile-54, form II begins at Thr-57.
CC -!- MISCELLANEOUS: [Isoform 3]: Dubious isoform produced through aberrant
CC splice sites. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; J05036; AAA52130.1; -; mRNA.
DR EMBL; M84424; AAA52300.1; -; Genomic_DNA.
DR EMBL; M84413; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84417; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84418; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84419; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84420; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84421; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; M84422; AAA52300.1; JOINED; Genomic_DNA.
DR EMBL; AJ250716; CAB82849.1; -; mRNA.
DR EMBL; AJ250717; CAB82850.1; -; mRNA.
DR EMBL; AK292057; BAF84746.1; -; mRNA.
DR EMBL; BX571818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91592.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91593.1; -; Genomic_DNA.
DR EMBL; BC042537; AAH42537.1; -; mRNA.
DR CCDS; CCDS73012.1; -. [P14091-2]
DR CCDS; CCDS73013.1; -. [P14091-1]
DR PIR; A42038; A34401.
DR RefSeq; NP_001304260.1; NM_001317331.1.
DR RefSeq; NP_001901.1; NM_001910.3. [P14091-1]
DR RefSeq; NP_683865.1; NM_148964.2. [P14091-2]
DR PDB; 1TZS; X-ray; 2.35 A; A=54-396, P=19-53.
DR PDBsum; 1TZS; -.
DR AlphaFoldDB; P14091; -.
DR SMR; P14091; -.
DR BioGRID; 107890; 12.
DR IntAct; P14091; 9.
DR STRING; 9606.ENSP00000350911; -.
DR BindingDB; P14091; -.
DR ChEMBL; CHEMBL3092; -.
DR DrugCentral; P14091; -.
DR GuidetoPHARMACOLOGY; 2346; -.
DR MEROPS; A01.010; -.
DR GlyGen; P14091; 1 site.
DR iPTMnet; P14091; -.
DR PhosphoSitePlus; P14091; -.
DR BioMuta; CTSE; -.
DR DMDM; 46397366; -.
DR jPOST; P14091; -.
DR MassIVE; P14091; -.
DR PaxDb; P14091; -.
DR PeptideAtlas; P14091; -.
DR PRIDE; P14091; -.
DR ProteomicsDB; 53019; -. [P14091-3]
DR ProteomicsDB; 53020; -. [P14091-1]
DR ProteomicsDB; 53021; -. [P14091-2]
DR Antibodypedia; 1957; 310 antibodies from 30 providers.
DR DNASU; 1510; -.
DR Ensembl; ENST00000358184.7; ENSP00000350911.2; ENSG00000196188.12. [P14091-1]
DR Ensembl; ENST00000678498.1; ENSP00000504305.1; ENSG00000196188.12. [P14091-2]
DR GeneID; 1510; -.
DR KEGG; hsa:1510; -.
DR MANE-Select; ENST00000358184.7; ENSP00000350911.2; NM_001910.4; NP_001901.1.
DR UCSC; uc001hdu.3; human. [P14091-1]
DR CTD; 1510; -.
DR DisGeNET; 1510; -.
DR GeneCards; CTSE; -.
DR HGNC; HGNC:2530; CTSE.
DR HPA; ENSG00000196188; Tissue enriched (stomach).
DR MIM; 116890; gene.
DR neXtProt; NX_P14091; -.
DR OpenTargets; ENSG00000196188; -.
DR PharmGKB; PA27030; -.
DR VEuPathDB; HostDB:ENSG00000196188; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000161300; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; P14091; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; P14091; -.
DR TreeFam; TF314990; -.
DR BRENDA; 3.4.23.34; 2681.
DR PathwayCommons; P14091; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR SABIO-RK; P14091; -.
DR SignaLink; P14091; -.
DR SIGNOR; P14091; -.
DR BioGRID-ORCS; 1510; 13 hits in 1071 CRISPR screens.
DR ChiTaRS; CTSE; human.
DR EvolutionaryTrace; P14091; -.
DR GeneWiki; Cathepsin_E; -.
DR GenomeRNAi; 1510; -.
DR Pharos; P14091; Tchem.
DR PRO; PR:P14091; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P14091; protein.
DR Bgee; ENSG00000196188; Expressed in jejunal mucosa and 114 other tissues.
DR Genevisible; P14091; HS.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008233; F:peptidase activity; IDA:ARUK-UCL.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IDA:ARUK-UCL.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033145; Cathepsin_E.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR PANTHER; PTHR47966:SF26; PTHR47966:SF26; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aspartyl protease;
KW Autocatalytic cleavage; Direct protein sequencing; Disulfide bond;
KW Endosome; Glycoprotein; Hydrolase; Protease; Reference proteome; Signal;
KW Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8346912"
FT PROPEP 20..53
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2334440,
FT ECO:0000269|PubMed:8346912"
FT /id="PRO_0000025974"
FT CHAIN 54..396
FT /note="Cathepsin E form I"
FT /id="PRO_0000025975"
FT CHAIN 57..396
FT /note="Cathepsin E form II"
FT /id="PRO_0000354668"
FT DOMAIN 78..396
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 60
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:7789521"
FT DISULFID 109..114
FT /evidence="ECO:0000250"
FT DISULFID 272..276
FT /evidence="ECO:0000250"
FT DISULFID 314..351
FT /evidence="ECO:0000250"
FT VAR_SEQ 154
FT /note="S -> SAFATQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7983070"
FT /id="VSP_059425"
FT VAR_SEQ 263..395
FT /note="IQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVEC
FT ANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDV
FT FIRQFYSVFDRGNNRVGLAPAV -> MLWSVPTLTSCRMSPSPLTESPIPSAQLPTPYW
FT TSWMECSSAAVAFKDLTSTLQLGPSGSWGMSSFDSFTQSLTVGITVWDWPQQSPKEGPC
FT VCACLSDR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12531480"
FT /id="VSP_059426"
FT VARIANT 82
FT /note="I -> V (in dbSNP:rs57621203)"
FT /id="VAR_061731"
FT VARIANT 324
FT /note="T -> I (in dbSNP:rs6503)"
FT /id="VAR_014572"
FT MUTAGEN 60
FT /note="C->A: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:7789521"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1TZS"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 158..168
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1TZS"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1TZS"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:1TZS"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1TZS"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:1TZS"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:1TZS"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:1TZS"
SQ SEQUENCE 396 AA; 42794 MW; 40B643C5FB01521E CRC64;
MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC
SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF
QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSVEGLTV VGQQFGESVT EPGQTFVDAE
FDGILGLGYP SLAVGGVTPV FDNMMAQNLV DLPMFSVYMS SNPEGGAGSE LIFGGYDHSH
FSGSLNWVPV TKQAYWQIAL DNIQVGGTVM FCSEGCQAIV DTGTSLITGP SDKIKQLQNA
IGAAPVDGEY AVECANLNVM PDVTFTINGV PYTLSPTAYT LLDFVDGMQF CSSGFQGLDI
HPPAGPLWIL GDVFIRQFYS VFDRGNNRVG LAPAVP
