ITA10_HUMAN
ID ITA10_HUMAN Reviewed; 1167 AA.
AC O75578; B2RAM4; B2RTV5; Q6UXJ6; Q9UHZ8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Integrin alpha-10;
DE Flags: Precursor;
GN Name=ITGA10; ORFNames=UNQ468/PRO827;
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=Articular chondrocyte;
RX PubMed=9685391; DOI=10.1074/jbc.273.32.20383;
RA Camper L., Hellman U., Lundgren-Aakerlund E.;
RT "Isolation, cloning, and sequence analysis of the integrin subunit alpha10,
RT a beta1-associated collagen binding integrin expressed on chondrocytes.";
RL J. Biol. Chem. 273:20383-20389(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Endothelial cell, and Heart;
RX PubMed=10702680; DOI=10.1159/000015434;
RA Lehnert K., Ni J., Leung E., Gough S.M., Morris C.M., Liu D., Wang S.-X.,
RA Langley R., Krissansen G.W.;
RT "The integrin alpha10 subunit: expression pattern, partial gene structure,
RT and chromosomal localization.";
RL Cytogenet. Cell Genet. 87:238-244(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
CC -!- FUNCTION: Integrin alpha-10/beta-1 is a receptor for collagen.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-10
CC associates with beta-1.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75578-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75578-2; Sequence=VSP_013114, VSP_013115;
CC Name=3;
CC IsoId=O75578-3; Sequence=VSP_054483;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in muscle
CC and heart. Found in articular cartilage.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AF074015; AAC31952.1; -; mRNA.
DR EMBL; AF112345; AAF21944.1; -; mRNA.
DR EMBL; AF172723; AAF61638.1; -; Genomic_DNA.
DR EMBL; AY358325; AAQ88691.1; -; mRNA.
DR EMBL; AK314255; BAG36921.1; -; mRNA.
DR EMBL; AL160282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471244; EAW71425.1; -; Genomic_DNA.
DR EMBL; BC140831; AAI40832.1; -; mRNA.
DR EMBL; BC144637; AAI44638.1; -; mRNA.
DR CCDS; CCDS72869.1; -. [O75578-1]
DR CCDS; CCDS76204.1; -. [O75578-3]
DR RefSeq; NP_001289969.1; NM_001303040.1.
DR RefSeq; NP_001289970.1; NM_001303041.1. [O75578-3]
DR RefSeq; NP_003628.2; NM_003637.4. [O75578-1]
DR AlphaFoldDB; O75578; -.
DR SMR; O75578; -.
DR BioGRID; 114087; 3.
DR ComplexPortal; CPX-1817; Integrin alpha10-beta1 complex.
DR CORUM; O75578; -.
DR IntAct; O75578; 1.
DR STRING; 9606.ENSP00000358310; -.
DR BindingDB; O75578; -.
DR ChEMBL; CHEMBL5882; -.
DR GlyGen; O75578; 11 sites.
DR iPTMnet; O75578; -.
DR PhosphoSitePlus; O75578; -.
DR BioMuta; ITGA10; -.
DR EPD; O75578; -.
DR jPOST; O75578; -.
DR MassIVE; O75578; -.
DR PaxDb; O75578; -.
DR PeptideAtlas; O75578; -.
DR PRIDE; O75578; -.
DR ProteomicsDB; 3449; -.
DR ProteomicsDB; 50095; -. [O75578-1]
DR ProteomicsDB; 50096; -. [O75578-2]
DR Antibodypedia; 20229; 39 antibodies from 16 providers.
DR DNASU; 8515; -.
DR Ensembl; ENST00000369304.8; ENSP00000358310.3; ENSG00000143127.13. [O75578-1]
DR Ensembl; ENST00000539363.2; ENSP00000439894.1; ENSG00000143127.13. [O75578-3]
DR GeneID; 8515; -.
DR KEGG; hsa:8515; -.
DR MANE-Select; ENST00000369304.8; ENSP00000358310.3; NM_003637.5; NP_003628.2.
DR UCSC; uc001eoa.4; human. [O75578-1]
DR CTD; 8515; -.
DR DisGeNET; 8515; -.
DR GeneCards; ITGA10; -.
DR HGNC; HGNC:6135; ITGA10.
DR HPA; ENSG00000143127; Low tissue specificity.
DR MIM; 604042; gene.
DR neXtProt; NX_O75578; -.
DR OpenTargets; ENSG00000143127; -.
DR PharmGKB; PA29936; -.
DR VEuPathDB; HostDB:ENSG00000143127; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000158423; -.
DR HOGENOM; CLU_004111_2_0_1; -.
DR InParanoid; O75578; -.
DR OMA; ILNCSRS; -.
DR OrthoDB; 52951at2759; -.
DR PhylomeDB; O75578; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; O75578; -.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR SignaLink; O75578; -.
DR SIGNOR; O75578; -.
DR BioGRID-ORCS; 8515; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; ITGA10; human.
DR GeneWiki; ITGA10; -.
DR GenomeRNAi; 8515; -.
DR Pharos; O75578; Tbio.
DR PRO; PR:O75578; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75578; protein.
DR Bgee; ENSG00000143127; Expressed in tibia and 127 other tissues.
DR Genevisible; O75578; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0034680; C:integrin alpha10-beta1 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005518; F:collagen binding; TAS:ProtInc.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 2.130.10.130; -; 2.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Disulfide bond; Glycoprotein;
KW Integrin; Magnesium; Membrane; Metal-binding; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1167
FT /note="Integrin alpha-10"
FT /id="PRO_0000016317"
FT TOPO_DOM 23..1122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1123..1145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1146..1167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 24..85
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 95..154
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 167..350
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 361..412
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 417..470
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 472..534
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 535..593
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 597..657
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 558
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 566
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 620
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 622
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 624
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1018
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..86
FT /evidence="ECO:0000250"
FT DISULFID 666..675
FT /evidence="ECO:0000250"
FT DISULFID 681..736
FT /evidence="ECO:0000250"
FT DISULFID 789..795
FT /evidence="ECO:0000250"
FT VAR_SEQ 19..161
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054483"
FT VAR_SEQ 123..124
FT /note="AC -> VS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013114"
FT VAR_SEQ 125..1167
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013115"
FT VARIANT 381
FT /note="R -> Q (in dbSNP:rs6665210)"
FT /id="VAR_027768"
FT VARIANT 668
FT /note="R -> W (in dbSNP:rs36073645)"
FT /id="VAR_034026"
FT VARIANT 691
FT /note="R -> H (in dbSNP:rs2274618)"
FT /id="VAR_027769"
FT VARIANT 702
FT /note="A -> T (in dbSNP:rs35515885)"
FT /id="VAR_034027"
FT VARIANT 725
FT /note="R -> Q (in dbSNP:rs2274616)"
FT /id="VAR_027770"
FT CONFLICT 844
FT /note="L -> I (in Ref. 1; AAC31952)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="V -> G (in Ref. 1; AAC31952)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="D -> E (in Ref. 1; AAC31952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1167 AA; 127602 MW; 2F7FF938B4C0CBAC CRC64;
MELPFVTHLF LPLVFLTGLC SPFNLDEHHP RLFPGPPEAE FGYSVLQHVG GGQRWMLVGA
PWDGPSGDRR GDVYRCPVGG AHNAPCAKGH LGDYQLGNSS HPAVNMHLGM SLLETDGDGG
FMACAPLWSR ACGSSVFSSG ICARVDASFQ PQGSLAPTAQ RCPTYMDVVI VLDGSNSIYP
WSEVQTFLRR LVGKLFIDPE QIQVGLVQYG ESPVHEWSLG DFRTKEEVVR AAKNLSRREG
RETKTAQAIM VACTEGFSQS HGGRPEAARL LVVVTDGESH DGEELPAALK ACEAGRVTRY
GIAVLGHYLR RQRDPSSFLR EIRTIASDPD ERFFFNVTDE AALTDIVDAL GDRIFGLEGS
HAENESSFGL EMSQIGFSTH RLKDGILFGM VGAYDWGGSV LWLEGGHRLF PPRMALEDEF
PPALQNHAAY LGYSVSSMLL RGGRRLFLSG APRFRHRGKV IAFQLKKDGA VRVAQSLQGE
QIGSYFGSEL CPLDTDRDGT TDVLLVAAPM FLGPQNKETG RVYVYLVGQQ SLLTLQGTLQ
PEPPQDARFG FAMGALPDLN QDGFADVAVG APLEDGHQGA LYLYHGTQSG VRPHPAQRIA
AASMPHALSY FGRSVDGRLD LDGDDLVDVA VGAQGAAILL SSRPIVHLTP SLEVTPQAIS
VVQRDCRRRG QEAVCLTAAL CFQVTSRTPG RWDHQFYMRF TASLDEWTAG ARAAFDGSGQ
RLSPRRLRLS VGNVTCEQLH FHVLDTSDYL RPVALTVTFA LDNTTKPGPV LNEGSPTSIQ
KLVPFSKDCG PDNECVTDLV LQVNMDIRGS RKAPFVVRGG RRKVLVSTTL ENRKENAYNT
SLSLIFSRNL HLASLTPQRE SPIKVECAAP SAHARLCSVG HPVFQTGAKV TFLLEFEFSC
SSLLSQVFVK LTASSDSLER NGTLQDNTAQ TSAYIQYEPH LLFSSESTLH RYEVHPYGTL
PVGPGPEFKT TLRVQNLGCY VVSGLIISAL LPAVAHGGNY FLSLSQVITN NASCIVQNLT
EPPGPPVHPE ELQHTNRLNG SNTQCQVVRC HLGQLAKGTE VSVGLLRLVH NEFFRRAKFK
SLTVVSTFEL GTEEGSVLQL TEASRWSESL LEVVQTRPIL ISLWILIGSV LGGLLLLALL
VFCLWKLGFF AHKKIPEEEK REEKLEQ
