ITA8_MOUSE
ID ITA8_MOUSE Reviewed; 1062 AA.
AC A2ARA8; O70304; Q3UXV8; Q8BRG3; Q8C0H7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Integrin alpha-8;
DE Contains:
DE RecName: Full=Integrin alpha-8 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-8 light chain;
DE Flags: Precursor;
GN Name=Itga8;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Testis, and Wolffian duct;
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].
RC STRAIN=C57BL/6J;
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 [MRNA] OF 45-1056 (ISOFORM 1), FUNCTION, DISRUPTION
RP PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC TISSUE=Fibroblast;
RX PubMed=9054500; DOI=10.1016/s0092-8674(00)81903-0;
RA Mueller U., Wang D., Denda S., Meneses J.J., Pedersen R.A., Reichardt L.F.;
RT "Integrin alpha8beta1 is critically important for epithelial-mesenchymal
RT interactions during kidney morphogenesis.";
RL Cell 88:603-613(1997).
RN [4]
RP FUNCTION.
RX PubMed=9548928; DOI=10.1021/bi9727489;
RA Denda S., Mueller U., Crossin K.L., Erickson H.P., Reichardt L.F.;
RT "Utilization of a soluble integrin-alkaline phosphatase chimera to
RT characterize integrin alpha 8 beta 1 receptor interactions with tenascin:
RT murine alpha 8 beta 1 binds to the RGD site in tenascin-C fragments, but
RT not to native tenascin-C.";
RL Biochemistry 37:5464-5474(1998).
RN [5]
RP FUNCTION.
RX PubMed=9614184; DOI=10.1091/mbc.9.6.1425;
RA Denda S., Reichardt L.F., Mueller U.;
RT "Identification of osteopontin as a novel ligand for the integrin alpha8
RT beta1 and potential roles for this integrin-ligand interaction in kidney
RT morphogenesis.";
RL Mol. Biol. Cell 9:1425-1435(1998).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10024342; DOI=10.1523/jneurosci.19-05-01541.1999;
RA Pinkstaff J.K., Detterich J., Lynch G., Gall C.;
RT "Integrin subunit gene expression is regionally differentiated in adult
RT brain.";
RL J. Neurosci. 19:1541-1556(1999).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10504498; DOI=10.1046/j.1523-1755.1999.00662.x;
RA Hartner A., Schoecklmann H., Proels F., Mueller U., Sterzel R.B.;
RT "Alpha8 integrin in glomerular mesangial cells and in experimental
RT glomerulonephritis.";
RL Kidney Int. 56:1468-1480(1999).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=10742111; DOI=10.1038/74286;
RA Littlewood Evans A., Mueller U.;
RT "Stereocilia defects in the sensory hair cells of the inner ear in mice
RT deficient in integrin alpha8beta1.";
RL Nat. Genet. 24:424-428(2000).
RN [9]
RP FUNCTION.
RX PubMed=11470831; DOI=10.1083/jcb.200103069;
RA Brandenberger R., Schmidt A., Linton J., Wang D., Backus C., Denda S.,
RA Mueller U., Reichardt L.F.;
RT "Identification and characterization of a novel extracellular matrix
RT protein nephronectin that is associated with integrin alpha8beta1 in the
RT embryonic kidney.";
RL J. Cell Biol. 154:447-458(2001).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11891185; DOI=10.1016/s0002-9440(10)64909-7;
RA Hartner A., Cordasic N., Klanke B., Mueller U., Sterzel R.B., Hilgers K.F.;
RT "The alpha8 integrin chain affords mechanical stability to the glomerular
RT capillary tuft in hypertensive glomerular disease.";
RL Am. J. Pathol. 160:861-867(2002).
RN [11]
RP DEVELOPMENTAL STAGE.
RX PubMed=14500699; DOI=10.1177/002215540305101008;
RA Wagner T.E., Frevert C.W., Herzog E.L., Schnapp L.M.;
RT "Expression of the integrin subunit alpha8 in murine lung development.";
RL J. Histochem. Cytochem. 51:1307-1315(2003).
RN [12]
RP FUNCTION.
RX PubMed=12787402; DOI=10.1046/j.1523-1755.2003.00057.x;
RA Bieritz B., Spessotto P., Colombatti A., Jahn A., Prols F., Hartner A.;
RT "Role of alpha8 integrin in mesangial cell adhesion, migration, and
RT proliferation.";
RL Kidney Int. 64:119-127(2003).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17537792; DOI=10.1242/dev.005033;
RA Linton J.M., Martin G.R., Reichardt L.F.;
RT "The ECM protein nephronectin promotes kidney development via integrin
RT alpha8beta1-mediated stimulation of Gdnf expression.";
RL Development 134:2501-2509(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Integrin alpha-8/beta-1 functions in the genesis of kidney
CC and probably of other organs by regulating the recruitment of
CC mesenchymal cells into epithelial structures. It recognizes the
CC sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1
CC TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney
CC genesis. Neuronal receptor for TNC it mediates cell-cell interactions
CC and regulates neurite outgrowth of sensory and motor neurons.
CC {ECO:0000269|PubMed:10742111, ECO:0000269|PubMed:11470831,
CC ECO:0000269|PubMed:11891185, ECO:0000269|PubMed:12787402,
CC ECO:0000269|PubMed:17537792, ECO:0000269|PubMed:9054500,
CC ECO:0000269|PubMed:9548928, ECO:0000269|PubMed:9614184}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond.
CC Alpha-8 associates with beta-1.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10742111}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:10742111}. Cell
CC membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2ARA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2ARA8-2; Sequence=VSP_027364, VSP_027365;
CC -!- TISSUE SPECIFICITY: In brain, expressed in deep cortex, hippocampal
CC CA1, basolateral amygdala and striatum. In kidney, expressed in
CC glomerular mesengium (at protein level). {ECO:0000269|PubMed:10024342,
CC ECO:0000269|PubMed:10504498}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mesenchymal cells of developing
CC organs such as gut, lung, gonads and nephrogenic cord.
CC {ECO:0000269|PubMed:14500699, ECO:0000269|PubMed:9054500}.
CC -!- DISRUPTION PHENOTYPE: Mice display renal agenesis and dysgenesis. This
CC is associated with a reduced expression of Gdnf that is similarly found
CC in mice lacking Npnt. Adult mice also display increased susceptibility
CC to glomerular capillary destruction upon mechanical stress. Mice
CC lacking Itga8 also have difficulty balancing associated with structural
CC defects in the inner ear where utricular hair cells lack stereocilia.
CC {ECO:0000269|PubMed:10742111, ECO:0000269|PubMed:11891185,
CC ECO:0000269|PubMed:17537792, ECO:0000269|PubMed:9054500}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; AK031326; BAC27348.1; -; mRNA.
DR EMBL; AK044910; BAC32137.1; -; mRNA.
DR EMBL; AK135193; BAE22455.1; -; mRNA.
DR EMBL; AL845313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF041409; AAC15665.1; -; mRNA.
DR CCDS; CCDS15689.1; -. [A2ARA8-1]
DR RefSeq; NP_001001309.1; NM_001001309.3. [A2ARA8-1]
DR AlphaFoldDB; A2ARA8; -.
DR SMR; A2ARA8; -.
DR BioGRID; 232293; 2.
DR ComplexPortal; CPX-3122; Integrin alpha8-beta1 complex.
DR STRING; 10090.ENSMUSP00000028106; -.
DR GlyGen; A2ARA8; 16 sites.
DR iPTMnet; A2ARA8; -.
DR PhosphoSitePlus; A2ARA8; -.
DR MaxQB; A2ARA8; -.
DR PaxDb; A2ARA8; -.
DR PeptideAtlas; A2ARA8; -.
DR PRIDE; A2ARA8; -.
DR ProteomicsDB; 268890; -. [A2ARA8-1]
DR ProteomicsDB; 268891; -. [A2ARA8-2]
DR Antibodypedia; 961; 208 antibodies from 28 providers.
DR DNASU; 241226; -.
DR Ensembl; ENSMUST00000028106; ENSMUSP00000028106; ENSMUSG00000026768. [A2ARA8-1]
DR GeneID; 241226; -.
DR KEGG; mmu:241226; -.
DR UCSC; uc008ijk.1; mouse. [A2ARA8-1]
DR UCSC; uc008ijl.1; mouse. [A2ARA8-2]
DR CTD; 8516; -.
DR MGI; MGI:109442; Itga8.
DR VEuPathDB; HostDB:ENSMUSG00000026768; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000156737; -.
DR HOGENOM; CLU_004111_4_0_1; -.
DR InParanoid; A2ARA8; -.
DR OMA; RTSVIWA; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; A2ARA8; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 241226; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Itga8; mouse.
DR PRO; PR:A2ARA8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2ARA8; protein.
DR Bgee; ENSMUSG00000026768; Expressed in ascending aorta and 187 other tissues.
DR ExpressionAtlas; A2ARA8; baseline and differential.
DR Genevisible; A2ARA8; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:BHF-UCL.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR Gene3D; 2.130.10.130; -; 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; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 6.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding;
KW Neurogenesis; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1062
FT /note="Integrin alpha-8"
FT /id="PRO_0000297709"
FT CHAIN 38..905
FT /note="Integrin alpha-8 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000297710"
FT CHAIN 906..1062
FT /note="Integrin alpha-8 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000297711"
FT TOPO_DOM 36..1010
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1011..1031
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1032..1062
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 41..104
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 121..182
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 187..239
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 252..305
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 306..371
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 372..430
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 434..497
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 454..456
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1004
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..105
FT /evidence="ECO:0000250"
FT DISULFID 149..170
FT /evidence="ECO:0000250"
FT DISULFID 186..199
FT /evidence="ECO:0000250"
FT DISULFID 506..517
FT /evidence="ECO:0000250"
FT DISULFID 523..579
FT /evidence="ECO:0000250"
FT DISULFID 640..646
FT /evidence="ECO:0000250"
FT DISULFID 712..725
FT /evidence="ECO:0000250"
FT DISULFID 866..923
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 928..933
FT /evidence="ECO:0000250"
FT VAR_SEQ 282..286
FT /note="ELVAG -> GQRHP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027364"
FT VAR_SEQ 287..1062
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027365"
FT CONFLICT 66
FT /note="D -> G (in Ref. 1; BAE22455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1062 AA; 117556 MW; DB1ACA43FADD3AC0 CRC64;
MSAGTHCGPP GNRAPPFARL CCVSAALGML WSPACLAFNL DVDKLTVYSG PEGSYFGYSL
DFYIPDARTA SVLVGAPKAN TSQPDIVEGG AVYYCPWPSE RSAQCKQIPF DTTNNRKIRV
NGTKEPIEFK SNQWFGATVR AHKGKVVACA PLYHWRTLKP NPAKDPVGTC YVAIQNFSAY
AEHSPCRNSN ADPEGQGYCQ AGFSLDFYKN GDLIVGGPGS FYWQGQVITV SIADIIANYS
FKDILRKLAA EKQTDVAPAS YDDSYLGYSV AAGEFTGDSQ QELVAGIPRG AQNFGYVSII
NSTDMTFIQN FTGEQMASYF GYTVVVSDVN NDGMDDILVG APLFMEREFE SNPREVGQVY
LYLQASALLF QDPQVLTGTE TFGRFGSSVA HLGDLNQDGY NDIAIGVPFA GKDQRGKVLI
YNGNPRGLHS KPSQVLQGIW GSQTIPSGFG FSLRGDADID KNDYPDLLVG AFGKGKVAVY
RARPVVTVDA QLLLHPMIIN LENKTCQIPE FPTPVACFSV RVCASIAGQS ISNTIALLAE
VQLDFLKQKG AIKRTLFLHN HQSHFTFPFV MKQQKSLHCQ DFMVYLRDET EFRDKLSPIN
ISLNYSLDDS TFKDSLEVKP ILNHYRDNVV TEQAHILVDC GEDNLCVPDL KLSARPDKHQ
IIIGDENHLM LIINARNEGE GAYEAELFVI IPEEADYVGI ERNNKGLRPL SCEYKMENVT
RMVVCDLGNP MVTGTNFSLG LRFAVPRLEK TNMSINFDLQ IRSSNKDNPD SNFERVQINI
TAIAQVEIRG VSHPPQIVLP IHNWEPEKKP HKEEEVGPLV EHIYELHNIG PSTISDSILD
VGWPFSARDE FLLYIFHLQT LGPLQCQTNP EINPQDIKPA ASPEDTPELS AFLRNATIPH
LVRKRDVPVV QLHRQSPARI LNCTNIDCLQ ISCAVGRLGG GESAVLKVRS RLWAHTFLKR
KNDHYALASL VSFEVKKMPY KEQPAKLPAG STAVKTSVIW ATPNVSFSIP LWVIILAILL
GLLVLAILTL ALWKCGFFDR ARPPQDEMTD REQLTSDKTP EA
