ID ITA8_HUMAN Reviewed; 1063 AA. AC P53708; B0YJ31; Q5VX94; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 3. DT 24-JAN-2024, entry version 189. 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 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 [GENOMIC DNA], AND VARIANTS LEU-216; PHE-577; PRO-581; RP HIS-748; VAL-993 AND ALA-994. RG SeattleSNPs variation discovery resource; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-1063, TISSUE SPECIFICITY, AND VARIANT RP ALA-994. RX PubMed=7768999; DOI=10.1242/jcs.108.2.537; RA Schnapp L.M., Breuss J.M., Ramos D.M., Sheppard D., Pytela R.; RT "Sequence and tissue distribution of the human integrin alpha 8 subunit: a RT beta 1-associated alpha subunit expressed in smooth muscle cells."; RL J. Cell Sci. 108:537-544(1995). RN [6] 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 [7] RP FUNCTION. RX PubMed=12415008; DOI=10.1242/jcs.00145; RA Lu M., Munger J.S., Steadele M., Busald C., Tellier M., Schnapp L.M.; RT "Integrin alpha8beta1 mediates adhesion to LAP-TGFbeta1."; RL J. Cell Sci. 115:4641-4648(2002). RN [8] RP FUNCTION. RX PubMed=15721307; DOI=10.1016/j.bbrc.2005.01.125; RA Farias E., Lu M., Li X., Schnapp L.M.; RT "Integrin alpha8beta1-fibronectin interactions promote cell survival via RT PI3 kinase pathway."; RL Biochem. Biophys. Res. Commun. 329:305-311(2005). RN [9] RP SUBCELLULAR LOCATION, VARIANTS RHDA1 MET-255 AND ARG-407, AND RP CHARACTERIZATION OF VARIANT RHDA1 ARG-407. RX PubMed=24439109; DOI=10.1016/j.ajhg.2013.12.017; RA Humbert C., Silbermann F., Morar B., Parisot M., Zarhrate M., Masson C., RA Tores F., Blanchet P., Perez M.J., Petrov Y., Khau Van Kien P., Roume J., RA Leroy B., Gribouval O., Kalaydjieva L., Heidet L., Salomon R., Antignac C., RA Benmerah A., Saunier S., Jeanpierre C.; RT "Integrin alpha 8 recessive mutations are responsible for bilateral renal RT agenesis in humans."; RL Am. J. Hum. Genet. 94:288-294(2014). RN [10] RP VARIANTS LEU-567; PHE-577; PRO-581; HIS-748; VAL-993 AND ALA-994. RX PubMed=15579315; DOI=10.1016/j.matbio.2004.08.005; RA Ekwa-Ekoka C., Diaz G.A., Carlson C., Hasegawa T., Samudrala R., Lim K.-C., RA Yabu J.M., Levy B., Schnapp L.M.; RT "Genomic organization and sequence variation of the human integrin subunit RT alpha8 gene (ITGA8)."; RL Matrix Biol. 23:487-496(2004). 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:12415008, ECO:0000269|PubMed:15721307}. 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:24439109}; Single- CC pass type I membrane protein {ECO:0000269|PubMed:24439109}. Cell CC membrane {ECO:0000269|PubMed:24439109}. CC -!- TISSUE SPECIFICITY: Expressed in mesenchymal cells, including alveolar CC myofibroblasts, kidney mesangial cells and hepatic stellar cells and CC vascular and visceral smooth muscle (at protein level). CC {ECO:0000269|PubMed:10504498, ECO:0000269|PubMed:7768999}. CC -!- DISEASE: Renal hypodysplasia/aplasia 1 (RHDA1) [MIM:191830]: A CC perinatally lethal renal disease encompassing a spectrum of kidney CC development defects, including renal agenesis, bilateral renal aplasia, CC hypoplasia, (cystic) dysplasia, and severe obstructive uropathy. CC {ECO:0000269|PubMed:24439109}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/itga8/"; 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; AY371697; AAQ56848.2; -; Genomic_DNA. DR EMBL; EF444991; ACA06009.1; -; Genomic_DNA. DR EMBL; AL359645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590636; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86235.1; -; Genomic_DNA. DR EMBL; L36531; AAA93514.1; -; mRNA. DR CCDS; CCDS31155.1; -. DR RefSeq; NP_003629.2; NM_003638.2. DR AlphaFoldDB; P53708; -. DR SMR; P53708; -. DR BioGRID; 114088; 64. DR ComplexPortal; CPX-1815; Integrin alpha8-beta1 complex. DR CORUM; P53708; -. DR IntAct; P53708; 15. DR STRING; 9606.ENSP00000367316; -. DR BindingDB; P53708; -. DR GlyCosmos; P53708; 20 sites, 1 glycan. DR GlyGen; P53708; 20 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P53708; -. DR PhosphoSitePlus; P53708; -. DR SwissPalm; P53708; -. DR BioMuta; ITGA8; -. DR DMDM; 311033437; -. DR EPD; P53708; -. DR jPOST; P53708; -. DR MassIVE; P53708; -. DR MaxQB; P53708; -. DR PaxDb; 9606-ENSP00000367316; -. DR PeptideAtlas; P53708; -. DR ProteomicsDB; 56614; -. DR Antibodypedia; 961; 227 antibodies from 28 providers. DR DNASU; 8516; -. DR Ensembl; ENST00000378076.4; ENSP00000367316.3; ENSG00000077943.8. DR GeneID; 8516; -. DR KEGG; hsa:8516; -. DR MANE-Select; ENST00000378076.4; ENSP00000367316.3; NM_003638.3; NP_003629.2. DR UCSC; uc001ioc.2; human. DR AGR; HGNC:6144; -. DR CTD; 8516; -. DR DisGeNET; 8516; -. DR GeneCards; ITGA8; -. DR HGNC; HGNC:6144; ITGA8. DR HPA; ENSG00000077943; Tissue enhanced (prostate). DR MalaCards; ITGA8; -. DR MIM; 191830; phenotype. DR MIM; 604063; gene. DR neXtProt; NX_P53708; -. DR OpenTargets; ENSG00000077943; -. DR Orphanet; 1848; Renal agenesis, bilateral. DR PharmGKB; PA29944; -. DR VEuPathDB; HostDB:ENSG00000077943; -. DR eggNOG; KOG3637; Eukaryota. DR GeneTree; ENSGT00940000156737; -. DR HOGENOM; CLU_004111_4_0_1; -. DR InParanoid; P53708; -. DR OMA; ECLRISC; -. DR OrthoDB; 3816176at2759; -. DR PhylomeDB; P53708; -. DR TreeFam; TF105391; -. DR PathwayCommons; P53708; -. DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR SignaLink; P53708; -. DR SIGNOR; P53708; -. DR BioGRID-ORCS; 8516; 5 hits in 1146 CRISPR screens. DR ChiTaRS; ITGA8; human. DR GeneWiki; ITGA8; -. DR GenomeRNAi; 8516; -. DR Pharos; P53708; Tbio. DR PRO; PR:P53708; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P53708; Protein. DR Bgee; ENSG00000077943; Expressed in descending thoracic aorta and 186 other cell types or tissues. DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0032591; C:dendritic spine membrane; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0034678; C:integrin alpha8-beta1 complex; TAS:BHF-UCL. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl. 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:0030030; P:cell projection organization; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0001822; P:kidney development; IMP:UniProtKB. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0001656; P:metanephros development; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl. DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl. DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl. DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1. DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR048286; Integrin_alpha_Ig-like_3. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF5; INTEGRIN ALPHA-8; 1. DR Pfam; PF01839; FG-GAP; 3. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF20806; Integrin_A_Ig_3; 1. DR Pfam; PF00357; Integrin_alpha; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 6. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. DR Genevisible; P53708; HS. PE 1: Evidence at protein level; KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues; KW Developmental protein; Differentiation; Disease variant; Disulfide bond; KW Glycoprotein; Integrin; Membrane; Metal-binding; Neurogenesis; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..38 FT /evidence="ECO:0000255" FT CHAIN 39..1063 FT /note="Integrin alpha-8" FT /id="PRO_0000016310" FT CHAIN 39..906 FT /note="Integrin alpha-8 heavy chain" FT /evidence="ECO:0000255" FT /id="PRO_0000016311" FT CHAIN 907..1063 FT /note="Integrin alpha-8 light chain" FT /evidence="ECO:0000255" FT /id="PRO_0000016312" FT TOPO_DOM 39..1012 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1013..1033 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1034..1063 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 44..105 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 122..183 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 188..240 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 253..306 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 307..372 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 373..431 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 435..498 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT MOTIF 455..457 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT BINDING 275 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 277 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 279 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 283 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 329 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 331 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 333 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 335 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 337 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 395 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 397 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 399 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 401 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 403 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 459 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 461 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 463 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 465 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 467 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P08648" FT CARBOHYD 81 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 122 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 239 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 311 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 504 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 601 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 605 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 719 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 737 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 753 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 780 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 896 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 923 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1005 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 96..106 FT /evidence="ECO:0000250" FT DISULFID 150..171 FT /evidence="ECO:0000250" FT DISULFID 187..200 FT /evidence="ECO:0000250" FT DISULFID 507..518 FT /evidence="ECO:0000250" FT DISULFID 524..580 FT /evidence="ECO:0000250" FT DISULFID 641..647 FT /evidence="ECO:0000250" FT DISULFID 713..726 FT /evidence="ECO:0000250" FT DISULFID 867..924 FT /note="Interchain (between heavy and light chains)" FT /evidence="ECO:0000250" FT DISULFID 929..934 FT /evidence="ECO:0000250" FT VARIANT 216 FT /note="V -> L (in dbSNP:rs7895372)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_018673" FT VARIANT 255 FT /note="T -> M (in RHDA1; uncertain significance; FT dbSNP:rs587777281)" FT /evidence="ECO:0000269|PubMed:24439109" FT /id="VAR_071106" FT VARIANT 407 FT /note="G -> R (in RHDA1; the mutant does not localize at FT the cell membrane; dbSNP:rs374664941)" FT /evidence="ECO:0000269|PubMed:24439109" FT /id="VAR_071107" FT VARIANT 567 FT /note="V -> L" FT /evidence="ECO:0000269|PubMed:15579315" FT /id="VAR_034682" FT VARIANT 577 FT /note="S -> F (in dbSNP:rs2298033)" FT /evidence="ECO:0000269|PubMed:15579315, ECO:0000269|Ref.1" FT /id="VAR_018674" FT VARIANT 581 FT /note="Q -> P (in dbSNP:rs9333269)" FT /evidence="ECO:0000269|PubMed:15579315, ECO:0000269|Ref.1" FT /id="VAR_018675" FT VARIANT 748 FT /note="R -> H (in dbSNP:rs9333174)" FT /evidence="ECO:0000269|PubMed:15579315, ECO:0000269|Ref.1" FT /id="VAR_018676" FT VARIANT 993 FT /note="I -> V (in dbSNP:rs9333241)" FT /evidence="ECO:0000269|PubMed:15579315, ECO:0000269|Ref.1" FT /id="VAR_018677" FT VARIANT 994 FT /note="V -> A (in dbSNP:rs1041135)" FT /evidence="ECO:0000269|PubMed:15579315, FT ECO:0000269|PubMed:7768999, ECO:0000269|Ref.1" FT /id="VAR_018678" FT CONFLICT 47 FT /note="T -> A (in Ref. 5; AAA93514)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="D -> G (in Ref. 5; AAA93514)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="R -> G (in Ref. 5; AAA93514)" FT /evidence="ECO:0000305" FT CONFLICT 304 FT /note="T -> Y (in Ref. 5; AAA93514)" FT /evidence="ECO:0000305" SQ SEQUENCE 1063 AA; 117474 MW; 8F9614BDBB897D77 CRC64; MSPGASRGPR GSQAPLIAPL CCAAAALGML LWSPACQAFN LDVEKLTVYS GPKGSYFGYA VDFHIPDART ASVLVGAPKA NTSQPDIVEG GAVYYCPWPA EGSAQCRQIP FDTTNNRKIR VNGTKEPIEF KSNQWFGATV KAHKGKVVAC APLYHWRTLK PTPEKDPVGT CYVAIQNFSA YAEFSPCRNS NADPEGQGYC QAGFSLDFYK NGDLIVGGPG SFYWQGQVIT ASVADIIANY SFKDILRKLA GEKQTEVAPA SYDDSYLGYS VAAGEFTGDS QQELVAGIPR GAQNFGYVSI INSTDMTFIQ NFTGEQMASY FGYTVVVSDV NSDGLDDVLV GAPLFMEREF ESNPREVGQI YLYLQVSSLL FRDPQILTGT ETFGRFGSAM AHLGDLNQDG YNDIAIGVPF AGKDQRGKVL IYNGNKDGLN TKPSQVLQGV WASHAVPSGF GFTLRGDSDI DKNDYPDLIV GAFGTGKVAV YRARPVVTVD AQLLLHPMII NLENKTCQVP DSMTSAACFS LRVCASVTGQ SIANTIVLMA EVQLDSLKQK GAIKRTLFLD NHQAHRVFPL VIKRQKSHQC QDFIVYLRDE TEFRDKLSPI NISLNYSLDE STFKEGLEVK PILNYYRENI VSEQAHILVD CGEDNLCVPD LKLSARPDKH QVIIGDENHL MLIINARNEG EGAYEAELFV MIPEEADYVG IERNNKGFRP LSCEYKMENV TRMVVCDLGN PMVSGTNYSL GLRFAVPRLE KTNMSINFDL QIRSSNKDNP DSNFVSLQIN ITAVAQVEIR GVSHPPQIVL PIHNWEPEEE PHKEEEVGPL VEHIYELHNI GPSTISDTIL EVGWPFSARD EFLLYIFHIQ TLGPLQCQPN PNINPQDIKP AASPEDTPEL SAFLRNSTIP HLVRKRDVHV VEFHRQSPAK ILNCTNIECL QISCAVGRLE GGESAVLKVR SRLWAHTFLQ RKNDPYALAS LVSFEVKKMP YTDQPAKLPE GSIVIKTSVI WATPNVSFSI PLWVIILAIL LGLLVLAILT LALWKCGFFD RARPPQEDMT DREQLTNDKT PEA //