ITA8_HUMAN
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 03-AUG-2022, entry version 181.
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/";
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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; 63.
DR ComplexPortal; CPX-1815; Integrin alpha8-beta1 complex.
DR CORUM; P53708; -.
DR IntAct; P53708; 15.
DR STRING; 9606.ENSP00000367316; -.
DR BindingDB; P53708; -.
DR GlyGen; P53708; 20 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P53708; -.
DR PhosphoSitePlus; P53708; -.
DR BioMuta; ITGA8; -.
DR DMDM; 311033437; -.
DR EPD; P53708; -.
DR jPOST; P53708; -.
DR MassIVE; P53708; -.
DR MaxQB; P53708; -.
DR PaxDb; P53708; -.
DR PeptideAtlas; P53708; -.
DR PRIDE; P53708; -.
DR ProteomicsDB; 56614; -.
DR Antibodypedia; 961; 208 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 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; RTSVIWA; -.
DR OrthoDB; 743479at2759; -.
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 1066 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 185 other tissues.
DR Genevisible; P53708; HS.
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: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:0014069; C:postsynaptic density; 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: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; 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: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; 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 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; unknown pathological 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
