ITA6_MOUSE
ID ITA6_MOUSE Reviewed; 1091 AA.
AC Q61739; A2AU04;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Integrin alpha-6;
DE AltName: Full=CD49 antigen-like family member F;
DE AltName: Full=VLA-6;
DE AltName: CD_antigen=CD49f;
DE Contains:
DE RecName: Full=Integrin alpha-6 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-6 light chain;
DE Contains:
DE RecName: Full=Processed integrin alpha-6;
DE Short=Alpha6p {ECO:0000303|PubMed:11359780};
DE Flags: Precursor;
GN Name=Itga6;
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 [MRNA] (ISOFORMS ALPHA-6X1A AND ALPHA-6X1B), AND
RP FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Mammary gland;
RX PubMed=8081870; DOI=10.3109/15419069309095680;
RA Hierck B.P., Thorsteinsdottir S., Niessen C.M., Freund E., van Iperen L.,
RA Feyen A., Hogervorst F., Poelmann R.E., Mummery C.L., Sonnenberg A.;
RT "Variants of the alpha 6 beta 1 laminin receptor in early murine
RT development: distribution, molecular cloning and chromosomal localization
RT of the mouse integrin alpha 6 subunit.";
RL Cell Adhes. Commun. 1:33-53(1993).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8673141; DOI=10.1038/ng0796-370;
RA Georges-Labouesse E., Messaddeq N., Yehia G., Cadalbert L., Dierich A.,
RA Le Meur M.;
RT "Absence of integrin alpha 6 leads to epidermolysis bullosa and neonatal
RT death in mice.";
RL Nat. Genet. 13:370-373(1996).
RN [4]
RP INTERACTION WITH ADAM9.
RX PubMed=10825303; DOI=10.1242/jcs.113.12.2319;
RA Nath D., Slocombe P.M., Webster A., Stephens P.E., Docherty A.J.,
RA Murphy G.;
RT "Meltrin gamma(ADAM-9) mediates cellular adhesion through
RT alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell
RT motility.";
RL J. Cell Sci. 113:2319-2328(2000).
RN [5]
RP FUNCTION, AND INTERACTION WITH CD9.
RX PubMed=10634791; DOI=10.1126/science.287.5451.321;
RA Miyado K., Yamada G., Yamada S., Hasuwa H., Nakamura Y., Ryu F., Suzuki K.,
RA Kosai K., Inoue K., Ogura A., Okabe M., Mekada E.;
RT "Requirement of CD9 on the egg plasma membrane for fertilization.";
RL Science 287:321-324(2000).
RN [6]
RP PROTEOLYTIC PROCESSING.
RX PubMed=11359780; DOI=10.1074/jbc.m102811200;
RA Davis T.L., Rabinovitz I., Futscher B.W., Schnoelzer M., Burger F., Liu Y.,
RA Kulesz-Martin M., Cress A.E.;
RT "Identification of a novel structural variant of the alpha 6 integrin.";
RL J. Biol. Chem. 276:26099-26106(2001).
RN [7]
RP PROTEOLYTIC PROCESSING, AND TISSUE SPECIFICITY.
RX PubMed=20664806; DOI=10.2174/1874079000802010001;
RA Demetriou M.C., Kwei K.A., Powell M.B., Nagle R.B., Bowden G.T.,
RA Cress A.E.;
RT "Integrin A6 cleavage in mouse skin tumors.";
RL Open Cancer J. 2:1-4(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-284; ASN-927 AND ASN-958.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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-6/beta-1 (ITGA6:ITGB1) is a receptor for
CC laminin on platelets (PubMed:8081870). Integrin alpha-6/beta-1
CC (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion
CC (PubMed:10634791). Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor
CC for laminin in epithelial cells and it plays a critical structural role
CC in the hemidesmosome (PubMed:8673141). ITGA6:ITGB4 binds to NRG1 (via
CC EGF domain) and this binding is essential for NRG1-ERBB signaling (By
CC similarity). ITGA6:ITGB4 binds to IGF1 and this binding is essential
CC for IGF1 signaling (By similarity). ITGA6:ITGB4 binds to IGF2 and this
CC binding is essential for IGF2 signaling (By similarity).
CC {ECO:0000250|UniProtKB:P23229, ECO:0000269|PubMed:10634791,
CC ECO:0000269|PubMed:8081870, ECO:0000269|PubMed:8673141}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:8081870).
CC The alpha subunit is composed of a heavy and a light chain linked by a
CC disulfide bond (PubMed:8081870). Alpha-6 associates with either beta-1
CC (ITGB1) or beta-4 (ITGB4) to form ITGA6:ITGB1 and ITGA6:ITGB4,
CC respectively (PubMed:8081870, PubMed:10634791). ITGA6:ITGB1 is found in
CC a complex with CD9; interaction takes place in oocytes and is involved
CC in sperm-egg fusion (PubMed:10634791). ITGA6:ITGB4 is found in a
CC ternary complex with NRG1 and ERBB3 (By similarity). ITGA6:ITGB4 is
CC found in a ternary complex with IGF1 and IGF1R (By similarity).
CC ITGA6:ITGB4 interacts with IGF2 (By similarity). Interacts with ADAM9
CC (PubMed:10825303). Interacts with RAB21 (By similarity). Interacts with
CC MDK. ITGA6:ITGB1 interacts with MDK; this interaction mediates MDK-
CC induced neurite outgrowth (By similarity).
CC {ECO:0000250|UniProtKB:P23229, ECO:0000269|PubMed:10634791,
CC ECO:0000269|PubMed:10825303, ECO:0000269|PubMed:8081870}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23229};
CC Single-pass type I membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:P23229}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P23229}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha-6X1B;
CC IsoId=Q61739-1; Sequence=Displayed;
CC Name=Alpha-6X1A;
CC IsoId=Q61739-2; Sequence=VSP_002726;
CC -!- TISSUE SPECIFICITY: [Processed integrin alpha-6]: Expressed at low
CC levels in normal skin tissue with elevated levels in skin tumors.
CC {ECO:0000269|PubMed:20664806}.
CC -!- PTM: Isoforms containing segment A, but not segment B, are the major
CC targets for PMA-induced phosphorylation. Phosphorylation occurs on
CC 'Ser-1064' of isoform alpha-6X1A. Phosphorylation is not required for
CC the induction of integrin alpha-6A/beta-1 high affinity but may reduce
CC the affinity for ligand (By similarity).
CC {ECO:0000250|UniProtKB:P23229}.
CC -!- PTM: Undergoes PLAU-mediated cleavage at residues Arg-595-596-Arg in a
CC time-dependent manner to produce processed integrin alpha-6 (alpha6p).
CC {ECO:0000269|PubMed:11359780, ECO:0000269|PubMed:20664806}.
CC -!- PTM: Palmitoylation by DHHC3 enhances stability and cell surface
CC expression. {ECO:0000250|UniProtKB:P23229}.
CC -!- DISRUPTION PHENOTYPE: Mice expressing a null mutation of the alpha-6
CC subunit gene die soon after birth and develop severe blistering
CC (PubMed:8673141). The blisters are due to separation of the basal
CC epithelial cells from a normally formed basement membrane
CC (PubMed:8673141). {ECO:0000269|PubMed:8673141}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; X69902; CAA49527.1; -; mRNA.
DR EMBL; AL928963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16118.1; -. [Q61739-2]
DR CCDS; CCDS71074.1; -. [Q61739-1]
DR PIR; A40463; A40463.
DR RefSeq; NP_001264899.1; NM_001277970.1. [Q61739-1]
DR RefSeq; XP_011237610.1; XM_011239308.1. [Q61739-1]
DR AlphaFoldDB; Q61739; -.
DR SMR; Q61739; -.
DR BioGRID; 200819; 10.
DR ComplexPortal; CPX-3119; Integrin alpha6-beta1 complex.
DR ComplexPortal; CPX-3120; integrin alpha6-beta4 complex.
DR STRING; 10090.ENSMUSP00000028522; -.
DR GlyConnect; 2399; 7 N-Linked glycans (4 sites).
DR GlyGen; Q61739; 8 sites, 7 N-linked glycans (4 sites).
DR iPTMnet; Q61739; -.
DR PhosphoSitePlus; Q61739; -.
DR SwissPalm; Q61739; -.
DR EPD; Q61739; -.
DR jPOST; Q61739; -.
DR MaxQB; Q61739; -.
DR PaxDb; Q61739; -.
DR PeptideAtlas; Q61739; -.
DR PRIDE; Q61739; -.
DR ProteomicsDB; 301686; -. [Q61739-1]
DR ProteomicsDB; 301687; -. [Q61739-2]
DR Antibodypedia; 1485; 1351 antibodies from 47 providers.
DR DNASU; 16403; -.
DR Ensembl; ENSMUST00000028522; ENSMUSP00000028522; ENSMUSG00000027111. [Q61739-2]
DR Ensembl; ENSMUST00000112101; ENSMUSP00000107729; ENSMUSG00000027111. [Q61739-1]
DR GeneID; 16403; -.
DR KEGG; mmu:16403; -.
DR UCSC; uc008kbd.2; mouse. [Q61739-1]
DR CTD; 3655; -.
DR MGI; MGI:96605; Itga6.
DR VEuPathDB; HostDB:ENSMUSG00000027111; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000155353; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; Q61739; -.
DR OMA; SGATRYG; -.
DR PhylomeDB; Q61739; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR BioGRID-ORCS; 16403; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Itga6; mouse.
DR PRO; PR:Q61739; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61739; protein.
DR Bgee; ENSMUSG00000027111; Expressed in sciatic nerve and 307 other tissues.
DR ExpressionAtlas; Q61739; baseline and differential.
DR Genevisible; Q61739; MM.
DR GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0030056; C:hemidesmosome; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031994; F:insulin-like growth factor I binding; ISS: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:0038132; F:neuregulin binding; ISS:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
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:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI.
DR GO; GO:0046847; P:filopodium assembly; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR GO; GO:0097534; P:lymphoid lineage cell migration; IMP:MGI.
DR GO; GO:0035878; P:nail development; ISO:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043589; P:skin morphogenesis; ISO: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; PF13517; FG-GAP_3; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
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; Disulfide bond; Glycoprotein; Integrin;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250|UniProtKB:P23229"
FT CHAIN 24..1091
FT /note="Integrin alpha-6"
FT /id="PRO_0000016261"
FT CHAIN 24..899
FT /note="Integrin alpha-6 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016262"
FT CHAIN 597..1091
FT /note="Processed integrin alpha-6"
FT /evidence="ECO:0000250|UniProtKB:P23229"
FT /id="PRO_0000448082"
FT CHAIN 903..1091
FT /note="Integrin alpha-6 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016263"
FT TOPO_DOM 24..1011
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1037
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1091
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 30..95
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 101..166
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 176..229
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 244..300
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 301..363
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 364..419
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 420..479
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1040..1044
FT /note="GFFKR motif"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 326
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="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 392
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="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT LIPID 1039
FT /note="S-palmitoyl cysteine; by DHHC3"
FT /evidence="ECO:0000250"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 958
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 86..94
FT /evidence="ECO:0000250"
FT DISULFID 131..154
FT /evidence="ECO:0000250"
FT DISULFID 175..188
FT /evidence="ECO:0000250"
FT DISULFID 489..496
FT /evidence="ECO:0000250"
FT DISULFID 502..562
FT /evidence="ECO:0000250"
FT DISULFID 626..632
FT /evidence="ECO:0000250"
FT DISULFID 726..737
FT /evidence="ECO:0000250"
FT DISULFID 881..928
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 934..939
FT /evidence="ECO:0000250"
FT VAR_SEQ 1045..1091
FT /note="SRYDDSIPRYHAVRIRKEEREIKDEKHMDNLEKKQWITKWNENESYS -> N
FT KKDHYDATYHKAEIHTQPSDKERLTSDA (in isoform Alpha-6X1A)"
FT /evidence="ECO:0000303|PubMed:8081870"
FT /id="VSP_002726"
FT CONFLICT 592
FT /note="S -> T (in Ref. 1; CAA49527)"
FT /evidence="ECO:0000305"
FT CONFLICT 781
FT /note="N -> K (in Ref. 1; CAA49527)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="V -> L (in Ref. 1; CAA49527)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="S -> T (in Ref. 1; CAA49527)"
FT /evidence="ECO:0000305"
FT CONFLICT 953
FT /note="R -> C (in Ref. 1; CAA49527)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="L -> V (in Ref. 1; CAA49527)"
FT /evidence="ECO:0000305"
FT MOD_RES Q61739-2:1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23229"
SQ SEQUENCE 1091 AA; 122159 MW; F33B055C2E8BAFAD CRC64;
MAVAGQLCLL YLSAGLLARL GTAFNLDTRE DNVIRKSGDP GSLFGFSLAM HWQLQPEDKR
LLLVGAPRAE ALPLQRANRT GGLYSCDITS RGPCTRIEFD NDADPMSESK EDQWMGVTVQ
SQGPGGKVVT CAHRYEKRQH VNTKQESRDI FGRCYVLSQN LRIEDDMDGG DWSFCDGRLR
GHEKFGSCQQ GVAATFTKDF HYIVFGAPGT YNWKGIVRVE QKNNTFFDMN IFEDGPYEVG
GETDHDESLV PVPANSYLGF SLDSGKGIVS KDDITFVSGA PRANHSGAVV LLKRDMKSAH
LLPEYIFDGE GLASSFGYDV AVVDLNADGW QDIVIGAPQY FDRDGEVGGA VYVYINQQGK
WSNVKPIRLN GTKDSMFGIS VKNIGDINQD GYPDIAVGAP YDDLGKVFIY HGSPTGIITK
PTQVLEGTSP YFGYSIAGNM DLDRNSYPDL AVGSLSDSVT IFRSRPVINI LKTITVTPNR
IDLRQKSMCG SPSGICLKVK ACFEYTAKPS GYNPPISILG ILEAEKERRK SGLSSRVQFR
NQGSEPKYTQ ELTLNRQKQR ACMEETLWLQ ENIRDKLRPI PITASVEIQE PSSRRRVNSL
PEVLPILNSN EAKTVQTDVH FLKEGCGDDN VCNSNLKLEY KFGTREGNQD KFSYLPIQKG
IPELVLKDQK DIALEITVTN SPSDPRNPRK DGDDAHEAKL IATFPDTLTY SAYRELRAFP
EKQLSCVANQ NGSQADCELG NPFKRNSSVT FYLILSTTEV TFDTTDLDIN LKLETTSNQD
NLAPITAKAK VVIELLLSVS GVAKPSQVYF GGTVVGEQAM KSEDEVGSLI EYEFRVINLG
KPLKNLGTAT LNIQWPKEIS NGKWLLYLMK VESKGLEQIV CEPHNEINYL KLKESHNSRK
KRELPEKQID DSRKFSLFPE RKYQTLNCSV NVRCVNIRCP LRGLDSKASL VLRSRLWNST
FLEEYSKLNY LDILLRASID VTAAAQNIKL PHAGTQVRVT VFPSKTVAQY SGVAWWIILL
AVLAGILMLA LLVFLLWKCG FFKRSRYDDS IPRYHAVRIR KEEREIKDEK HMDNLEKKQW
ITKWNENESY S
