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   27-MAR-2024, entry version 198.
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,
RC   Pancreas, 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}.
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; 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.ENSMUSP00000107729; -.
DR   GlyConnect; 2399; 7 N-Linked glycans (4 sites).
DR   GlyCosmos; Q61739; 8 sites, 7 glycans.
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; 10090-ENSMUSP00000028522; -.
DR   PeptideAtlas; Q61739; -.
DR   ProteomicsDB; 301686; -. [Q61739-1]
DR   ProteomicsDB; 301687; -. [Q61739-2]
DR   Pumba; Q61739; -.
DR   Antibodypedia; 1485; 1433 antibodies from 47 providers.
DR   DNASU; 16403; -.
DR   Ensembl; ENSMUST00000028522.10; ENSMUSP00000028522.4; ENSMUSG00000027111.17. [Q61739-2]
DR   Ensembl; ENSMUST00000112101.8; ENSMUSP00000107729.2; ENSMUSG00000027111.17. [Q61739-1]
DR   GeneID; 16403; -.
DR   KEGG; mmu:16403; -.
DR   UCSC; uc008kbd.2; mouse. [Q61739-1]
DR   AGR; MGI:96605; -.
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; HYINRTV; -.
DR   OrthoDB; 3816176at2759; -.
DR   PhylomeDB; Q61739; -.
DR   TreeFam; TF105391; -.
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; 3 hits in 79 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 310 other cell types or tissues.
DR   ExpressionAtlas; Q61739; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; ISO:MGI.
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:0030175; C:filopodium; ISO:MGI.
DR   GO; GO:0030056; C:hemidesmosome; IDA:MGI.
DR   GO; GO:0034676; C:integrin alpha6-beta4 complex; ISO: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:0043236; F:laminin binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0038132; F:neuregulin binding; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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; ISO:MGI.
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:0010811; P:positive regulation of cell-substrate adhesion; 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; 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:SF9; INTEGRIN ALPHA-6; 1.
DR   Pfam; PF13517; FG-GAP_3; 1.
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   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
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; Q61739; MM.
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
//