ITAL_MOUSE
ID ITAL_MOUSE Reviewed; 1162 AA.
AC P24063; E9Q5M7; E9QNL8; Q3U159;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Integrin alpha-L {ECO:0000305};
DE AltName: Full=CD11 antigen-like family member A;
DE AltName: Full=Leukocyte adhesion glycoprotein LFA-1 alpha chain;
DE Short=LFA-1A;
DE AltName: Full=Leukocyte function-associated molecule 1 alpha chain;
DE AltName: Full=Lymphocyte antigen 15;
DE Short=Ly-15;
DE AltName: CD_antigen=CD11a;
DE Flags: Precursor;
GN Name=Itgal {ECO:0000312|MGI:MGI:96606}; Synonyms=Lfa-1, Ly-15;
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] (ISOFORM 2), AND FUNCTION.
RX PubMed=2051027;
RA Kaufmann Y., Tseng E., Springer T.A.;
RT "Cloning of the murine lymphocyte function-associated molecule-1 alpha-
RT subunit and its expression in COS cells.";
RL J. Immunol. 147:369-374(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Spleen;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 24-42.
RX PubMed=3887182; DOI=10.1038/314540a0;
RA Springer T.A., Teplow D.B., Dreyer W.J.;
RT "Sequence homology of the LFA-1 and Mac-1 leukocyte adhesion glycoproteins
RT and unexpected relation to leukocyte interferon.";
RL Nature 314:540-542(1985).
RN [6]
RP FUNCTION.
RX PubMed=16234355; DOI=10.1182/blood-2005-08-3123;
RA Liu Z., Zhao M., Li N., Diaz L.A., Mayadas T.N.;
RT "Differential roles for beta2 integrins in experimental autoimmune bullous
RT pemphigoid.";
RL Blood 107:1063-1069(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, 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).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24158516; DOI=10.1161/atvbaha.113.302077;
RA Jiang E., Perrard X.D., Yang D., Khan I.M., Perrard J.L., Smith C.W.,
RA Ballantyne C.M., Wu H.;
RT "Essential role of CD11a in CD8+ T-cell accumulation and activation in
RT adipose tissue.";
RL Arterioscler. Thromb. Vasc. Biol. 34:34-43(2014).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25108025; DOI=10.4049/jimmunol.1301820;
RA Bose T.O., Colpitts S.L., Pham Q.M., Puddington L., Lefrancois L.;
RT "CD11a is essential for normal development of hematopoietic
RT intermediates.";
RL J. Immunol. 193:2863-2872(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29100055; DOI=10.1016/j.molcel.2017.10.003;
RA Swaim C.D., Scott A.F., Canadeo L.A., Huibregtse J.M.;
RT "Extracellular ISG15 signals cytokine secretion through the LFA-1 integrin
RT receptor.";
RL Mol. Cell 68:581-590(2017).
CC -!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3
CC and ICAM4 (PubMed:2051027). Integrin ITGAL/ITGB2 is a receptor for F11R
CC (By similarity). Integrin ITGAL/ITGB2 is a receptor for the secreted
CC form of ubiquitin-like protein ISG15; the interaction is mediated by
CC ITGAL (PubMed:29100055). Involved in a variety of immune phenomena
CC including leukocyte-endothelial cell interaction, cytotoxic T-cell
CC mediated killing, and antibody dependent killing by granulocytes and
CC monocytes. Contributes to natural killer cell cytotoxicity. Involved in
CC leukocyte adhesion and transmigration of leukocytes including T-cells
CC and neutrophils (PubMed:16234355, PubMed:24158516). Required for
CC generation of common lymphoid progenitor cells in bone marrow,
CC indicating the role in lymphopoiesis (PubMed:25108025). Integrin
CC ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic
CC neutrophil phagocytosis by macrophages. {ECO:0000250|UniProtKB:P20701,
CC ECO:0000269|PubMed:16234355, ECO:0000269|PubMed:2051027,
CC ECO:0000269|PubMed:24158516, ECO:0000269|PubMed:25108025,
CC ECO:0000269|PubMed:29100055}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The ITGAL alpha
CC subunit associates with the ITGB2 beta subunit. Interacts with THBD.
CC {ECO:0000250|UniProtKB:P20701}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20701};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P24063-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P24063-2; Sequence=VSP_061239;
CC -!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000269|PubMed:24158516,
CC ECO:0000269|PubMed:25108025}.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage. The I-domain is necessary
CC and sufficient for interaction with ICAM1 and F11R.
CC {ECO:0000250|UniProtKB:P20701}.
CC -!- PTM: In resting T-cells, up to 40% of surface ITGAL is constitutively
CC phosphorylated. Phosphorylation causes conformational changes needed
CC for ligand binding and is necessary for the activation by some
CC physiological agents. {ECO:0000250|UniProtKB:P20701}.
CC -!- DISRUPTION PHENOTYPE: Mice show decreased cellularity in thymus but not
CC spleen, and impaired early T cell development (PubMed:25108025). Obese
CC mutant mice show decreased total number of T-cells, lower levels of
CC neutrophil elastase and reduced cytotoxic T-cell proliferation in
CC adipose tissue, as well as improved glucose tolerance and insulin
CC resistance in comparison to obese wild type mice (PubMed:24158516).
CC Splenocytes from mutant mice do not respond to extracellular Isg15 as
CC demonstrated by lack of Ifng secretion in contrast to wild-type cells
CC which secrete Ifng in response to treatment with Isg15
CC (PubMed:29100055). {ECO:0000269|PubMed:24158516,
CC ECO:0000269|PubMed:25108025, ECO:0000269|PubMed:29100055}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39426.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M60778; AAA39426.1; ALT_FRAME; mRNA.
DR EMBL; AK156251; BAE33641.1; -; mRNA.
DR EMBL; AC133494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145802; AAI45803.1; -; mRNA.
DR CCDS; CCDS57588.1; -. [P24063-2]
DR CCDS; CCDS57589.1; -. [P24063-1]
DR PIR; I56126; I56126.
DR RefSeq; NP_001240801.1; NM_001253872.1.
DR RefSeq; NP_001240802.1; NM_001253873.1.
DR AlphaFoldDB; P24063; -.
DR SMR; P24063; -.
DR ComplexPortal; CPX-3128; Integrin alphaL-beta2 complex.
DR DIP; DIP-35643N; -.
DR IntAct; P24063; 4.
DR STRING; 10090.ENSMUSP00000101913; -.
DR BindingDB; P24063; -.
DR ChEMBL; CHEMBL1075188; -.
DR GlyGen; P24063; 15 sites.
DR iPTMnet; P24063; -.
DR PhosphoSitePlus; P24063; -.
DR SwissPalm; P24063; -.
DR EPD; P24063; -.
DR MaxQB; P24063; -.
DR PaxDb; P24063; -.
DR PRIDE; P24063; -.
DR ProteomicsDB; 301689; -.
DR ProteomicsDB; 312541; -.
DR ProteomicsDB; 355028; -.
DR Antibodypedia; 13698; 2108 antibodies from 47 providers.
DR DNASU; 16408; -.
DR Ensembl; ENSMUST00000106306; ENSMUSP00000101913; ENSMUSG00000030830. [P24063-1]
DR Ensembl; ENSMUST00000117762; ENSMUSP00000113946; ENSMUSG00000030830. [P24063-2]
DR GeneID; 16408; -.
DR KEGG; mmu:16408; -.
DR CTD; 3683; -.
DR MGI; MGI:96606; Itgal.
DR VEuPathDB; HostDB:ENSMUSG00000030830; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000161495; -.
DR HOGENOM; CLU_004111_3_0_1; -.
DR InParanoid; P24063; -.
DR OMA; TVCFQLK; -.
DR OrthoDB; 73876at2759; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16408; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Itgal; mouse.
DR PRO; PR:P24063; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P24063; protein.
DR Bgee; ENSMUSG00000030830; Expressed in granulocyte and 82 other tissues.
DR ExpressionAtlas; P24063; baseline and differential.
DR Genevisible; P24063; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0034687; C:integrin alphaL-beta2 complex; ISO:MGI.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0030369; F:ICAM-3 receptor activity; 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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:MGI.
DR GO; GO:0035683; P:memory T cell extravasation; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IDA:MGI.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; ISO:MGI.
DR Gene3D; 2.130.10.130; -; 2.
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 InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 2.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
KW Magnesium; Membrane; Metal-binding; Phagocytosis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3887182"
FT CHAIN 24..1162
FT /note="Integrin alpha-L"
FT /id="PRO_0000016293"
FT TOPO_DOM 24..1088
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1110..1162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 28..79
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 80..138
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 153..325
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 336..387
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 390..443
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 444..504
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 505..561
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 565..625
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1124..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1112..1116
FT /note="GFFKR motif"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 528
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 536
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 588
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 596
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 891
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..77
FT /evidence="ECO:0000250"
FT DISULFID 108..126
FT /evidence="ECO:0000250"
FT DISULFID 147..199
FT /evidence="ECO:0000250"
FT DISULFID 651..705
FT /evidence="ECO:0000250"
FT DISULFID 768..774
FT /evidence="ECO:0000250"
FT DISULFID 841..857
FT /evidence="ECO:0000250"
FT DISULFID 994..1010
FT /evidence="ECO:0000250"
FT DISULFID 1018..1049
FT /evidence="ECO:0000250"
FT VAR_SEQ 743
FT /note="Missing (in isoform 2)"
FT /id="VSP_061239"
FT CONFLICT 973
FT /note="W -> R (in Ref. 1; AAA39426, 2; BAE33641 and 4;
FT AAI45803)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="P -> L (in Ref. 1; AAA39426, 2; BAE33641 and 4;
FT AAI45803)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="R -> W (in Ref. 1; AAA39426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1162 AA; 128314 MW; CA2118033958BC44 CRC64;
MSFRIAGPRL LLLGLQLFAK AWSYNLDTRP TQSFLAQAGR HFGYQVLQIE DGVVVGAPGE
GDNTGGLYHC RTSSEFCQPV SLHGSNHTSK YLGMTLATDA AKGSLLACDP GLSRTCDQNT
YLSGLCYLFP QSLEGPMLQN RPAYQECMKG KVDLVFLFDG SQSLDRKDFE KILEFMKDVM
RKLSNTSYQF AAVQFSTDCR TEFTFLDYVK QNKNPDVLLG SVQPMFLLTN TFRAINYVVA
HVFKEESGAR PDATKVLVII TDGEASDKGN ISAAHDITRY IIGIGKHFVS VQKQKTLHIF
ASEPVEEFVK ILDTFEKLKD LFTDLQRRIY AIEGTNRQDL TSFNMELSSS GISADLSKGH
AVVGAVGAKD WAGGFLDLRE DLQGATFVGQ EPLTSDVRGG YLGYTVAWMT SRSSRPLLAA
GAPRYQHVGQ VLLFQAPEAG GRWNQTQKIE GTQIGSYFGG ELCSVDLDQD GEAELLLIGA
PLFFGEQRGG RVFTYQRRQS LFEMVSELQG DPGYPLGRFG AAITALTDIN GDRLTDVAVG
APLEEQGAVY IFNGKPGGLS PQPSQRIQGA QVFPGIRWFG RSIHGVKDLG GDRLADVVVG
AEGRVVVLSS RPVVDVVTEL SFSPEEIPVH EVECSYSARE EQKHGVKLKA CFRIKPLTPQ
FQGRLLANLS YTLQLDGHRM RSRGLFPDGS HELSGNTSIT PDKSCLDFHF HFPICIQDLI
SPINVSLNFS LLEEEGTPRD QKVGRAMQPI LRPSIHTVTK EIPFEKNCGE DKKCEANLTL
SSPARSGPLR LMSSASLAVE WTLSNSGEDA YWVRLDLDFP RGLSFRKVEM LQPHSRMPVS
CEELTEGSSL LTKTLKCNVS SPIFKAGQEV SLQVMFNTLL NSSWEDFVEL NGTVHCENEN
SSLQEDNSAA THIPVLYPVN ILTKEQENST LYISFTPKGP KTQQVQHVYQ VRIQPSAYDH
NMPTLEALVG VPWPHSEDPI TYTWSVQTDP LVTCHSEDLK RPSSEAEQPC LPGVQFRCPI
VFRREILIQV TGTVELSKEI KASSTLSLCS SLSVSFNSSK HFHLYGSKAS EAQVLVKVDL
IHEKEMLHVY VLSGIGGLVL LFLIFLALYK VGFFKRNLKE KMEADGGVPN GSPPEDTDPL
AVPGEETKDM GCLEPLRESD KD
