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   27-MAR-2024, entry version 184.
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};
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; 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. [P24063-1]
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   GlyCosmos; P24063; 15 sites, No reported glycans.
DR   GlyGen; P24063; 16 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P24063; -.
DR   PhosphoSitePlus; P24063; -.
DR   SwissPalm; P24063; -.
DR   EPD; P24063; -.
DR   MaxQB; P24063; -.
DR   PaxDb; 10090-ENSMUSP00000101913; -.
DR   ProteomicsDB; 301689; -.
DR   ProteomicsDB; 312541; -.
DR   ProteomicsDB; 355028; -.
DR   Antibodypedia; 13698; 2405 antibodies from 47 providers.
DR   DNASU; 16408; -.
DR   Ensembl; ENSMUST00000106306.9; ENSMUSP00000101913.3; ENSMUSG00000030830.19. [P24063-1]
DR   Ensembl; ENSMUST00000117762.8; ENSMUSP00000113946.2; ENSMUSG00000030830.19. [P24063-2]
DR   GeneID; 16408; -.
DR   KEGG; mmu:16408; -.
DR   AGR; MGI:96606; -.
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; 3816176at2759; -.
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 79 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 cell types or tissues.
DR   ExpressionAtlas; P24063; baseline and differential.
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; 1.20.5.2120; -; 1.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2.
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; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF84; INTEGRIN ALPHA-L; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 2.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   Genevisible; P24063; MM.
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
//