ITAM_MOUSE
ID ITAM_MOUSE Reviewed; 1153 AA.
AC P05555; Q8CA73;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Integrin alpha-M;
DE AltName: Full=CD11 antigen-like family member B;
DE AltName: Full=CR-3 alpha chain;
DE AltName: Full=Cell surface glycoprotein MAC-1 subunit alpha;
DE AltName: Full=Leukocyte adhesion receptor MO1;
DE AltName: CD_antigen=CD11b;
DE Flags: Precursor;
GN Name=Itgam;
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 1).
RX PubMed=3044779; DOI=10.1002/j.1460-2075.1988.tb02953.x;
RA Pytela R.;
RT "Amino acid sequence of the murine Mac-1 alpha chain reveals homology with
RT the integrin family and an additional domain related to von Willebrand
RT factor.";
RL EMBO J. 7:1371-1378(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [GENOMIC DNA] OF 11-45.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=2942940; DOI=10.1073/pnas.83.15.5644;
RA Sastre L., Roman J.M., Teplow D.B., Dreyer W.J., Gee C.E., Larson R.S.,
RA Roberts T.M., Springer T.A.;
RT "A partial genomic DNA clone for the alpha subunit of the mouse complement
RT receptor type 3 and cellular adhesion molecule Mac-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5644-5648(1986).
RN [4]
RP PROTEIN SEQUENCE OF 17-28, AND TISSUE SPECIFICITY.
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=8986723; DOI=10.1016/s1074-7613(00)80278-2;
RA Coxon A., Rieu P., Barkalow F.J., Askari S., Sharpe A.H., von Andrian U.H.,
RA Arnaout M.A., Mayadas T.N.;
RT "A novel role for the beta 2 integrin CD11b/CD18 in neutrophil apoptosis: a
RT homeostatic mechanism in inflammation.";
RL Immunity 5:653-666(1996).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9382884; DOI=10.1084/jem.186.11.1853;
RA Tang T., Rosenkranz A., Assmann K.J., Goodman M.J., Gutierrez-Ramos J.C.,
RA Carroll M.C., Cotran R.S., Mayadas T.N.;
RT "A role for Mac-1 (CDIIb/CD18) in immune complex-stimulated neutrophil
RT function in vivo: Mac-1 deficiency abrogates sustained Fcgamma receptor-
RT dependent neutrophil adhesion and complement-dependent proteinuria in acute
RT glomerulonephritis.";
RL J. Exp. Med. 186:1853-1863(1997).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=9207125; DOI=10.1073/pnas.94.14.7526;
RA Dong Z.M., Gutierrez-Ramos J.C., Coxon A., Mayadas T.N., Wagner D.D.;
RT "A new class of obesity genes encodes leukocyte adhesion receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7526-7530(1997).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=9862668;
RA Rosenkranz A.R., Coxon A., Maurer M., Gurish M.F., Austen K.F.,
RA Friend D.S., Galli S.J., Mayadas T.N.;
RT "Impaired mast cell development and innate immunity in Mac-1 (CD11b/CD18,
RT CR3)-deficient mice.";
RL J. Immunol. 161:6463-6467(1998).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18685038; DOI=10.1523/jneurosci.1006-08.2008;
RA Wakselman S., Bechade C., Roumier A., Bernard D., Triller A., Bessis A.;
RT "Developmental neuronal death in hippocampus requires the microglial CD11b
RT integrin and DAP12 immunoreceptor.";
RL J. Neurosci. 28:8138-8143(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, 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).
CC -!- FUNCTION: Integrin ITGAM/ITGB2 is implicated in various adhesive
CC interactions of monocytes, macrophages and granulocytes as well as in
CC mediating the uptake of complement-coated particles and pathogens (By
CC similarity). It is identical with CR-3, the receptor for the iC3b
CC fragment of the third complement component. It probably recognizes the
CC R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for
CC fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of
CC fibrinogen gamma chain. Regulates neutrophil migration. In association
CC with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated
CC activation of TNF primed neutrophils (By similarity). May regulate
CC phagocytosis-induced apoptosis in extravasated neutrophils (By
CC similarity). May play a role in mast cell development (By similarity).
CC Required with TYROBP/DAP12 in microglia to control production of
CC microglial superoxide ions which promote the neuronal apoptosis that
CC occurs during brain development (PubMed:18685038).
CC {ECO:0000250|UniProtKB:P11215, ECO:0000269|PubMed:18685038,
CC ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9382884,
CC ECO:0000269|PubMed:9862668}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. ITGAM associates
CC with ITGB2. Found in a complex with CD177 and ITGB2/CD18. Interacts
CC with JAM3. Interacts with THBD. Interacts with complement factor H/CFH;
CC this interaction mediates adhesion of neutrophils to pathogens leading
CC to pathogen clearance. {ECO:0000250|UniProtKB:P11215}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8986723,
CC ECO:0000269|PubMed:9862668}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P11215}. Membrane raft
CC {ECO:0000250|UniProtKB:P11215}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P11215}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05555-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05555-2; Sequence=VSP_010473;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in monocytes and
CC granulocytes (PubMed:3887182, PubMed:8986723). Expressed in a subset of
CC peritoneal mast cells (PubMed:9862668). Expressed in microglia (at
CC protein level) (PubMed:18685038). {ECO:0000269|PubMed:18685038,
CC ECO:0000269|PubMed:3887182, ECO:0000269|PubMed:8986723,
CC ECO:0000269|PubMed:9862668}.
CC -!- INDUCTION: Induced by lipopolysaccharide (LPS) in mast cells.
CC {ECO:0000269|PubMed:9862668}.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate
CC (PubMed:8986723). The numbers of blood leukocytes are normal and
CC neutrophils rolling on blood vessels is not affected (PubMed:8986723).
CC Impaired LTB4-induced neutrophil adhesion to venules (PubMed:8986723).
CC Numbers of mast cells in the peritoneal cavity, peritoneal wall and in
CC the dorsal skin are reduced (PubMed:9862668). In an experimental model
CC of thioglycolate-induced peritonitis, abnormal accumulation of
CC recruited neutrophils due to impaired apoptosis (PubMed:8986723). In an
CC experimental model of acute septic peritonitis, 5-fold increase in
CC mortality rate, reduced neutrophil recruitment in the peritoneum,
CC reduced histamine production and impaired bacterial clearence
CC (PubMed:9862668). In experimental model of immune complex-mediated
CC glomerulonephritis, reduced neutrophil accumulation without affecting
CC their initial recruitment and reduced proteinuria (PubMed:9382884).
CC Enhanced susceptibility to high fat diet-induced obesity characterized
CC by a weight increase and higher levels of white and brown fat
CC (PubMed:9207125). Reduced apoptosis in the hippocampus in neonates
CC (PubMed:18685038). {ECO:0000269|PubMed:18685038,
CC ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9207125,
CC ECO:0000269|PubMed:9382884, ECO:0000269|PubMed:9862668}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; X07640; CAA30479.1; -; mRNA.
DR EMBL; AK039444; BAC30350.1; -; mRNA.
DR EMBL; M14293; AAA39484.1; -; Genomic_DNA.
DR CCDS; CCDS21889.1; -. [P05555-1]
DR PIR; S00551; S00551.
DR PDB; 6RHV; X-ray; 2.29 A; C=143-337.
DR PDBsum; 6RHV; -.
DR AlphaFoldDB; P05555; -.
DR SMR; P05555; -.
DR ComplexPortal; CPX-3129; Integrin alphaM-beta2 complex.
DR IntAct; P05555; 1.
DR STRING; 10090.ENSMUSP00000068468; -.
DR ChEMBL; CHEMBL3603; -.
DR GlyConnect; 2401; 3 N-Linked glycans (3 sites).
DR GlyGen; P05555; 16 sites, 3 N-linked glycans (3 sites).
DR PhosphoSitePlus; P05555; -.
DR EPD; P05555; -.
DR MaxQB; P05555; -.
DR PaxDb; P05555; -.
DR PeptideAtlas; P05555; -.
DR PRIDE; P05555; -.
DR ProteomicsDB; 268894; -. [P05555-1]
DR ProteomicsDB; 268895; -. [P05555-2]
DR ABCD; P05555; 8 sequenced antibodies.
DR MGI; MGI:96607; Itgam.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; P05555; -.
DR PhylomeDB; P05555; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
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 ChiTaRS; Itgam; mouse.
DR PRO; PR:P05555; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P05555; protein.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0034688; C:integrin alphaM-beta2 complex; IMP:ARUK-UCL.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0038024; F:cargo receptor activity; IGI:ARUK-UCL.
DR GO; GO:0001851; F:complement component C3b binding; IGI:ARUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA: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:0001846; F:opsonin binding; IDA:MGI.
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:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; IMP:ARUK-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0045123; P:cellular extravasation; IMP:MGI.
DR GO; GO:0150062; P:complement-mediated synapse pruning; IMP:ARUK-UCL.
DR GO; GO:0030900; P:forebrain development; IDA:ARUK-UCL.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0061756; P:leukocyte adhesion to vascular endothelial cell; IMP:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:MGI.
DR GO; GO:0014005; P:microglia development; IDA:MGI.
DR GO; GO:0001774; P:microglial cell activation; IMP:ARUK-UCL.
DR GO; GO:0045963; P:negative regulation of dopamine metabolic process; IDA:ARUK-UCL.
DR GO; GO:0001781; P:neutrophil apoptotic process; IMP:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:ARUK-UCL.
DR GO; GO:0110090; P:positive regulation of hippocampal neuron apoptotic process; IDA:ARUK-UCL.
DR GO; GO:0060376; P:positive regulation of mast cell differentiation; IMP:UniProtKB.
DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; IMP:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:ARUK-UCL.
DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; ISO:MGI.
DR GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IMP:ARUK-UCL.
DR GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; IMP:ARUK-UCL.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:ARUK-UCL.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:ARUK-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ARUK-UCL.
DR GO; GO:0150064; P:vertebrate eye-specific patterning; IMP:ARUK-UCL.
DR Gene3D; 2.130.10.130; -; 1.
DR Gene3D; 3.40.50.410; -; 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 InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 1.
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; 3.
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 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:3887182"
FT CHAIN 17..1153
FT /note="Integrin alpha-M"
FT /id="PRO_0000016290"
FT TOPO_DOM 17..1105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1106..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1130..1153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 18..75
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 76..135
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 164..338
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 339..390
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 391..442
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 443..503
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 506..564
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 569..629
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1132..1136
FT /note="GFFKR motif"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 533
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 537
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
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 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
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 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1022
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1051
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..73
FT /evidence="ECO:0000250"
FT DISULFID 105..123
FT /evidence="ECO:0000250"
FT DISULFID 654..711
FT /evidence="ECO:0000250"
FT DISULFID 770..776
FT /evidence="ECO:0000250"
FT DISULFID 999..1023
FT /evidence="ECO:0000250"
FT DISULFID 1028..1033
FT /evidence="ECO:0000250"
FT VAR_SEQ 453..569
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010473"
FT CONFLICT 37
FT /note="N -> S (in Ref. 2; BAC30350)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="V -> G (in Ref. 2; BAC30350)"
FT /evidence="ECO:0000305"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:6RHV"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6RHV"
FT STRAND 186..200
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:6RHV"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6RHV"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:6RHV"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:6RHV"
FT TURN 288..292
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:6RHV"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:6RHV"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6RHV"
SQ SEQUENCE 1153 AA; 127481 MW; 178DB988AECB0343 CRC64;
MTLKALLVTA LALCHGFNLD TEHPMTFQEN AKGFGQNVVQ LGGTSVVVAA PQEAKAVNQT
GALYQCDYST SRCHPIPLQV PPEAVNMSLG LSLAVSTVPQ QLLACGPTVH QNCKENTYVN
GLCYLFGSNL LRPPQQFPEA LRECPQQESD IVFLIDGSGS INNIDFQKMK EFVSTVMEQF
KKSKTLFSLM QYSDEFRIHF TFNDFKRNPS PRSHVSPIKQ LNGRTKTASG IRKVVRELFH
KTNGARENAA KILVVITDGE KFGDPLDYKD VIPEADRAGV IRYVIGVGNA FNKPQSRREL
DTIASKPAGE HVFQVDNFEA LNTIQNQLQE KIFAIEGTQT GSTSSFEHEM SQEGFSASIT
SNGPLLGSVG SFDWAGGAFL YTSKDKVTFI NTTRVDSDMN DAYLGYASAV ILRNRVQSLV
LGAPRYQHIG LVVMFRENFG TWEPHTSIKG SQIGSYFGAS LCSVDMDADG NTNLILIGAP
HYYEKTRGGQ VSVCPLPRGR ARWQCEALLH GDQGHPWGRF GAALTVLGDV NGDKLTDVAI
GAPGEQENQG AVYIFYGASI ASLSASHSHR IIGAHFSPGL QYFGQSLSGG KDLTMDGLMD
LAVGAQGHLL LLRAQPVLRL EATMEFSPKK VARSVFACQE QVLKNKDAGE VRVCLRVRKN
TKDRLREGDI QSTVTYDLAL DPVRSRIRAF FDETKNNTRR RTQVFGLMQK CETLKLILPD
CVDDSVSPII LRLNYTLVGE PLRSFGNLRP VLAMDAQRFF TAMFPFEKNC GNDSICQDDL
SITMSAMGLD TLVVGGPQDF NMSVTLRNDG EDSYGTQVTV YYPSGLSYRK DSASQNPLTK
KPWFVKPAES SSSSEGHGAL KSTTWNINHP IFPANSEVTF NVTFDVDSHA SFGNKLLLKA
IVASENNMSR THKTKFQLEL PVKYAIYMIV TSDESSIRYL NFTASEMTSK VIQHQYQFNN
LGQRSLPVSV VFWIPVQINN VTVWDHPQVI FSQNLSSACH TEQKSPPHSN FRDQLERTPV
LNCSVAVCKR IQCDLPSFNT QEIFNVTLKG NLSFDWYIKT SHGHLLLVSS TEILFNDSAF
ALLPGQESYV RSKTETKVEP YEVHNPVPLI VGSSIGGLVL LALITAGLYK LGFFKRQYKD
MMNEAAPQDA PPQ
