ITAM_CAVPO
ID ITAM_CAVPO Reviewed; 126 AA.
AC P11578;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 105.
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: Fragment;
GN Name=ITGAM;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2833753; DOI=10.1073/pnas.85.8.2776;
RA Arnaout M.A., Remold-O'Donnell E., Pierce M.W., Harris P., Tenen D.G.;
RT "Molecular cloning of the alpha subunit of human and guinea pig leukocyte
RT adhesion glycoprotein Mo1: chromosomal localization and homology to the
RT alpha subunits of integrins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2776-2780(1988).
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. It is identical
CC with CR-3, the receptor for the iC3b fragment of the third complement
CC component. It probably recognizes the R-G-D peptide in C3b. Integrin
CC ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It
CC recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates
CC neutrophil migration. In association with beta subunit ITGB2/CD18,
CC required for CD177-PRTN3-mediated activation of TNF primed neutrophils.
CC May regulate phagocytosis-induced apoptosis in extravasated
CC neutrophils. May play a role in mast cell development. Required with
CC TYROBP/DAP12 in microglia to control production of microglial
CC superoxide ions which promote the neuronal apoptosis that occurs during
CC brain development. {ECO:0000250|UniProtKB:P05555,
CC ECO:0000250|UniProtKB:P11215}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. ITGAM associates
CC with ITGB2. Found in a complex with CD177 and ITGB2/CD18. Interacts
CC with JAM3. Interacts with THBD. {ECO:0000250|UniProtKB:P11215}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11215};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11215}.
CC Membrane raft {ECO:0000250|UniProtKB:P11215}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:P11215}.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; M19663; AAA37045.1; -; mRNA.
DR PIR; B30892; B30892.
DR AlphaFoldDB; P11578; -.
DR SMR; P11578; -.
DR STRING; 10141.ENSCPOP00000011658; -.
DR eggNOG; KOG3637; Eukaryota.
DR HOGENOM; CLU_1986516_0_0_1; -.
DR InParanoid; P11578; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; ISS:UniProtKB.
DR InterPro; IPR032695; Integrin_dom_sf.
DR SUPFAM; SSF69179; SSF69179; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Glycoprotein; Integrin; Membrane; Receptor;
KW Reference proteome.
FT CHAIN <1..>126
FT /note="Integrin alpha-M"
FT /id="PRO_0000174217"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 126
SQ SEQUENCE 126 AA; 14411 MW; 6063E140F4E1CA6B CRC64;
QLELPVKYAV YLIVTSGEAS TTYLNFTTSE KTIQTMKHQY KFTNLGKRSL PISVVFWVPV
RLNNEIVWDR PQVTFSPNLS SACNTEERSP PHSDFLAELE KTHVLNCSIA VCQRIACDIP
YFNIQE