ICAM3_BOVIN
ID ICAM3_BOVIN Reviewed; 544 AA.
AC Q28125;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Intercellular adhesion molecule 3;
DE Short=ICAM-3;
DE AltName: CD_antigen=CD50;
DE Flags: Precursor;
GN Name=ICAM3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Lymph node, and Mammary gland;
RX PubMed=8890753; DOI=10.1016/0378-1119(96)00082-0;
RA Lee E.K., Kehrli M.E. Jr., Dietz A.B., Bosworth B.T., Reinhardt T.A.;
RT "Cloning and sequencing of a cDNA encoding bovine intercellular adhesion
RT molecule 3 (ICAM-3).";
RL Gene 174:311-313(1996).
CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein
CC LFA-1 (integrin alpha-L/beta-2). ICAM3 is also a ligand for integrin
CC alpha-D/beta-2. In association with integrin alpha-L/beta-2,
CC contributes to apoptotic neutrophil phagocytosis by macrophages.
CC {ECO:0000250|UniProtKB:P32942}.
CC -!- SUBUNIT: Interacts with moesin/MSN. {ECO:0000250|UniProtKB:P32942}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000250|UniProtKB:P32942}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
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DR EMBL; L41844; AAB39264.1; -; mRNA.
DR PIR; JC5018; JC5018.
DR RefSeq; NP_776774.1; NM_174349.1.
DR AlphaFoldDB; Q28125; -.
DR SMR; Q28125; -.
DR STRING; 9913.ENSBTAP00000020903; -.
DR PaxDb; Q28125; -.
DR PRIDE; Q28125; -.
DR GeneID; 281840; -.
DR KEGG; bta:281840; -.
DR CTD; 3385; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR InParanoid; Q28125; -.
DR OrthoDB; 731140at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phagocytosis; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..544
FT /note="Intercellular adhesion molecule 3"
FT /id="PRO_0000014793"
FT TOPO_DOM 32..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..200
FT /note="Ig-like C2-type 2"
FT DOMAIN 237..302
FT /note="Ig-like C2-type 3"
FT DOMAIN 330..383
FT /note="Ig-like C2-type 4"
FT DOMAIN 417..470
FT /note="Ig-like C2-type 5"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..98
FT /evidence="ECO:0000250|UniProtKB:P32942,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 59..102
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT DISULFID 141..193
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT DISULFID 244..295
FT /evidence="ECO:0000255"
FT DISULFID 337..376
FT /evidence="ECO:0000255"
FT DISULFID 424..463
FT /evidence="ECO:0000255"
SQ SEQUENCE 544 AA; 59735 MW; 63EA8C70913C2DF0 CRC64;
MIASGPPPRV YWTSLIFLLL ACCLLPTGAQ GQTYQVRVEP KDPVVPFGEP LVVNCTLDCP
GPGLISLETA LSKEPHSRGL GWAAFRLTNV TGDMEILCSG ICNKSQVVGF SNITVFGFPK
RVELAPLPLW QPVGEELNLS CLVSGGAPRA HLSVVLLRGE EELGRQPLGK EEPAKVTFMV
QPRREDHGTN FSCRSELDLR SQGLELFQNT SAPRKLQTYA MPKTAPRLVF PRFWEMETSW
PVNCSLNGLF PASEAHIQLA LGNQMLNATV VSHADTLTAT ATAKTEQEGT QEIVCNVTLG
VENRETRESL VAYRFQGPNL NLSESNATEG TPVTVTCAAG PQVQVMLDGV PAAVPGQPAQ
LQLKATEMDD RRTFFCNATL KVHGVTLHRN RSIQLRVLYG PTIDRAKCPQ RLMWKEKTMH
ILQCQARGNP NPQLQCLREG SKFKVPVGIP FLVLLNYSGT YSCQAASSRG TDKMLVMMDV
QGRNPVTINI VLGVLAILGL VTLAAASVYV FWVQRQHDIY HLTPRSTRWR LTSTQPVTVA
EELS
