ICAM3_PANTR
ID ICAM3_PANTR Reviewed; 547 AA.
AC Q5NKU6; Q5NKU5; Q5NKU7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Intercellular adhesion molecule 3;
DE Short=ICAM-3;
DE AltName: CD_antigen=CD50;
DE Flags: Precursor;
GN Name=ICAM3;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-537.
RC STRAIN=Isolate Bonnie, Isolate Caesar, and Isolate Deca; TISSUE=Blood;
RA Messier W., Walter N.A.R., Hink R.L.;
RT "The chimpanzee ICAM proteins have been positively selected.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000250|UniProtKB:P32942}.
CC -!- PTM: Upon stimulation by a physiologic stimuli becomes rapidly and
CC transiently phosphorylated on serine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
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DR EMBL; AF340055; AAQ14912.1; -; mRNA.
DR EMBL; AF340056; AAQ14913.1; -; mRNA.
DR EMBL; AF340057; AAQ14914.1; -; mRNA.
DR RefSeq; NP_001009167.1; NM_001009167.1.
DR AlphaFoldDB; Q5NKU6; -.
DR SMR; Q5NKU6; -.
DR STRING; 9598.ENSPTRP00000017837; -.
DR PaxDb; Q5NKU6; -.
DR GeneID; 494138; -.
DR KEGG; ptr:494138; -.
DR CTD; 3385; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR InParanoid; Q5NKU6; -.
DR OrthoDB; 731140at2759; -.
DR Proteomes; UP000002277; 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; IPR007110; Ig-like_dom.
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; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phagocytosis; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..547
FT /note="Intercellular adhesion molecule 3"
FT /id="PRO_0000014795"
FT TOPO_DOM 30..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..103
FT /note="Ig-like C2-type 1"
FT DOMAIN 132..197
FT /note="Ig-like C2-type 2"
FT DOMAIN 234..301
FT /note="Ig-like C2-type 3"
FT DOMAIN 329..382
FT /note="Ig-like C2-type 4"
FT DOMAIN 416..469
FT /note="Ig-like C2-type 5"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 57..100
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT DISULFID 139..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 241..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 336..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 423..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 537
FT /note="Q -> E (in strain: Isolate Deca)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_021253"
SQ SEQUENCE 547 AA; 59533 MW; 5A57BAFD2D0C4CB3 CRC64;
MATMVPSVLW PRACWTLLVC CLLTPGVQGQ EFLLRVEPQN PVLSAGGSLF VNCSTDCPSS
EKIALETSLS KELVASGMGW AAFNLSNVTG NSRILCSVYC NGSQITGSSN ITVYRLPERV
ELAPLPPWQR VGQNFTLRCQ VEGGSPRTSL TVVLLRWEEE LSRQPAVEEP AEVTATVLAS
RDDHGAPFSC RTELDMQPQG LGLFVNTSAP RQLRTFVLPV TPPRLVAPRF LEVETSWPVD
CTLDGLFPAS EAQVYLALGD QMLNATVMNH GDTLTATATA TARADQEGAR EIVCNVTLGG
ERREARENLT VFSFLGPTVN LSEPTAPEGS TVTVSCMAGA RVQVTLDGVP AAAPGQPAQL
QLNATESDDR RSFFCSATLE VDGEFLHRNS SVQLRVLYGP KIDRATCPQH LKWKDKTTHV
LQCQARGNPY PELRCLKEGS SREVPVGIPF FVNVTHNGTY QCQASSSRGK YTLVVVMDIE
AGSSHFVPVF VAVLLTLGVV TIVLALMYVF REHKRSGSYH VREESTYLPL TSMQPTQAMG
EEPSRAE
