ICAM4_PANTR
ID ICAM4_PANTR Reviewed; 269 AA.
AC Q5NKT8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Intercellular adhesion molecule 4;
DE Short=ICAM-4;
DE AltName: CD_antigen=CD242;
DE Flags: Precursor; Fragment;
GN Name=ICAM4;
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].
RC STRAIN=Isolate Bonnie; 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). ICAM4 is also a ligand for alpha-
CC 4/beta-1 and alpha-V integrins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ERM2};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
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DR EMBL; AF340064; AAQ14921.1; -; mRNA.
DR RefSeq; NP_001181868.1; NM_001194939.1.
DR AlphaFoldDB; Q5NKT8; -.
DR SMR; Q5NKT8; -.
DR STRING; 9598.ENSPTRP00000054779; -.
DR PaxDb; Q5NKT8; -.
DR GeneID; 455698; -.
DR KEGG; ptr:455698; -.
DR CTD; 3386; -.
DR eggNOG; ENOG502TF7V; Eukaryota.
DR InParanoid; Q5NKT8; -.
DR OrthoDB; 1345330at2759; -.
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 Gene3D; 2.60.40.10; -; 2.
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 Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL <1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..269
FT /note="Intercellular adhesion molecule 4"
FT /id="PRO_0000014798"
FT TOPO_DOM 21..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..122
FT /note="Ig-like C2-type 1"
FT DOMAIN 144..215
FT /note="Ig-like C2-type 2"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..115
FT /evidence="ECO:0000250"
FT DISULFID 67..111
FT /evidence="ECO:0000250|UniProtKB:P32942,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 71..115
FT /evidence="ECO:0000250|UniProtKB:P32942"
FT DISULFID 151..208
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 269 AA; 29109 MW; E6AB57AAFC43CFCF CRC64;
SLFPLSLLFF LAAAYPGVGS ALGRRTKRAQ SPKGSPLAPS GTSVPFWVRM SPEFVAVQPG
KSVQLNCSNS CPQPQNSSLR TPLRQGKTLR GPGWVSYQLL DVRAWSSLAH CLVTCAGKTR
WATSRITAYK PPHSVILEPP VLKGRKYTLR CHVTQVFPVG YLVVTLRHGS RVIYSESLER
FTGLDLANVT LTYEFAAGPR DFWQPVICHA RLNLDGLVVR NSSAPITLML AWSSAPTALA
SVSIAALVGI LLTVGAAYLC KCLAMKSQA
