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Database: UniProt
Entry: H9G1S6_MACMU
LinkDB: H9G1S6_MACMU
Original site: H9G1S6_MACMU 
ID   H9G1S6_MACMU            Unreviewed;       458 AA.
AC   H9G1S6;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=T-cell surface glycoprotein CD4 {ECO:0000256|ARBA:ARBA00016522};
DE   AltName: Full=T-cell surface antigen T4/Leu-3 {ECO:0000256|ARBA:ARBA00029974};
GN   Name=CD4 {ECO:0000313|EMBL:AFE80835.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE80835.1};
RN   [1] {ECO:0000313|EMBL:AFE80835.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE80835.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [2] {ECO:0000313|EMBL:AXC25036.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2 {ECO:0000313|EMBL:AXC25036.1};
RA   Warren C.J., Meyerson N.R., Stabell A.C., Wilkerson G.K., Sawyer S.L.;
RT   "The CD4 receptor restricts cellular entry of HIV-1 in nonhuman primates.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Forms disulfide-linked homodimers at the cell surface.
CC       Interacts with LCK. Interacts with PTK2/FAK1. Binds to P4HB/PDI.
CC       Interacts with IL16; this interaction induces a CD4-dependent signaling
CC       in lymphocytes. Interacts (via Ig-like V-type domain) with MHCII alpha
CC       chain (via alpha-2 domain) and beta chain (via beta-2 domain); this
CC       interaction increases the affinity of TCR for peptide-MHCII. CD4
CC       oligomerization via Ig-like C2-type 2 and 3 domains appears to be
CC       required for stable binding to MHCII and adhesion between T cells and
CC       APCs. {ECO:0000256|ARBA:ARBA00024047}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; JU337082; AFE80835.1; -; mRNA.
DR   EMBL; MF632287; AXC25036.1; -; mRNA.
DR   AlphaFoldDB; H9G1S6; -.
DR   SMR; H9G1S6; -.
DR   GO; GO:0009986; C:cell surface; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd22570; CD4_CD; 1.
DR   CDD; cd07695; IgV_3_CD4; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 1.20.5.900; transmembrane domain of human cd4; 1.
DR   InterPro; IPR000973; CD4.
DR   InterPro; IPR015274; CD4-extracel.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008424; Ig_C2-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR021963; Tcell_CD4_Cterm.
DR   PANTHER; PTHR11422; T-CELL SURFACE GLYCOPROTEIN CD4; 1.
DR   PANTHER; PTHR11422:SF0; T-CELL SURFACE GLYCOPROTEIN CD4; 1.
DR   Pfam; PF05790; C2-set; 2.
DR   Pfam; PF09191; CD4-extracel; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF12104; Tcell_CD4_C; 1.
DR   PRINTS; PR00692; CD4TCANTIGEN.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..458
FT                   /note="T-cell surface glycoprotein CD4"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033698389"
FT   TRANSMEM        397..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..121
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   458 AA;  50858 MW;  4103862905AA4614 CRC64;
     MNRGIPFRHL LLVLQLALLP AVTQGKKVVL GKKGDTVELT CNASQKKNTQ FHWKNSNQIK
     ILGIQGSFLT KGPSKLSDRA DSRKSLWDQG CFSMIIKNLK IEDSDTYICE VENKKEEVEL
     LVFGLTANSD THLLEGQSLT LTLESPPGSS PSVKCRSPGG KNIQGGRTLS VPQLERQDSG
     TWTCTVSQDQ KTVEFKIDIV VLAFQKASST VYKKEGEQVE FSFPLAFTLE KLTGSGELWW
     QAERASSSKS WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA
     LEAKTGKLHQ EVNLVVMRAT QFQENLTCEV WGPTSPKLTL SLKLENKGAT VSKQAKAVWV
     LNPEAGMWQC LLSDSGQVLL ESNIKVVPTW PTPVQPMALI VLGGVAGLLL FTGLGIFFCV
     RCRHRRRQAE RMSQIKRLLS EKKTCQCPHR FQKTCSPI
//
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