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CD1D_PANTR
ID   CD1D_PANTR              Reviewed;         335 AA.
AC   Q4ACW4; Q4ACU8;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Antigen-presenting glycoprotein CD1d;
DE   AltName: CD_antigen=CD1d;
DE   Flags: Precursor;
GN   Name=CD1D;
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 [GENOMIC DNA].
RX   PubMed=16305684; DOI=10.1111/j.1399-0039.2005.00504.x;
RA   Saito N., Takahashi M., Akahata W., Ido E., Hidaka C., Ibuki K., Miura T.,
RA   Hayami M., Takahashi H.;
RT   "Analysis of evolutionary conservation in CD1d molecules among primates.";
RL   Tissue Antigens 66:674-682(2005).
CC   -!- FUNCTION: Antigen-presenting protein that binds self and non-self
CC       glycolipids and presents them to T-cell receptors on natural killer T-
CC       cells. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with
CC       MHC II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15813};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15813}.
CC       Basolateral cell membrane {ECO:0000250|UniProtKB:P15813}; Single-pass
CC       type I membrane protein {ECO:0000250|UniProtKB:P15813}. Endosome
CC       membrane {ECO:0000250|UniProtKB:P15813}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P15813}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:P15813}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P15813}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P15813}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P15813}. Note=Subject to intracellular
CC       trafficking between the cell membrane, endosomes and lysosomes.
CC       {ECO:0000250|UniProtKB:P15813}.
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DR   EMBL; AB222997; BAE16552.2; -; Genomic_DNA.
DR   EMBL; AB222998; BAE16553.1; -; Genomic_DNA.
DR   EMBL; AB223044; BAE16753.2; -; Genomic_DNA.
DR   RefSeq; NP_001065272.1; NM_001071804.1.
DR   RefSeq; XP_009432153.2; XM_009433878.2.
DR   AlphaFoldDB; Q4ACW4; -.
DR   SMR; Q4ACW4; -.
DR   STRING; 9598.ENSPTRP00000002527; -.
DR   PaxDb; Q4ACW4; -.
DR   GeneID; 469524; -.
DR   KEGG; ptr:469524; -.
DR   CTD; 912; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   HOGENOM; CLU_047501_9_2_1; -.
DR   InParanoid; Q4ACW4; -.
DR   OrthoDB; 827472at2759; -.
DR   TreeFam; TF336723; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0030883; F:endogenous lipid antigen binding; IBA:GO_Central.
DR   GO; GO:0030884; F:exogenous lipid antigen binding; ISS:UniProtKB.
DR   GO; GO:0030882; F:lipid antigen binding; ISS:UniProtKB.
DR   GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
DR   GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; ISS:UniProtKB.
DR   GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF16497; MHC_I_3; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Endoplasmic reticulum; Endosome; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Innate immunity; Lysosome; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..335
FT                   /note="Antigen-presenting glycoprotein CD1d"
FT                   /id="PRO_0000042220"
FT   TOPO_DOM        20..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..335
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          185..292
FT                   /note="Ig-like"
FT   MOTIF           331..334
FT                   /note="Internalization signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="a D-galactosylceramide"
FT                   /ligand_id="ChEBI:CHEBI:36498"
FT                   /evidence="ECO:0000250|UniProtKB:P15813"
FT   BINDING         169..172
FT                   /ligand="a D-galactosylceramide"
FT                   /ligand_id="ChEBI:CHEBI:36498"
FT                   /evidence="ECO:0000250|UniProtKB:P15813"
FT   BINDING         169
FT                   /ligand="a D-galactosylceramide"
FT                   /ligand_id="ChEBI:CHEBI:36498"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="a D-galactosylceramide"
FT                   /ligand_id="ChEBI:CHEBI:36498"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   335 AA;  37758 MW;  2F90B2741110001D CRC64;
     MGCLLFLLLW ALLQAWGSAE VPQRLFPLRC LQISSFANSS WTRTDGLAWL GELQTHSWSN
     DSDTVRSLKP WSQGTFSDQQ WETLQHIFRV YRSSFTRDVK EFAKMLRLSY PLELQVSAGC
     EVHPGNASNN FFHVAFQGKD ILSFQGTSWE PTQEAPLWVN LAIQVLNQDK WTRETVQWLL
     NGTCPQFVSG LLESGKSELE KQVKPKAWLS RGPSPGPGRL LLVCHVSGFY PKPVWVKWMR
     GEQEQQDTQP GDILPNADET WYLRATLDVA AGEAAGLSCR VKHSSLEGQD IILYWGGSYT
     SVGLIVLAVL ACLLFLLIVG FTSRFKRQTS YQGVL
 
 
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