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TACT_RAT
ID   TACT_RAT                Reviewed;         603 AA.
AC   Q5BK49;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=T-cell surface protein tactile;
DE   AltName: Full=Cell surface antigen CD96;
DE   AltName: Full=T cell-activated increased late expression protein;
DE   AltName: CD_antigen=CD96;
DE   Flags: Precursor;
GN   Name=Cd96;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in adhesive interactions of activated T and
CC       NK cells during the late phase of the immune response. Promotes NK
CC       cell-target adhesion by interacting with PVR present on target cells.
CC       May function at a time after T and NK cells have penetrated the
CC       endothelium using integrins and selectins, when they are actively
CC       engaging diseased cells and moving within areas of inflammation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PVR (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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DR   EMBL; BC091206; AAH91206.1; -; mRNA.
DR   RefSeq; NP_001020203.1; NM_001025032.1.
DR   AlphaFoldDB; Q5BK49; -.
DR   STRING; 10116.ENSRNOP00000034871; -.
DR   GlyGen; Q5BK49; 16 sites.
DR   PaxDb; Q5BK49; -.
DR   Ensembl; ENSRNOT00000035485; ENSRNOP00000034871; ENSRNOG00000023030.
DR   GeneID; 498079; -.
DR   KEGG; rno:498079; -.
DR   UCSC; RGD:1565249; rat.
DR   CTD; 10225; -.
DR   RGD; 1565249; Cd96.
DR   eggNOG; ENOG502QWNP; Eukaryota.
DR   GeneTree; ENSGT00390000003446; -.
DR   HOGENOM; CLU_033543_1_0_1; -.
DR   InParanoid; Q5BK49; -.
DR   OMA; QHGFYCA; -.
DR   OrthoDB; 1115066at2759; -.
DR   PhylomeDB; Q5BK49; -.
DR   Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   PRO; PR:Q5BK49; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000023030; Expressed in testis and 11 other tissues.
DR   Genevisible; Q5BK49; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
DR   GO; GO:0002728; P:negative regulation of natural killer cell cytokine production; ISO:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR042381; CD96.
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   PANTHER; PTHR15317; PTHR15317; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..603
FT                   /note="T-cell surface protein tactile"
FT                   /id="PRO_0000313892"
FT   TOPO_DOM        22..537
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        538..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        559..603
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..132
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          139..245
FT                   /note="Ig-like V-type 2"
FT   DOMAIN          251..356
FT                   /note="Ig-like C2-type"
FT   REGION          359..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        161..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        272..336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   603 AA;  67228 MW;  8D46DDC0AE9B6840 CRC64;
     MGRKWTYCVV YAIIQIQFFR GAWEELFNAG DNNVYALPGS DVNLTCQTME KDLMVQMQWS
     KVTDEIDMIV VYHPQYGFHY MQGVACESRV AAVETLKDAT KWTLNLRNIS SSLSGKYECS
     FTMYPTGTKT IVYNLIVEPY TQDEHNRTIE IETNRTLEIP CFQNTSSEIS PRFTFSWLVE
     KDGVEDVLFT YDYHVSNSTA FKGRVGLGAD YGLRLSPVQI QDDGRTFSCF LRISPLKVWK
     TSTTVKVFAK PEILMTVENT TMDVLGERVF TCLLKNVFPK ASITWLIDGR LFQGNEEGIY
     ITNEEKNSSS GFWELKSVLT RMHNRTSQSN NMTVWCMALS PGPGNKMWNT SSQPITFSLD
     SGTAPTKRLP NVTGSTLGAQ TFPDAEVSPT RYLATSSMTI VDENVLTPDP TPQTSNSSMT
     TKDVNYSQPS SGTDAKNSSR AASSSDGGSR PFPSTSPPKW LSLPHTSTGP QEPDSAVSWI
     PTDAYTSGSS DASLTSHDVI IRTTKEFPDV LTTANGTTKI KHGHVTGITV NKPRDGMSWP
     VAVATLLFFC ILLFGLGVRK WCQYQKEIME RPPPFKPPPP PIKYMCIQEP TGRGMPCHEM
     EVL
 
 
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