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NCTR1_MOUSE
ID   NCTR1_MOUSE             Reviewed;         325 AA.
AC   Q8C567; Q1RLN4; Q80UY6; Q9Z0Q4;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Natural cytotoxicity triggering receptor 1;
DE   AltName: Full=Activating receptor 1;
DE            Short=mAR-1;
DE   AltName: Full=Lymphocyte antigen 94;
DE   AltName: Full=Natural killer cell p46-related protein;
DE            Short=NK-p46;
DE            Short=NKp46;
DE            Short=mNKp46;
DE   AltName: CD_antigen=CD335;
DE   Flags: Precursor;
GN   Name=Ncr1; Synonyms=Ly94;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Lymphoid tissue;
RX   PubMed=10092106;
RX   DOI=10.1002/(sici)1521-4141(199903)29:03<1014::aid-immu1014>3.0.co;2-o;
RA   Biassoni R., Pessino A., Bottino C., Pende D., Moretta L., Moretta A.;
RT   "The murine homologue of the human NKp46, a triggering receptor involved in
RT   the induction of natural cytotoxicity.";
RL   Eur. J. Immunol. 29:1014-1020(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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: Cytotoxicity-activating receptor that may contribute to the
CC       increased efficiency of activated natural killer (NK) cells to mediate
CC       tumor cell lysis. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CD3Z and FCER1G. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8C567; P27918: CFP; Xeno; NbExp=2; IntAct=EBI-11707971, EBI-9038570;
CC       Q8C567; PRO_0000035863 [P27918]: CFP; Xeno; NbExp=3; IntAct=EBI-11707971, EBI-15183949;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Selectively expressed by NK cells.
CC       {ECO:0000269|PubMed:10092106}.
CC   -!- SIMILARITY: Belongs to the natural cytotoxicity receptor (NCR) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ223765; CAB39169.1; -; mRNA.
DR   EMBL; AK079401; BAC37635.1; -; mRNA.
DR   EMBL; BC042788; AAH42788.1; -; mRNA.
DR   EMBL; BC115364; AAI15365.1; -; mRNA.
DR   CCDS; CCDS20734.1; -.
DR   RefSeq; NP_034876.2; NM_010746.3.
DR   AlphaFoldDB; Q8C567; -.
DR   SMR; Q8C567; -.
DR   IntAct; Q8C567; 3.
DR   STRING; 10090.ENSMUSP00000006792; -.
DR   GlyGen; Q8C567; 3 sites.
DR   PhosphoSitePlus; Q8C567; -.
DR   PaxDb; Q8C567; -.
DR   PRIDE; Q8C567; -.
DR   ProteomicsDB; 287460; -.
DR   DNASU; 17086; -.
DR   GeneID; 17086; -.
DR   KEGG; mmu:17086; -.
DR   UCSC; uc009exi.1; mouse.
DR   CTD; 9437; -.
DR   MGI; MGI:1336212; Ncr1.
DR   eggNOG; ENOG502RWVC; Eukaryota.
DR   InParanoid; Q8C567; -.
DR   OrthoDB; 1327293at2759; -.
DR   PhylomeDB; Q8C567; -.
DR   TreeFam; TF336644; -.
DR   BioGRID-ORCS; 17086; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q8C567; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8C567; protein.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR   GO; GO:0009597; P:detection of virus; IMP:MGI.
DR   Gene3D; 2.60.40.10; -; 2.
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; PF13895; Ig_2; 1.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..325
FT                   /note="Natural cytotoxicity triggering receptor 1"
FT                   /id="PRO_0000015029"
FT   TOPO_DOM        17..255
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..325
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          34..118
FT                   /note="Ig-like 1"
FT   DOMAIN          129..211
FT                   /note="Ig-like 2"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..98
FT                   /evidence="ECO:0000250|UniProtKB:O76036"
FT   DISULFID        144..190
FT                   /evidence="ECO:0000250|UniProtKB:O76036"
FT   CONFLICT        131
FT                   /note="R -> Q (in Ref. 2; BAC37635)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  37266 MW;  ED24E48ABF22F029 CRC64;
     MLPTLTALLC LGLCLSQRIN TEKETLPKPI IWAKPSIMVT NGNSVNIWCQ GAQSASEYQL
     YFEGSFFALE RPKPSRSMNK VRFFISQMTS HTAGIYTCFY QSGELWSKSS NPLKLVVTGL
     YDTPNLWVYP RPEVTLGENV TFFCQLKTAT SKFFLLKERG SNHIQNKYGN IQAEFPMGPV
     TRAHRGTYRC FGSYNDYAWS FPSEPVTLLI TGGVENSSLA PTDPTSSLDY WEFDLSTNES
     GLQKDSAFWD HTTQNLIRIG LACIILITLV WLLTEDWLSK RKDHEEANRL TNWECRRRWR
     MQHYFEEEQR NAISMMELKA TPGAL
 
 
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