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CLM5_MOUSE
ID   CLM5_MOUSE              Reviewed;         221 AA.
AC   Q8VCH2; Q8BRU3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=CMRF35-like molecule 5 {ECO:0000303|PubMed:14662855};
DE            Short=CLM-5 {ECO:0000303|PubMed:14662855};
DE   AltName: Full=CD300 antigen like family member D;
DE   AltName: Full=Leukocyte mono-Ig-like receptor 4 {ECO:0000303|PubMed:17438331};
DE   AltName: Full=Myeloid-associated immunoglobulin-like receptor 4;
DE            Short=MAIR-4;
DE            Short=MAIR-IV;
DE   Flags: Precursor;
GN   Name=Cd300ld {ECO:0000312|MGI:MGI:2442358};
GN   Synonyms=Clm5 {ECO:0000303|PubMed:14662855},
GN   Lmir4 {ECO:0000303|PubMed:17438331};
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=14662855; DOI=10.4049/jimmunol.171.12.6541;
RA   Chung D.-H., Humphrey M.B., Nakamura M.C., Ginzinger D.G., Seaman W.E.,
RA   Daws M.R.;
RT   "CMRF-35-like molecule-1, a novel mouse myeloid receptor, can inhibit
RT   osteoclast formation.";
RL   J. Immunol. 171:6541-6548(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION,
RP   AND INTERACTION WITH FCER1G.
RC   STRAIN=CBA/J;
RX   PubMed=17438331; DOI=10.1074/jbc.m701100200;
RA   Izawa K., Kitaura J., Yamanishi Y., Matsuoka T., Oki T., Shibata F.,
RA   Kumagai H., Nakajima H., Maeda-Yamamoto M., Hauchins J.P., Tybulewicz V.L.,
RA   Takai T., Kitamura T.;
RT   "Functional analysis of activating receptor LMIR4 as a counterpart of
RT   inhibitory receptor LMIR3.";
RL   J. Biol. Chem. 282:17997-18008(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   FCER1G.
RX   PubMed=16940041; DOI=10.1093/intimm/dxl083;
RA   Fujimoto M., Takatsu H., Ohno H.;
RT   "CMRF-35-like molecule-5 constitutes novel paired receptors, with CMRF-35-
RT   like molecule-1, to transduce activation signal upon association with
RT   FcRgamma.";
RL   Int. Immunol. 18:1499-1508(2006).
RN   [6]
RP   INTERACTION WITH FCER1G, AND MUTAGENESIS OF 165-SER--ARG-170 AND
RP   177-TYR--LEU-186.
RX   PubMed=20817736; DOI=10.1074/jbc.m110.137166;
RA   Enomoto Y., Yamanishi Y., Izawa K., Kaitani A., Takahashi M., Maehara A.,
RA   Oki T., Takamatsu R., Kajikawa M., Takai T., Kitamura T., Kitaura J.;
RT   "Characterization of leukocyte mono-immunoglobulin-like receptor 7
RT   (LMIR7)/CLM-3 as an activating receptor: its similarities to and
RT   differences from LMIR4/CLM-5.";
RL   J. Biol. Chem. 285:35274-35283(2010).
RN   [7]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=27681626; DOI=10.1073/pnas.1605575113;
RA   Haga K., Fujimoto A., Takai-Todaka R., Miki M., Doan Y.H., Murakami K.,
RA   Yokoyama M., Murata K., Nakanishi A., Katayama K.;
RT   "Functional receptor molecules CD300lf and CD300ld within the CD300 family
RT   enable murine noroviruses to infect cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E6248-E6255(2016).
RN   [8]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=27540007; DOI=10.1126/science.aaf1220;
RA   Orchard R.C., Wilen C.B., Doench J.G., Baldridge M.T., McCune B.T.,
RA   Lee Y.C., Lee S., Pruett-Miller S.M., Nelson C.A., Fremont D.H.,
RA   Virgin H.W.;
RT   "Discovery of a proteinaceous cellular receptor for a norovirus.";
RL   Science 353:933-936(2016).
CC   -!- FUNCTION: Acts as an activating receptor in myeloid cells and mast
CC       cells. {ECO:0000269|PubMed:16940041, ECO:0000269|PubMed:17438331}.
CC   -!- FUNCTION: (Microbial infection) Acts as a functional murine norovirus
CC       (MNV) receptor. Primary determinant of MNV species tropism and is
CC       sufficient to render cells permissive to infection by MNV. Can render
CC       nonmurine mammalian cells susceptible to MNV infection
CC       (PubMed:27681626, PubMed:27540007). {ECO:0000269|PubMed:27540007,
CC       ECO:0000269|PubMed:27681626}.
CC   -!- SUBUNIT: Interacts with FCER1G. {ECO:0000269|PubMed:16940041,
CC       ECO:0000269|PubMed:17438331, ECO:0000269|PubMed:20817736}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16940041};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:16940041}.
CC   -!- TISSUE SPECIFICITY: Expressed in dendritic cells, macrophages and
CC       granulocytes. Present on the surface of granulocytes and
CC       monocytes/macrophages (at protein level). {ECO:0000269|PubMed:16940041,
CC       ECO:0000269|PubMed:17438331}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:17438331}.
CC   -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR   EMBL; AY457051; AAR27942.1; -; mRNA.
DR   EMBL; AB292062; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK041292; BAC30893.1; -; mRNA.
DR   EMBL; BC019814; AAH19814.1; -; mRNA.
DR   CCDS; CCDS25615.1; -.
DR   RefSeq; NP_663412.1; NM_145437.2.
DR   AlphaFoldDB; Q8VCH2; -.
DR   SMR; Q8VCH2; -.
DR   STRING; 10090.ENSMUSP00000047022; -.
DR   iPTMnet; Q8VCH2; -.
DR   PhosphoSitePlus; Q8VCH2; -.
DR   MaxQB; Q8VCH2; -.
DR   PaxDb; Q8VCH2; -.
DR   PRIDE; Q8VCH2; -.
DR   ProteomicsDB; 283526; -.
DR   DNASU; 217305; -.
DR   Ensembl; ENSMUST00000045075; ENSMUSP00000047022; ENSMUSG00000034641.
DR   GeneID; 217305; -.
DR   KEGG; mmu:217305; -.
DR   UCSC; uc007mgd.2; mouse.
DR   CTD; 100131439; -.
DR   MGI; MGI:2442358; Cd300ld.
DR   VEuPathDB; HostDB:ENSMUSG00000034641; -.
DR   eggNOG; ENOG502S8BD; Eukaryota.
DR   GeneTree; ENSGT00940000154332; -.
DR   HOGENOM; CLU_051023_3_0_1; -.
DR   InParanoid; Q8VCH2; -.
DR   OMA; CAVIWMS; -.
DR   OrthoDB; 1494510at2759; -.
DR   PhylomeDB; Q8VCH2; -.
DR   TreeFam; TF334441; -.
DR   BioGRID-ORCS; 217305; 4 hits in 72 CRISPR screens.
DR   PRO; PR:Q8VCH2; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8VCH2; protein.
DR   Bgee; ENSMUSG00000034641; Expressed in granulocyte and 57 other tissues.
DR   Genevisible; Q8VCH2; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0032675; P:regulation of interleukin-6 production; IDA:MGI.
DR   GO; GO:0032680; P:regulation of tumor necrosis factor production; IDA:MGI.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Host cell receptor for virus entry;
KW   Immunity; Immunoglobulin domain; Membrane; Receptor; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..221
FT                   /note="CMRF35-like molecule 5"
FT                   /id="PRO_0000320128"
FT   TOPO_DOM        19..177
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        199..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          19..124
FT                   /note="Ig-like V-type"
FT   REGION          38..48
FT                   /note="May play an important role in murine norovirus (MNV)
FT                   binding"
FT                   /evidence="ECO:0000269|PubMed:27681626"
FT   REGION          165..170
FT                   /note="Important for maintaining surface expression and for
FT                   interaction with FCER1G"
FT   REGION          177..186
FT                   /note="Important for maintaining surface expression and for
FT                   interaction with FCER1G"
FT   DISULFID        40..108
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         165..170
FT                   /note="SRPHTR->NSLFIW: Decreases surface expression in
FT                   transfected pro-B cells and impairs interaction with
FT                   FCER1G."
FT                   /evidence="ECO:0000269|PubMed:20817736"
FT   MUTAGEN         177..186
FT                   /note="YFLLMVFVEL->SFLLMVFVVV: Increases surface expression
FT                   in transfected pro-B cells and impairs interaction with
FT                   FCER1G."
FT                   /evidence="ECO:0000269|PubMed:20817736"
FT   CONFLICT        20..21
FT                   /note="DS -> NP (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41..48
FT                   /note="RYSSYWKG -> QYTSDWKD (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="R -> Q (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="R -> K (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63..66
FT                   /note="DILV -> VFLI (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="D -> E (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="T -> I (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113..118
FT                   /note="GGPDPM -> AGYDPV (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124..127
FT                   /note="NIDQ -> SINP (in Ref. 2; AB292062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="L -> P (in Ref. 3; BAC30893)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   221 AA;  24954 MW;  C9E6203BE64922C1 CRC64;
     MWQFSALLLF FLPGCCTAQD SVTGPEEVSG QEQGSLTVQC RYSSYWKGYK KYWCRGVPQR
     SCDILVETDK SEQLVKKNRV SIRDNQRDFI FTVTMEDLRM SDAGIYWCGI TKGGPDPMFK
     VNVNIDQAPK SSMMTTTATV LKSIQPSAEN TGKEQVTQSK EVTQSRPHTR SLLSSIYFLL
     MVFVELPLLL SMLSAVLWVT RPQRCFGRGE NDLVKTHSPV A
 
 
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