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
