CLM9_MOUSE
ID CLM9_MOUSE Reviewed; 331 AA.
AC Q1ERP8; A2A503; Q1ERP9; Q1ERQ0; Q3UU12; Q6SJP9; Q9D7B8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=CMRF35-like molecule 9;
DE Short=CLM-9;
DE AltName: Full=CD300 antigen-like family member G;
DE AltName: Full=Nepmucin;
DE AltName: CD_antigen=CD300g;
DE Flags: Precursor;
GN Name=Cd300lg; Synonyms=Clm9, D11Ertd736e;
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] (ISOFORM 5), AND TISSUE SPECIFICITY.
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] (ISOFORMS 1; 2; 3 AND 5), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=C57BL/6J; TISSUE=Lymph node;
RX PubMed=16754720; DOI=10.1084/jem.20052543;
RA Umemoto E., Tanaka T., Kanda H., Jin S., Tohya K., Otani K., Matsutani T.,
RA Matsumoto M., Ebisuno Y., Jang M.H., Fukuda M., Hirata T., Miyasaka M.;
RT "Nepmucin, a novel HEV sialomucin, mediates L-selectin-dependent lymphocyte
RT rolling and promotes lymphocyte adhesion under flow.";
RL J. Exp. Med. 203:1603-1614(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16876123; DOI=10.1016/j.bbrc.2006.07.047;
RA Takatsu H., Hase K., Ohmae M., Ohshima S., Hashimoto K., Taniura N.,
RA Yamamoto A., Ohno H.;
RT "CD300 antigen like family member G: a novel Ig receptor like protein
RT exclusively expressed on capillary endothelium.";
RL Biochem. Biophys. Res. Commun. 348:183-191(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Tongue, and Vein;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor which may mediate L-selectin-dependent lymphocyte
CC rollings. Binds SELL in a calcium dependent manner. Binds lymphocyte.
CC {ECO:0000269|PubMed:16754720, ECO:0000269|PubMed:16876123}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:16754720, ECO:0000269|PubMed:16876123}; Single-pass
CC type I membrane protein {ECO:0000305|PubMed:16754720}. Basolateral cell
CC membrane {ECO:0000269|PubMed:16754720, ECO:0000269|PubMed:16876123};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:16754720}.
CC Endosome, multivesicular body membrane {ECO:0000269|PubMed:16876123};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:16754720}.
CC Note=Exclusively localized on capillary endothelium. Transcytoses
CC across the cytoplasm in the capillary endothelium.
CC {ECO:0000269|PubMed:16876123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=isoform C, CD300LG-beta;
CC IsoId=Q1ERP8-1; Sequence=Displayed;
CC Name=2; Synonyms=isoform B, CD300LG-gamma;
CC IsoId=Q1ERP8-2; Sequence=VSP_028413;
CC Name=3; Synonyms=isoform A, CD300LG-delta;
CC IsoId=Q1ERP8-3; Sequence=VSP_028415;
CC Name=4;
CC IsoId=Q1ERP8-4; Sequence=VSP_028413, VSP_028416, VSP_028417;
CC Name=5; Synonyms=isoform D, CD300LG-alpha;
CC IsoId=Q1ERP8-5; Sequence=VSP_028414;
CC -!- TISSUE SPECIFICITY: Expressed in monocyte cell lines. Expressed in
CC certain types of endothelial and myeloid lineage cells. Expressed in
CC mesenteric lymph nodes (LNs), spleen, thymus, lung, heart and kidney.
CC Expressed in high endothelial venules (HEVs) in peripheral and
CC mesenteric LNs (at protein level). Highly expressed in heart. Slightly
CC expressed in spleen and thymus. Isoform 5 is expressed preferentially
CC in heart. Isoform 1 is expressed predominantly in kidney and liver.
CC {ECO:0000269|PubMed:14662855, ECO:0000269|PubMed:16754720,
CC ECO:0000269|PubMed:16876123}.
CC -!- DOMAIN: Ig-like V-type domain mediates binding to lymphocyte.
CC -!- PTM: O-glycosylated with sialylated oligosaccharides.
CC {ECO:0000269|PubMed:16754720}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM23248.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY457055; AAR27946.1; -; mRNA.
DR EMBL; AB243063; BAE96046.1; -; mRNA.
DR EMBL; AB243064; BAE96047.1; -; mRNA.
DR EMBL; AB243065; BAE96048.1; -; mRNA.
DR EMBL; AB243066; BAE96049.1; -; mRNA.
DR EMBL; AK009375; BAB26251.1; -; mRNA.
DR EMBL; AK138920; BAE23817.1; -; mRNA.
DR EMBL; AK171982; BAE42759.1; -; mRNA.
DR EMBL; AL591145; CAM23248.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL591145; CAM23249.1; -; Genomic_DNA.
DR EMBL; AL591145; CAM23250.1; -; Genomic_DNA.
DR EMBL; AL591145; CAM23251.1; -; Genomic_DNA.
DR EMBL; BC116906; AAI16907.1; -; mRNA.
DR EMBL; BC119315; AAI19316.1; -; mRNA.
DR CCDS; CCDS25484.1; -. [Q1ERP8-5]
DR CCDS; CCDS48939.1; -. [Q1ERP8-3]
DR CCDS; CCDS48940.1; -. [Q1ERP8-2]
DR RefSeq; NP_001154183.1; NM_001160711.1. [Q1ERP8-3]
DR RefSeq; NP_001154184.1; NM_001160712.1. [Q1ERP8-1]
DR RefSeq; NP_001154185.1; NM_001160713.1. [Q1ERP8-2]
DR RefSeq; NP_082263.2; NM_027987.3. [Q1ERP8-5]
DR AlphaFoldDB; Q1ERP8; -.
DR SMR; Q1ERP8; -.
DR GlyGen; Q1ERP8; 11 sites.
DR iPTMnet; Q1ERP8; -.
DR PhosphoSitePlus; Q1ERP8; -.
DR CPTAC; non-CPTAC-3349; -.
DR MaxQB; Q1ERP8; -.
DR PaxDb; Q1ERP8; -.
DR PeptideAtlas; Q1ERP8; -.
DR PRIDE; Q1ERP8; -.
DR ProteomicsDB; 283308; -. [Q1ERP8-1]
DR ProteomicsDB; 283309; -. [Q1ERP8-2]
DR ProteomicsDB; 283310; -. [Q1ERP8-3]
DR ProteomicsDB; 283311; -. [Q1ERP8-4]
DR ProteomicsDB; 283312; -. [Q1ERP8-5]
DR ABCD; Q1ERP8; 22 sequenced antibodies.
DR Antibodypedia; 1022; 119 antibodies from 21 providers.
DR DNASU; 52685; -.
DR Ensembl; ENSMUST00000017453; ENSMUSP00000017453; ENSMUSG00000017309. [Q1ERP8-5]
DR Ensembl; ENSMUST00000107163; ENSMUSP00000102781; ENSMUSG00000017309. [Q1ERP8-2]
DR Ensembl; ENSMUST00000107164; ENSMUSP00000102782; ENSMUSG00000017309. [Q1ERP8-3]
DR GeneID; 52685; -.
DR KEGG; mmu:52685; -.
DR UCSC; uc007lqf.2; mouse. [Q1ERP8-4]
DR UCSC; uc007lqg.2; mouse. [Q1ERP8-5]
DR UCSC; uc007lqh.2; mouse. [Q1ERP8-1]
DR UCSC; uc007lqi.2; mouse. [Q1ERP8-3]
DR UCSC; uc007lqj.2; mouse. [Q1ERP8-2]
DR CTD; 146894; -.
DR MGI; MGI:1289168; Cd300lg.
DR VEuPathDB; HostDB:ENSMUSG00000017309; -.
DR eggNOG; ENOG502SURU; Eukaryota.
DR GeneTree; ENSGT00940000162429; -.
DR InParanoid; Q1ERP8; -.
DR OMA; YAGEEGQ; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q1ERP8; -.
DR TreeFam; TF334441; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 52685; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q1ERP8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q1ERP8; protein.
DR Bgee; ENSMUSG00000017309; Expressed in interventricular septum and 69 other tissues.
DR ExpressionAtlas; Q1ERP8; baseline and differential.
DR Genevisible; Q1ERP8; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001791; F:IgM binding; IDA:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0002414; P:immunoglobulin transcytosis in epithelial cells; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
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 InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Endosome;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..331
FT /note="CMRF35-like molecule 9"
FT /id="PRO_0000306113"
FT TOPO_DOM 19..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..120
FT /note="Ig-like V-type"
FT REGION 278..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 136
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT DISULFID 37..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 126..170
FT /note="GKRDNAVPAGTCCPSSPTPSFQPLTPTRSLQPKAKAWQTQLPEPR -> ASP
FT GLHPTVVTAKQGKTGVKAPVFTEVAPAWSTGTSQVPPGISPYAGSSPHTATPARSAGTS
FT QVPPGISPYAGRSPHTATSPHAG (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16754720, ECO:0000303|PubMed:16876123"
FT /id="VSP_028413"
FT VAR_SEQ 127..170
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14662855,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16754720, ECO:0000303|PubMed:16876123"
FT /id="VSP_028414"
FT VAR_SEQ 170
FT /note="R -> TSPGLHPTVVTAKQGKTGVKAPVFTEVAPAWSTGTSQVPPGISPYAG
FT SSPHTATPARSAGTSQVPPGISPYAGRSPHTATSPHAG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16754720,
FT ECO:0000303|PubMed:16876123"
FT /id="VSP_028415"
FT VAR_SEQ 197
FT /note="S -> R (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028416"
FT VAR_SEQ 198..331
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028417"
FT CONFLICT 172
FT /note="S -> Y (in Ref. 2; BAE96049 and 3; BAB26251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36756 MW; 8223E678E7987A8A CRC64;
MRPLVLLWGC LVLPGYEALK GPKEISGFEG DTVSLRCTYV EKMKEHRKYW CRQGGILVSR
CGDIVYANQD QEVTRGRMSI RDSPQELSMT VIMRDLTLKD SGKYWCGIDR LGRDESFEVT
LIVFPGKRDN AVPAGTCCPS SPTPSFQPLT PTRSLQPKAK AWQTQLPEPR SSRPVVWLPL
TTPQDSRAVA SSVSKPSVSI PMVRMMAPVL ILLSLLLAAG LIAFGSHMLR WRKKAWLATE
TQKNEKVYLE TSLPGNGWTT EDSTIDLAVT PECLRNLNPS AVPSPETQNL SQSTEEEEAA
RSLDDDKEDV MAPPPLQMSA EELAFSEFIS V
