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CLM7_HUMAN
ID   CLM7_HUMAN              Reviewed;         201 AA.
AC   A8K4G0; Q1EG73; Q8IX40; Q8N6D1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=CMRF35-like molecule 7;
DE            Short=CLM-7;
DE   AltName: Full=CD300 antigen-like family member B;
DE   AltName: Full=CMRF35-A2;
DE   AltName: Full=Immune receptor expressed on myeloid cells 3;
DE            Short=IREM-3;
DE   AltName: Full=Leukocyte mono-Ig-like receptor 5;
DE   AltName: Full=Triggering receptor expressed on myeloid cells 5;
DE            Short=TREM-5;
DE   AltName: CD_antigen=CD300b;
DE   Flags: Precursor;
GN   Name=CD300LB; Synonyms=CD300B, CLM7, CMRF35A2, IREM3, LMIR5, TREM5;
GN   ORFNames=UNQ2530/PRO6029;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION
RP   AT TYR-188, MUTAGENESIS OF LYS-158 AND TYR-188, AND INTERACTION WITH
RP   TYROBP.
RX   PubMed=16920917; DOI=10.4049/jimmunol.177.5.2819;
RA   Martinez-Barriocanal A., Sayos J.;
RT   "Molecular and functional characterization of CD300b, a new activating
RT   immunoglobulin receptor able to transduce signals through two different
RT   pathways.";
RL   J. Immunol. 177:2819-2830(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Colonna M.;
RT   "Triggering receptor expressed on myeloid cells 5.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Blood;
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   [8]
RP   IDENTIFICATION.
RX   PubMed=12483297; DOI=10.1007/s00439-002-0851-y;
RA   Speckman R.A., Wright Daw J.A., Helms C., Duan S., Cao L.,
RA   Taillon-Miller P., Kwok P.Y., Menter A., Bowcock A.M.;
RT   "Novel immunoglobulin superfamily gene cluster, mapping to a region of
RT   human chromosome 17q25, linked to psoriasis susceptibility.";
RL   Hum. Genet. 112:34-41(2003).
RN   [9]
RP   PHOSPHORYLATION AT TYR-188, INTERACTION WITH TYROBP, AND FUNCTION.
RX   PubMed=17928527; DOI=10.1182/blood-2007-04-085787;
RA   Yamanishi Y., Kitaura J., Izawa K., Matsuoka T., Oki T., Lu Y., Shibata F.,
RA   Yamazaki S., Kumagai H., Nakajima H., Maeda-Yamamoto M., Tybulewicz V.L.J.,
RA   Takai T., Kitamura T.;
RT   "Analysis of mouse LMIR5/CLM-7 as an activating receptor: differential
RT   regulation of LMIR5/CLM-7 in mouse versus human cells.";
RL   Blood 111:688-698(2008).
CC   -!- FUNCTION: Acts as an activating immune receptor through its interaction
CC       with ITAM-bearing adapter TYROBP, and also independently by recruitment
CC       of GRB2. {ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17928527}.
CC   -!- SUBUNIT: Interacts with TYROBP, which enhances cell surface expression
CC       and activation properties. Interacts with GRB2 in the presence of FYN.
CC       {ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17928527}.
CC   -!- INTERACTION:
CC       A8K4G0; Q9UGN4: CD300A; NbExp=2; IntAct=EBI-26499879, EBI-10320732;
CC       A8K4G0; Q08708: CD300C; NbExp=4; IntAct=EBI-26499879, EBI-3915344;
CC       A8K4G0; Q496F6: CD300E; NbExp=2; IntAct=EBI-26499879, EBI-18010148;
CC       A8K4G0; A8K4G0: CD300LB; NbExp=7; IntAct=EBI-26499879, EBI-26499879;
CC       A8K4G0; Q6UXZ3: CD300LD; NbExp=2; IntAct=EBI-26499879, EBI-4314468;
CC       A8K4G0; Q8TDQ1: CD300LF; NbExp=3; IntAct=EBI-26499879, EBI-7381492;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in myeloid lineages.
CC       {ECO:0000269|PubMed:16920917}.
CC   -!- PTM: Phosphorylation on Tyr-188 by FYN is required for interaction with
CC       GRB2. {ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17928527}.
CC   -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH28091.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF83614.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAW89170.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY646929; AAV69612.1; -; mRNA.
DR   EMBL; AF427618; AAN86133.1; -; mRNA.
DR   EMBL; AY359025; AAQ89384.1; -; mRNA.
DR   EMBL; AK290925; BAF83614.1; ALT_INIT; mRNA.
DR   EMBL; AC079325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471099; EAW89170.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC028091; AAH28091.1; ALT_INIT; mRNA.
DR   CCDS; CCDS11700.2; -.
DR   RefSeq; NP_777552.3; NM_174892.3.
DR   AlphaFoldDB; A8K4G0; -.
DR   SMR; A8K4G0; -.
DR   BioGRID; 125877; 6.
DR   IntAct; A8K4G0; 5.
DR   STRING; 9606.ENSP00000376397; -.
DR   iPTMnet; A8K4G0; -.
DR   PhosphoSitePlus; A8K4G0; -.
DR   BioMuta; CD300LB; -.
DR   MassIVE; A8K4G0; -.
DR   PaxDb; A8K4G0; -.
DR   PeptideAtlas; A8K4G0; -.
DR   PRIDE; A8K4G0; -.
DR   Antibodypedia; 53132; 112 antibodies from 21 providers.
DR   DNASU; 124599; -.
DR   Ensembl; ENST00000392621.6; ENSP00000376397.2; ENSG00000178789.9.
DR   GeneID; 124599; -.
DR   KEGG; hsa:124599; -.
DR   MANE-Select; ENST00000392621.6; ENSP00000376397.2; NM_174892.4; NP_777552.3.
DR   UCSC; uc002jkx.4; human.
DR   CTD; 124599; -.
DR   DisGeNET; 124599; -.
DR   GeneCards; CD300LB; -.
DR   HGNC; HGNC:30811; CD300LB.
DR   HPA; ENSG00000178789; Tissue enhanced (bone marrow, brain, lymphoid tissue).
DR   MIM; 610705; gene.
DR   neXtProt; NX_A8K4G0; -.
DR   OpenTargets; ENSG00000178789; -.
DR   PharmGKB; PA142672151; -.
DR   VEuPathDB; HostDB:ENSG00000178789; -.
DR   eggNOG; ENOG502S7MA; Eukaryota.
DR   GeneTree; ENSGT00940000162729; -.
DR   HOGENOM; CLU_051023_3_1_1; -.
DR   InParanoid; A8K4G0; -.
DR   OMA; IYWCGIQ; -.
DR   OrthoDB; 1494510at2759; -.
DR   PhylomeDB; A8K4G0; -.
DR   TreeFam; TF334441; -.
DR   PathwayCommons; A8K4G0; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-2172127; DAP12 interactions.
DR   SignaLink; A8K4G0; -.
DR   SIGNOR; A8K4G0; -.
DR   BioGRID-ORCS; 124599; 5 hits in 268 CRISPR screens.
DR   ChiTaRS; CD300LB; human.
DR   GenomeRNAi; 124599; -.
DR   Pharos; A8K4G0; Tbio.
DR   PRO; PR:A8K4G0; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; A8K4G0; protein.
DR   Bgee; ENSG00000178789; Expressed in monocyte and 108 other tissues.
DR   ExpressionAtlas; A8K4G0; baseline and differential.
DR   Genevisible; A8K4G0; HS.
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:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
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   Cell membrane; Disulfide bond; Immunity; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..201
FT                   /note="CMRF35-like molecule 7"
FT                   /id="PRO_0000320130"
FT   TOPO_DOM        18..151
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          18..120
FT                   /note="Ig-like V-type"
FT   SITE            158
FT                   /note="Interaction with TYROBP"
FT   MOD_RES         188
FT                   /note="Phosphotyrosine; by FYN"
FT                   /evidence="ECO:0000269|PubMed:16920917,
FT                   ECO:0000269|PubMed:17928527"
FT   DISULFID        36..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   MUTAGEN         158
FT                   /note="K->L: Abolishes interaction with TYROBP, and
FT                   strongly reduces activation properties."
FT                   /evidence="ECO:0000269|PubMed:16920917"
FT   MUTAGEN         188
FT                   /note="Y->F: No effect on interaction with TYROBP, but
FT                   strongly reduces activation properties."
FT                   /evidence="ECO:0000269|PubMed:16920917"
FT   CONFLICT        144
FT                   /note="G -> R (in Ref. 1; AAV69612)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  22689 MW;  2B8027A488B97CAF CRC64;
     MWLPPALLLL SLSGCFSIQG PESVRAPEQG SLTVQCHYKQ GWETYIKWWC RGVRWDTCKI
     LIETRGSEQG EKSDRVSIKD NQKDRTFTVT MEGLRRDDAD VYWCGIERRG PDLGTQVKVI
     VDPEGAASTT ASSPTNSNMA VFIGSHKRNH YMLLVFVKVP ILLILVTAIL WLKGSQRVPE
     EPGEQPIYMN FSEPLTKDMA T
 
 
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