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TARM1_HUMAN
ID   TARM1_HUMAN             Reviewed;         271 AA.
AC   B6A8C7; B4DWY4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=T-cell-interacting, activating receptor on myeloid cells protein 1;
DE   AltName: Full=OSCAR-like transcript-2 protein;
DE            Short=OLT-2;
DE   Flags: Precursor;
GN   Name=TARM1;
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] (ISOFORM 1).
RC   TISSUE=Bone marrow;
RA   Barrow A.D., de Bono B., Trowsdale J.;
RT   "OSCAR-like transcript-2 (OLT-2) mRNA.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH FCER1G, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=26311901; DOI=10.4049/jimmunol.1401847;
RA   Radjabova V., Mastroeni P., Skjoedt K., Zaccone P., de Bono B.,
RA   Goodall J.C., Chilvers E.R., Juss J.K., Jones D.C., Trowsdale J.,
RA   Barrow A.D.;
RT   "TARM1 is a novel leukocyte receptor complex-encoded ITAM receptor that
RT   costimulates proinflammatory cytokine secretion by macrophages and
RT   neutrophils.";
RL   J. Immunol. 195:3149-3159(2015).
CC   -!- FUNCTION: May act as receptor (By similarity). Negatively regulates
CC       TCR-mediated CD4(+) T cell proliferation and activation, possibly by
CC       binding an unknown ligand on the T cell surface (PubMed:26311901).
CC       Enhances Toll-like receptor-mediated production of pro-inflammatory
CC       cytokines by macrophages and neutrophils (By similarity).
CC       {ECO:0000250|UniProtKB:B6A8R8, ECO:0000269|PubMed:26311901}.
CC   -!- SUBUNIT: Interacts with Fc receptor gamma chain FCER1G.
CC       {ECO:0000269|PubMed:26311901}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26311901};
CC       Single-pass type I membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B6A8C7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B6A8C7-2; Sequence=VSP_039225;
CC   -!- TISSUE SPECIFICITY: Expressed in fetal and adult liver, lung, testis,
CC       thymus and spleen. Expressed in blood neutrophils.
CC       {ECO:0000269|PubMed:26311901}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26311901}.
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DR   EMBL; DQ479398; ABF19808.1; -; mRNA.
DR   EMBL; AK301730; BAG63196.1; -; mRNA.
DR   EMBL; AC012314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS46173.1; -. [B6A8C7-1]
DR   CCDS; CCDS82395.1; -. [B6A8C7-2]
DR   RefSeq; NP_001129158.2; NM_001135686.2.
DR   RefSeq; NP_001317579.1; NM_001330650.1.
DR   AlphaFoldDB; B6A8C7; -.
DR   SMR; B6A8C7; -.
DR   STRING; 9606.ENSP00000439454; -.
DR   GlyGen; B6A8C7; 1 site.
DR   iPTMnet; B6A8C7; -.
DR   PhosphoSitePlus; B6A8C7; -.
DR   BioMuta; TARM1; -.
DR   MassIVE; B6A8C7; -.
DR   PaxDb; B6A8C7; -.
DR   PeptideAtlas; B6A8C7; -.
DR   PRIDE; B6A8C7; -.
DR   Antibodypedia; 65161; 80 antibodies from 15 providers.
DR   DNASU; 441864; -.
DR   Ensembl; ENST00000432826.2; ENSP00000439454.1; ENSG00000248385.8.
DR   Ensembl; ENST00000611088.1; ENSP00000479824.1; ENSG00000276145.1. [B6A8C7-1]
DR   Ensembl; ENST00000611419.1; ENSP00000478234.1; ENSG00000275806.1. [B6A8C7-1]
DR   Ensembl; ENST00000612678.1; ENSP00000482624.1; ENSG00000275123.1. [B6A8C7-1]
DR   Ensembl; ENST00000614463.1; ENSP00000480049.1; ENSG00000276355.4. [B6A8C7-1]
DR   Ensembl; ENST00000615726.1; ENSP00000479185.1; ENSG00000275384.1. [B6A8C7-1]
DR   Ensembl; ENST00000619320.1; ENSP00000479062.1; ENSG00000276604.1. [B6A8C7-1]
DR   Ensembl; ENST00000620140.4; ENSP00000477830.1; ENSG00000276355.4. [B6A8C7-2]
DR   Ensembl; ENST00000620398.1; ENSP00000479374.1; ENSG00000273875.1. [B6A8C7-1]
DR   Ensembl; ENST00000620707.1; ENSP00000480377.1; ENSG00000277178.1. [B6A8C7-1]
DR   Ensembl; ENST00000622245.1; ENSP00000478822.1; ENSG00000274889.1. [B6A8C7-1]
DR   GeneID; 441864; -.
DR   KEGG; hsa:441864; -.
DR   UCSC; uc010yei.1; human. [B6A8C7-1]
DR   CTD; 441864; -.
DR   GeneCards; TARM1; -.
DR   HGNC; HGNC:37250; TARM1.
DR   HPA; ENSG00000248385; Tissue enriched (bone).
DR   neXtProt; NX_B6A8C7; -.
DR   PharmGKB; PA165394443; -.
DR   VEuPathDB; HostDB:ENSG00000248385; -.
DR   eggNOG; ENOG502RYEX; Eukaryota.
DR   HOGENOM; CLU_021100_1_0_1; -.
DR   InParanoid; B6A8C7; -.
DR   OrthoDB; 1327293at2759; -.
DR   PhylomeDB; B6A8C7; -.
DR   TreeFam; TF336644; -.
DR   PathwayCommons; B6A8C7; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 441864; 15 hits in 1062 CRISPR screens.
DR   ChiTaRS; TARM1; human.
DR   GenomeRNAi; 441864; -.
DR   Pharos; B6A8C7; Tdark.
DR   PRO; PR:B6A8C7; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; B6A8C7; protein.
DR   Bgee; ENSG00000248385; Expressed in bone marrow and 22 other tissues.
DR   ExpressionAtlas; B6A8C7; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR   GO; GO:0034987; F:immunoglobulin receptor binding; IPI:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:2000515; P:negative regulation of CD4-positive, alpha-beta T cell activation; IDA:UniProtKB.
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   Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunity; Immunoglobulin domain; Innate immunity; Membrane;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..271
FT                   /note="T-cell-interacting, activating receptor on myeloid
FT                   cells protein 1"
FT                   /id="PRO_0000394231"
FT   TOPO_DOM        17..236
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..113
FT                   /note="Ig-like C2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          126..212
FT                   /note="Ig-like C2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        146..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..12
FT                   /note="MIPKLLSLLCFR -> MKERKKKERKERKRKKERNG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039225"
FT   VARIANT         37
FT                   /note="S -> P (in dbSNP:rs17305269)"
FT                   /id="VAR_063151"
FT   VARIANT         111
FT                   /note="R -> H (in dbSNP:rs80087697)"
FT                   /id="VAR_063152"
FT   VARIANT         258
FT                   /note="R -> W (in dbSNP:rs77768804)"
FT                   /id="VAR_063153"
SQ   SEQUENCE   271 AA;  29474 MW;  B1E2B17A1C657060 CRC64;
     MIPKLLSLLC FRLCVGQGDT RGDGSLPKPS LSAWPSSVVP ANSNVTLRCW TPARGVSFVL
     RKGGIILESP KPLDSTEGAA EFHLNNLKVR NAGEYTCEYY RKASPHILSQ RSDVLLLLVT
     GHLSKPFLRT YQRGTVTAGG RVTLQCQKRD QLFVPIMFAL LKAGTPSPIQ LQSPAGKEID
     FSLVDVTAGD AGNYSCMYYQ TKSPFWASEP SDQLEILVTV PPGTTSSNYS LGNFVRLGLA
     AVIVVIMGAF LVEAWYSRNV SPGESEAFKP E
 
 
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