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C209E_MOUSE
ID   C209E_MOUSE             Reviewed;         208 AA.
AC   Q91ZW7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=CD209 antigen-like protein E;
DE   AltName: Full=DC-SIGN-related protein 4;
DE            Short=DC-SIGNR4;
DE   AltName: CD_antigen=CD209;
GN   Name=Cd209e;
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=11581173; DOI=10.1093/intimm/13.10.1283;
RA   Park C.G., Takahara K., Umemoto E., Yashima Y., Matsubara K., Matsuda Y.,
RA   Clausen B.E., Inaba K., Steinman R.M.;
RT   "Five mouse homologues of the human dendritic cell C-type lectin, DC-
RT   SIGN.";
RL   Int. Immunol. 13:1283-1290(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, 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).
CC   -!- FUNCTION: Putative pathogen-recognition receptor. May mediate the
CC       endocytosis of pathogens which are subsequently degraded in lysosomal
CC       compartments.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- CAUTION: In mouse, 5 genes homologous to human CD209/DC-SIGN and
CC       CD209L/DC-SIGNR have been identified. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=SIGNR4;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_164";
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DR   EMBL; AF373412; AAL13238.1; -; mRNA.
DR   EMBL; AK040917; BAC30744.1; -; mRNA.
DR   CCDS; CCDS22074.1; -.
DR   RefSeq; NP_570975.1; NM_130905.2.
DR   AlphaFoldDB; Q91ZW7; -.
DR   SMR; Q91ZW7; -.
DR   STRING; 10090.ENSMUSP00000033888; -.
DR   EPD; Q91ZW7; -.
DR   PaxDb; Q91ZW7; -.
DR   PRIDE; Q91ZW7; -.
DR   ProteomicsDB; 281709; -.
DR   DNASU; 170780; -.
DR   Ensembl; ENSMUST00000033888; ENSMUSP00000033888; ENSMUSG00000040197.
DR   GeneID; 170780; -.
DR   KEGG; mmu:170780; -.
DR   UCSC; uc009kss.1; mouse.
DR   CTD; 170780; -.
DR   MGI; MGI:2157948; Cd209e.
DR   VEuPathDB; HostDB:ENSMUSG00000040197; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000155012; -.
DR   HOGENOM; CLU_049894_7_3_1; -.
DR   InParanoid; Q91ZW7; -.
DR   OMA; WDWTFFN; -.
DR   OrthoDB; 1232767at2759; -.
DR   PhylomeDB; Q91ZW7; -.
DR   TreeFam; TF333341; -.
DR   BioGRID-ORCS; 170780; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q91ZW7; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q91ZW7; protein.
DR   Bgee; ENSMUSG00000040197; Expressed in morula and 14 other tissues.
DR   ExpressionAtlas; Q91ZW7; baseline and differential.
DR   Genevisible; Q91ZW7; MM.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR   GO; GO:0005537; F:mannose binding; IDA:MGI.
DR   GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033989; CD209-like_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endocytosis; Lectin; Membrane; Receptor;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..208
FT                   /note="CD209 antigen-like protein E"
FT                   /id="PRO_0000046608"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          83..198
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        105..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        176..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   208 AA;  24389 MW;  219CF71ED878DEB7 CRC64;
     MRAPQMGSLG FLDKGHIPLV LQLLFLILFT GLLVAIIIQV SKMPSSEEIQ WEHTKQEKMY
     KDLSQLKSEV DRLCRLCPWD WTFFNGNCYF FSKSQRDWHD SMTACKEMGA QLVIIKSHEE
     QSFLQQTSKK NSYTWMGLSD LNKEGEWYWL DGSPLSDSFE KYWKKGQPNN VGGQDCVEFR
     DNGWNDAKCE QRKFWICKKI ATTCLSKW
 
 
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