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CNTFR_MOUSE
ID   CNTFR_MOUSE             Reviewed;         372 AA.
AC   O88507; Q80T01;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Ciliary neurotrophic factor receptor subunit alpha;
DE            Short=CNTF receptor subunit alpha;
DE            Short=CNTFR-alpha;
DE   Flags: Precursor;
GN   Name=Cntfr;
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   TISSUE=Brain;
RA   Maeda M., Yaguchi N., Hanyuu C., Nakata Y., Onoda N., Tulin E.E.,
RA   Kojima T., Hasegawa M., Kikuchi Y., Nomura H.;
RT   "Mouse homolog of human ciliary neurotrophic factor receptor.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60 AND ASN-70.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Brown adipose tissue;
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: Binds to CNTF. The alpha subunit provides the receptor
CC       specificity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterotrimer with LIFR and IL6ST. Interacts with
CC       heterodimeric neurotropic cytokine composed of CLCF1/CLC and CRLF1/CLF-
CC       1. Either alone or in complex with the heterodimer CLCF1-CRLF1
CC       interacts with SORL1; this interaction may promote internalization and
CC       lysosomal degradation. {ECO:0000250|UniProtKB:P26992}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-surface
CC       receptor binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF068615; AAC25711.1; -; mRNA.
DR   EMBL; BC046974; AAH46974.1; -; mRNA.
DR   EMBL; BC050928; AAH50928.1; -; mRNA.
DR   CCDS; CCDS18067.1; -.
DR   RefSeq; NP_001129528.1; NM_001136056.3.
DR   RefSeq; NP_057882.2; NM_016673.2.
DR   RefSeq; XP_006537660.1; XM_006537597.3.
DR   RefSeq; XP_006537661.1; XM_006537598.2.
DR   RefSeq; XP_006537662.1; XM_006537599.3.
DR   RefSeq; XP_011248218.1; XM_011249916.2.
DR   RefSeq; XP_011248219.1; XM_011249917.2.
DR   RefSeq; XP_017175430.1; XM_017319941.1.
DR   RefSeq; XP_017175431.1; XM_017319942.1.
DR   AlphaFoldDB; O88507; -.
DR   BMRB; O88507; -.
DR   SMR; O88507; -.
DR   BioGRID; 198796; 2.
DR   IntAct; O88507; 3.
DR   MINT; O88507; -.
DR   STRING; 10090.ENSMUSP00000100026; -.
DR   GlyConnect; 2215; 5 N-Linked glycans (2 sites).
DR   GlyGen; O88507; 4 sites, 5 N-linked glycans (2 sites).
DR   iPTMnet; O88507; -.
DR   PhosphoSitePlus; O88507; -.
DR   MaxQB; O88507; -.
DR   PaxDb; O88507; -.
DR   PRIDE; O88507; -.
DR   ProteomicsDB; 283410; -.
DR   Antibodypedia; 25488; 334 antibodies from 39 providers.
DR   DNASU; 12804; -.
DR   Ensembl; ENSMUST00000102961; ENSMUSP00000100026; ENSMUSG00000028444.
DR   Ensembl; ENSMUST00000102962; ENSMUSP00000100027; ENSMUSG00000028444.
DR   GeneID; 12804; -.
DR   KEGG; mmu:12804; -.
DR   UCSC; uc008sje.2; mouse.
DR   CTD; 1271; -.
DR   MGI; MGI:99605; Cntfr.
DR   VEuPathDB; HostDB:ENSMUSG00000028444; -.
DR   eggNOG; ENOG502QUDK; Eukaryota.
DR   GeneTree; ENSGT00940000158864; -.
DR   HOGENOM; CLU_047259_0_0_1; -.
DR   InParanoid; O88507; -.
DR   OMA; KICDTGE; -.
DR   OrthoDB; 741136at2759; -.
DR   PhylomeDB; O88507; -.
DR   TreeFam; TF331210; -.
DR   Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR   SABIO-RK; O88507; -.
DR   BioGRID-ORCS; 12804; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Cntfr; mouse.
DR   PRO; PR:O88507; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; O88507; protein.
DR   Bgee; ENSMUSG00000028444; Expressed in ventricular zone and 163 other tissues.
DR   ExpressionAtlas; O88507; baseline and differential.
DR   Genevisible; O88507; MM.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; ISO:MGI.
DR   GO; GO:0097059; C:CNTFR-CLCF1 complex; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; IGI:MGI.
DR   GO; GO:0019955; F:cytokine binding; ISO:MGI.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0003360; P:brainstem development; IMP:MGI.
DR   GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; IGI:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR   GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0007548; P:sex differentiation; IMP:MGI.
DR   GO; GO:0060538; P:skeletal muscle organ development; IMP:MGI.
DR   GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
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; IPR003598; Ig_sub2.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..342
FT                   /note="Ciliary neurotrophic factor receptor subunit alpha"
FT                   /id="PRO_0000010993"
FT   PROPEP          343..372
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010994"
FT   DOMAIN          27..104
FT                   /note="Ig-like C2-type"
FT   DOMAIN          108..205
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          206..306
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          301..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           290..294
FT                   /note="WSXWS motif"
FT   COMPBIAS        312..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           342
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        2
FT                   /note="A -> T (in Ref. 1; AAC25711)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   372 AA;  40801 MW;  0704AA35CF1BBE12 CRC64;
     MAASVPWACC AVLAAAAAAV YTQKHSPQEA PHVQYERLGA DVTLPCGTAS WDAAVTWRVN
     GTDLAPDLLN GSQLILRSLE LGHSGLYACF HRDSWHLRHQ VLLHVGLPPR EPVLSCRSNT
     YPKGFYCSWH LPTPTYIPNT FNVTVLHGSK IMVCEKDPAL KNRCHIRYMH LFSTIKYKVS
     ISVSNALGHN TTAITFDEFT IVKPDPPENV VARPVPSNPR RLEVTWQTPS TWPDPESFPL
     KFFLRYRPLI LDQWQHVELS DGTAHTITDA YAGKEYIIQV AAKDNEIGTW SDWSVAAHAT
     PWTEEPRHLT TEAQAPETTT STTSSLAPPP TTKICDPGEL GSGGGPSILF LTSVPVTLVL
     AAAAATANNL LI
 
 
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