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CRLF1_MOUSE
ID   CRLF1_MOUSE             Reviewed;         425 AA.
AC   Q9JM58;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Cytokine receptor-like factor 1;
DE   AltName: Full=Cytokine receptor-like molecule 3;
DE            Short=CRLM-3;
DE   AltName: Full=Cytokine-like factor 1;
DE            Short=CLF-1;
DE   AltName: Full=Novel cytokine receptor 6;
DE            Short=NR6;
DE   Flags: Precursor;
GN   Name=Crlf1; Synonyms=Crlm3;
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].
RA   Hiroyama T., Iwama A., Nakamura Y., Nakauchi H.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10359701; DOI=10.1016/s0960-9822(99)80266-8;
RA   Alexander W.S., Rakar S., Robb L., Farley A., Willson T.A., Zhang J.-G.,
RA   Hartley L., Kikuchi Y., Kojima T., Nomura H., Hasegawa M., Maeda M.,
RA   Fabri L., Jachno K., Nash A., Metcalf D., Nicola N.A., Hilton D.J.;
RT   "Suckling defect in mice lacking the soluble haemopoietin receptor NR6.";
RL   Curr. Biol. 9:605-608(1999).
RN   [3]
RP   PHOSPHORYLATION AT SER-222.
RX   PubMed=15378723; DOI=10.1002/rcm.1604;
RA   Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT   "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT   purification and linear ion trap mass spectrometry.";
RL   Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
CC   -!- FUNCTION: In complex with CLCF1, forms a heterodimeric neurotropic
CC       cytokine that plays a crucial role during neuronal development (By
CC       similarity). Plays a role in the initiation and/or maintenance of
CC       suckling in neonatal mice (PubMed:10359701). May also play a regulatory
CC       role in the immune system (By similarity).
CC       {ECO:0000250|UniProtKB:O75462, ECO:0000269|PubMed:10359701}.
CC   -!- SUBUNIT: Forms covalent di- and tetramers. Forms a heteromeric complex
CC       with cardiotrophin-like cytokine CLCF1/CLC; the CRLF1-CLCF1 complex is
CC       a ligand for the ciliary neurotrophic factor receptor/CNTFR. The CRLF1-
CC       CLCF1 heterodimer, as well as tripartite signaling complex formed by
CC       CRLF1, CLCF1 and CNTFR bind SORL1 (via N-terminal ectodomain); within
CC       this complex, the interaction is mediated predominantly by the CRLF1
CC       moiety. {ECO:0000250|UniProtKB:O75462}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in the embryo. Not detected in the
CC       brain of adult mice. {ECO:0000269|PubMed:10359701}.
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.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB040038; BAA92777.1; -; mRNA.
DR   CCDS; CCDS22369.1; -.
DR   RefSeq; NP_061297.1; NM_018827.3.
DR   AlphaFoldDB; Q9JM58; -.
DR   SMR; Q9JM58; -.
DR   BioGRID; 198889; 1.
DR   IntAct; Q9JM58; 2.
DR   MINT; Q9JM58; -.
DR   STRING; 10090.ENSMUSP00000008032; -.
DR   GlyGen; Q9JM58; 6 sites.
DR   iPTMnet; Q9JM58; -.
DR   PhosphoSitePlus; Q9JM58; -.
DR   MaxQB; Q9JM58; -.
DR   PaxDb; Q9JM58; -.
DR   PeptideAtlas; Q9JM58; -.
DR   PRIDE; Q9JM58; -.
DR   ProteomicsDB; 278036; -.
DR   Antibodypedia; 28115; 245 antibodies from 27 providers.
DR   DNASU; 12931; -.
DR   Ensembl; ENSMUST00000008032; ENSMUSP00000008032; ENSMUSG00000007888.
DR   GeneID; 12931; -.
DR   KEGG; mmu:12931; -.
DR   UCSC; uc009maj.1; mouse.
DR   CTD; 9244; -.
DR   MGI; MGI:1340030; Crlf1.
DR   VEuPathDB; HostDB:ENSMUSG00000007888; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000156569; -.
DR   HOGENOM; CLU_017892_0_0_1; -.
DR   InParanoid; Q9JM58; -.
DR   OMA; HKTRNQA; -.
DR   OrthoDB; 144839at2759; -.
DR   PhylomeDB; Q9JM58; -.
DR   TreeFam; TF106501; -.
DR   Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR   Reactome; R-MMU-9020956; Interleukin-27 signaling.
DR   BioGRID-ORCS; 12931; 3 hits in 76 CRISPR screens.
DR   PRO; PR:Q9JM58; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9JM58; protein.
DR   Bgee; ENSMUSG00000007888; Expressed in metanephric ureteric bud and 148 other tissues.
DR   ExpressionAtlas; Q9JM58; baseline and differential.
DR   Genevisible; Q9JM58; MM.
DR   GO; GO:0097058; C:CRLF-CLCF1 complex; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:MGI.
DR   GO; GO:0005125; F:cytokine activity; ISO:MGI.
DR   GO; GO:0019955; F:cytokine binding; ISO:MGI.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:BHF-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR   GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF09067; EpoR_lig-bind; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..425
FT                   /note="Cytokine receptor-like factor 1"
FT                   /id="PRO_0000011040"
FT   DOMAIN          35..134
FT                   /note="Ig-like C2-type"
FT   DOMAIN          140..235
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          240..344
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          335..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           330..334
FT                   /note="WSXWS motif"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:15378723"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        146..156
FT                   /evidence="ECO:0000250"
FT   DISULFID        187..198
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  46662 MW;  910535C629CA7056 CRC64;
     MPAGRPGPVA QSARRPPRPL SSLWSPLLLC VLGVPRGGSG AHTAVISPQD PTLLIGSSLQ
     ATCSIHGDTP GATAEGLYWT LNGRRLPSEL SRLLNTSTLA LALANLNGSR QQSGDNLVCH
     ARDGSILAGS CLYVGLPPEK PFNISCWSRN MKDLTCRWTP GAHGETFLHT NYSLKYKLRW
     YGQDNTCEEY HTVGPHSCHI PKDLALFTPY EIWVEATNRL GSARSDVLTL DVLDVVTTDP
     PPDVHVSRVG GLEDQLSVRW VSPPALKDFL FQAKYQIRYR VEDSVDWKVV DDVSNQTSCR
     LAGLKPGTVY FVQVRCNPFG IYGSKKAGIW SEWSHPTAAS TPRSERPGPG GGVCEPRGGE
     PSSGPVRREL KQFLGWLKKH AYCSNLSFRL YDQWRAWMQK SHKTRNQDEG ILPSGRRGAA
     RGPAG
 
 
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