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UCN1_RAT
ID   UCN1_RAT                Reviewed;         122 AA.
AC   P55090;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Urocortin;
DE   AltName: Full=Corticotensin;
DE   Flags: Precursor;
GN   Name=Ucn;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=7477349; DOI=10.1038/378287a0;
RA   Vaughan J.M., Donaldson C.J., Bittencourt J., Perrin M.H., Lewis K.A.,
RA   Sutton S.W., Chan R., Turnbull A., Lovejoy D., Rivier C., Rivier J.E.,
RA   Sawchenko P., Vale W.W.;
RT   "Urocortin, a mammalian neuropeptide related to fish urotensin I and to
RT   corticotropin-releasing factor.";
RL   Nature 378:287-292(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lewis;
RA   Park J.H., Lee Y.J., Kim K.L.;
RT   "Detection of rat urocortin in lymphoid tissues: implications for the
RT   functional assessment of urocortin as a novel neuro-immunomodulatory
RT   peptide.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=21540451; DOI=10.1152/ajpendo.00695.2010;
RA   Yakabi K., Noguchi M., Ohno S., Ro S., Onouchi T., Ochiai M.,
RA   Takabayashi H., Takayama K., Harada Y., Sadakane C., Hattori T.;
RT   "Urocortin 1 reduces food intake and ghrelin secretion via CRF(2)
RT   receptors.";
RL   Am. J. Physiol. 301:E72-82(2011).
CC   -!- FUNCTION: Acts in vitro to stimulate the secretion of
CC       adrenocorticotropic hormone (ACTH) (PubMed:7477349). Binds with high
CC       affinity to CRF receptor types 1, 2-alpha, and 2-beta (By similarity).
CC       Plays a role in the establishment of normal hearing thresholds (By
CC       similarity). Reduces food intake and regulates ghrelin levels in
CC       gastric body and plasma (PubMed:21540451).
CC       {ECO:0000250|UniProtKB:P55089, ECO:0000250|UniProtKB:P81615,
CC       ECO:0000269|PubMed:21540451, ECO:0000269|PubMed:7477349}.
CC   -!- SUBUNIT: Interacts with CRHR1 and CRHR2 (via their N-terminal
CC       extracellular domain). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P55090; P35353: Crhr1; NbExp=3; IntAct=EBI-9030248, EBI-9030306;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the sauvagine/corticotropin-releasing
CC       factor/urotensin I family. {ECO:0000305}.
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DR   EMBL; U33935; AAA87566.1; -; mRNA.
DR   EMBL; AF093623; AAF63153.1; -; Genomic_DNA.
DR   PIR; S60262; S60262.
DR   RefSeq; NP_062023.1; NM_019150.1.
DR   AlphaFoldDB; P55090; -.
DR   SMR; P55090; -.
DR   BioGRID; 247834; 5.
DR   IntAct; P55090; 1.
DR   STRING; 10116.ENSRNOP00000008037; -.
DR   PaxDb; P55090; -.
DR   Ensembl; ENSRNOT00000008037; ENSRNOP00000008037; ENSRNOG00000006090.
DR   GeneID; 29151; -.
DR   KEGG; rno:29151; -.
DR   CTD; 7349; -.
DR   RGD; 3929; Ucn.
DR   eggNOG; ENOG502S63E; Eukaryota.
DR   GeneTree; ENSGT00940000154473; -.
DR   HOGENOM; CLU_138901_0_0_1; -.
DR   InParanoid; P55090; -.
DR   OMA; PGARNQG; -.
DR   OrthoDB; 1570341at2759; -.
DR   PhylomeDB; P55090; -.
DR   TreeFam; TF332956; -.
DR   Reactome; R-RNO-373080; Class B/2 (Secretin family receptors).
DR   PRO; PR:P55090; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000006090; Expressed in skeletal muscle tissue and 7 other tissues.
DR   Genevisible; P55090; RN.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0043679; C:axon terminus; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0043196; C:varicosity; IDA:RGD.
DR   GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD.
DR   GO; GO:0051431; F:corticotropin-releasing hormone receptor 2 binding; IPI:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IDA:RGD.
DR   GO; GO:0046811; F:histone deacetylase inhibitor activity; IDA:RGD.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0034199; P:activation of protein kinase A activity; IDA:RGD.
DR   GO; GO:0009060; P:aerobic respiration; IDA:RGD.
DR   GO; GO:0008306; P:associative learning; IDA:RGD.
DR   GO; GO:0042756; P:drinking behavior; IMP:RGD.
DR   GO; GO:0007631; P:feeding behavior; IMP:RGD.
DR   GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0035483; P:gastric emptying; IDA:RGD.
DR   GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR   GO; GO:0007611; P:learning or memory; IDA:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0032099; P:negative regulation of appetite; IDA:RGD.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IDA:RGD.
DR   GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR   GO; GO:0045792; P:negative regulation of cell size; IDA:RGD.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IDA:RGD.
DR   GO; GO:0060455; P:negative regulation of gastric acid secretion; IDA:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:RGD.
DR   GO; GO:0046888; P:negative regulation of hormone secretion; IDA:RGD.
DR   GO; GO:0060547; P:negative regulation of necrotic cell death; IDA:RGD.
DR   GO; GO:1901215; P:negative regulation of neuron death; IDA:RGD.
DR   GO; GO:0031175; P:neuron projection development; IDA:RGD.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IDA:RGD.
DR   GO; GO:0030157; P:pancreatic juice secretion; IDA:RGD.
DR   GO; GO:2000987; P:positive regulation of behavioral fear response; IDA:RGD.
DR   GO; GO:0090280; P:positive regulation of calcium ion import; IDA:RGD.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:RGD.
DR   GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IDA:RGD.
DR   GO; GO:0030307; P:positive regulation of cell growth; IDA:RGD.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:RGD.
DR   GO; GO:0051461; P:positive regulation of corticotropin secretion; IDA:RGD.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:RGD.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:RGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:RGD.
DR   GO; GO:0043117; P:positive regulation of vascular permeability; IDA:RGD.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IDA:RGD.
DR   GO; GO:0010996; P:response to auditory stimulus; ISO:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR   GO; GO:0048265; P:response to pain; IEP:RGD.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR   GO; GO:0035176; P:social behavior; IDA:RGD.
DR   GO; GO:0001964; P:startle response; ISO:RGD.
DR   GO; GO:0042311; P:vasodilation; IDA:RGD.
DR   InterPro; IPR018446; Corticotropin-releasing_fac_CS.
DR   InterPro; IPR000187; CRF.
DR   InterPro; IPR003620; Urocortin_CRF.
DR   PANTHER; PTHR15035; PTHR15035; 1.
DR   Pfam; PF00473; CRF; 1.
DR   PRINTS; PR01612; CRFFAMILY.
DR   SMART; SM00039; CRF; 1.
DR   PROSITE; PS00511; CRF; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Hearing; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..80
FT                   /id="PRO_0000006237"
FT   PEPTIDE         81..120
FT                   /note="Urocortin"
FT                   /id="PRO_0000006238"
FT   MOD_RES         120
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   122 AA;  13711 MW;  9F0AF834CBFFCE74 CRC64;
     MRQRGRATLL VALLLLVQLR PESSQWSPAA AAANVVQDPN LRWNPGVRNQ GGGVRALLLL
     LAERFPRRAG SEPAGERQRR DDPPLSIDLT FHLLRTLLEL ARTQSQRERA EQNRIIFDSV
     GK
 
 
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