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UTS1_ONCMY
ID   UTS1_ONCMY              Reviewed;         165 AA.
AC   O93448;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=UI;
DE   Contains:
DE     RecName: Full=Urophysin;
DE   Contains:
DE     RecName: Full=Urotensin-1;
DE     AltName: Full=Urotensin I;
DE   Flags: Precursor;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypothalamus;
RX   PubMed=10417230; DOI=10.1006/gcen.1999.7290;
RA   Barsyte D., Tipping D.R., Smart D., Conlon J.M., Baker B.I., Lovejoy D.A.;
RT   "Rainbow trout (Oncorhynchus mykiss) urotensin-I: structural differences
RT   between urotensins-I and urocortins.";
RL   Gen. Comp. Endocrinol. 115:169-177(1999).
CC   -!- FUNCTION: Urotensin is found in the teleost caudal neurosecretory
CC       system. It has a suggested role in osmoregulation and as a
CC       corticotropin-releasing factor. The non-hormonal portion of this
CC       precursor may be a urotensin binding protein, urophysin.
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; AJ005264; CAA06461.1; -; mRNA.
DR   RefSeq; NP_001117815.1; NM_001124343.1.
DR   AlphaFoldDB; O93448; -.
DR   SMR; O93448; -.
DR   Ensembl; ENSOMYT00000166895; ENSOMYP00000123692; ENSOMYG00000051449.
DR   GeneID; 100136016; -.
DR   KEGG; omy:100136016; -.
DR   CTD; 7349; -.
DR   OrthoDB; 1373116at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Hormone; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..120
FT                   /note="Urophysin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000006253"
FT   PEPTIDE         123..163
FT                   /note="Urotensin-1"
FT                   /id="PRO_0000006254"
FT   MOD_RES         163
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   165 AA;  18632 MW;  3263357EE76E3A1A CRC64;
     MKPVPLILLL ATVLLSSHIP PSVCRPRDLA MFDGHGYKSQ LDEVLLKAGD NAISYLIGEK
     ILRYLQRNPR LQAGLPPQFP FEVTPLGSRG LGHLARSLPP LEEQRAPEEG NSLEEFVELT
     KRNDDPPISI DLTFHLLRNM IEMARIESQK EQAELNRKYL DEVGK
 
 
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