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EDN1_CAVPO
ID   EDN1_CAVPO              Reviewed;         149 AA.
AC   P97740;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Endothelin-1;
DE            Short=ET-1;
DE   AltName: Full=Preproendothelin-1;
DE            Short=PPET1;
DE   Contains:
DE     RecName: Full=Big endothelin-1;
DE   Flags: Precursor; Fragment;
GN   Name=EDN1;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8624482;
RA   Shima H., Yamanouchi M., Omori K., Sugiura M., Kawashima K., Sato T.;
RT   "Endothelin-1 production and endothelin converting enzyme expression by
RT   guinea pig airway epithelial cells.";
RL   Biochem. Mol. Biol. Int. 37:1001-1010(1995).
CC   -!- FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides
CC       (By similarity). Probable ligand for G-protein coupled receptors EDNRA
CC       and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and
CC       RHOA cascade in glomerular mesangial cells (By similarity). Also binds
CC       the DEAR/FBXW7-AS1 receptor (By similarity).
CC       {ECO:0000250|UniProtKB:P05305, ECO:0000250|UniProtKB:P09558}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC       {ECO:0000305}.
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DR   EMBL; S82654; AAB46735.1; -; mRNA.
DR   AlphaFoldDB; P97740; -.
DR   SMR; P97740; -.
DR   STRING; 10141.ENSCPOP00000008982; -.
DR   eggNOG; ENOG502S1NV; Eukaryota.
DR   InParanoid; P97740; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR   InterPro; IPR020475; Endothelin.
DR   InterPro; IPR019764; Endothelin_toxin_CS.
DR   InterPro; IPR001928; Endothln-like_toxin.
DR   PANTHER; PTHR13874; PTHR13874; 1.
DR   Pfam; PF00322; Endothelin; 1.
DR   PRINTS; PR00365; ENDOTHELIN.
DR   SMART; SM00272; END; 2.
DR   PROSITE; PS00270; ENDOTHELIN; 2.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Reference proteome;
KW   Secreted; Vasoactive; Vasoconstrictor.
FT   PROPEP          <1..33
FT                   /evidence="ECO:0000250|UniProtKB:P22388"
FT                   /id="PRO_0000008052"
FT   PEPTIDE         36..74
FT                   /note="Big endothelin-1"
FT                   /evidence="ECO:0000250|UniProtKB:P22388"
FT                   /id="PRO_0000436395"
FT   PEPTIDE         36..56
FT                   /note="Endothelin-1"
FT                   /id="PRO_0000008053"
FT   PROPEP          57..>149
FT                   /id="PRO_0000008054"
FT   REGION          6..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..107
FT                   /note="Endothelin-like"
FT   SITE            56..57
FT                   /note="Cleavage; by KEL"
FT                   /evidence="ECO:0000250|UniProtKB:P05305"
FT   DISULFID        36..50
FT                   /evidence="ECO:0000250|UniProtKB:P05305"
FT   DISULFID        38..46
FT                   /evidence="ECO:0000250|UniProtKB:P05305"
FT   NON_TER         1
FT   NON_TER         149
SQ   SEQUENCE   149 AA;  16455 MW;  EC0EB64A18E7610E CRC64;
     AAETVVSGAE LSLTANSGGE KTPPHAPGLL RRSKRCSCSS LMDKECVYFC HLDIIWVNTP
     GHIAPYGLGG PFRSKRSLKE LFPTKATEHR NRCQCANQKD KKCWNFCQAG KELSSQDTMQ
     KGWDNHKKGK DCSKLGKKCI SQQLGNGKK
 
 
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