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GUC2A_RAT
ID   GUC2A_RAT               Reviewed;         115 AA.
AC   P28902;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Guanylin;
DE   AltName: Full=Guanylate cyclase activator 2A;
DE   Flags: Precursor;
GN   Name=Guca2a; Synonyms=Guca2;
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].
RC   TISSUE=Intestine;
RX   PubMed=1379587; DOI=10.1016/s0021-9258(18)41955-2;
RA   Schulz S., Chrisman T.D., Garbers D.L.;
RT   "Cloning and expression of guanylin. Its existence in various mammalian
RT   tissues.";
RL   J. Biol. Chem. 267:16019-16021(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1378267; DOI=10.1016/0006-291x(92)91699-q;
RA   Wiegand R.C., Kato J., Currie M.G.;
RT   "Rat guanylin cDNA: characterization of the precursor of an endogenous
RT   activator of intestinal guanylate cyclase.";
RL   Biochem. Biophys. Res. Commun. 185:812-817(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 101-115.
RC   STRAIN=Lewis; TISSUE=Duodenum;
RA   Maegert H.J., Khun M., Kruhoffer M., Forssmann W.-G.;
RL   Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 101-115.
RC   TISSUE=Jejunum;
RX   PubMed=1346555; DOI=10.1073/pnas.89.3.947;
RA   Currie M.G., Fok K.F., Kato J., Moore R.J., Hamra F.K., Duffin K.L.,
RA   Smith C.E.;
RT   "Guanylin: an endogenous activator of intestinal guanylate cyclase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:947-951(1992).
CC   -!- FUNCTION: Endogenous activator of intestinal guanylate cyclase. It
CC       stimulates this enzyme through the same receptor binding region as the
CC       heat-stable enterotoxins.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Intestine and in low abundance in adrenal gland,
CC       kidney, and uterus/oviduct.
CC   -!- SIMILARITY: Belongs to the guanylin family. {ECO:0000305}.
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DR   EMBL; M95493; AAA41302.1; -; mRNA.
DR   EMBL; M93005; AAA41300.1; -; mRNA.
DR   EMBL; X67669; CAA47901.1; -; mRNA.
DR   PIR; JN0318; JN0318.
DR   RefSeq; NP_037250.1; NM_013118.1.
DR   AlphaFoldDB; P28902; -.
DR   SMR; P28902; -.
DR   STRING; 10116.ENSRNOP00000011867; -.
DR   PaxDb; P28902; -.
DR   PRIDE; P28902; -.
DR   Ensembl; ENSRNOT00000011867; ENSRNOP00000011867; ENSRNOG00000008849.
DR   GeneID; 25656; -.
DR   KEGG; rno:25656; -.
DR   CTD; 2980; -.
DR   RGD; 2766; Guca2a.
DR   eggNOG; ENOG502S7QR; Eukaryota.
DR   GeneTree; ENSGT00940000154436; -.
DR   HOGENOM; CLU_166952_0_0_1; -.
DR   InParanoid; P28902; -.
DR   OMA; CAEPMLP; -.
DR   OrthoDB; 1552271at2759; -.
DR   PhylomeDB; P28902; -.
DR   TreeFam; TF330731; -.
DR   Reactome; R-RNO-8935690; Digestion.
DR   PRO; PR:P28902; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000008849; Expressed in jejunum and 17 other tissues.
DR   Genevisible; P28902; RN.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030250; F:guanylate cyclase activator activity; IDA:RGD.
DR   GO; GO:0030249; F:guanylate cyclase regulator activity; NAS:RGD.
DR   Gene3D; 3.90.1450.10; -; 1.
DR   InterPro; IPR000879; Guanylin.
DR   InterPro; IPR036382; Guanylin_sf.
DR   PANTHER; PTHR11318; PTHR11318; 1.
DR   Pfam; PF02058; Guanylin; 1.
DR   PIRSF; PIRSF001849; Guanylin; 1.
DR   PRINTS; PR00774; GUANYLIN.
DR   SUPFAM; SSF89890; SSF89890; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..100
FT                   /evidence="ECO:0000269|PubMed:1346555"
FT                   /id="PRO_0000013141"
FT   PEPTIDE         101..115
FT                   /note="Guanylin"
FT                   /id="PRO_0000013142"
FT   DISULFID        69..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        104..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        107..115
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   115 AA;  12574 MW;  35AC63C7AC130EE5 CRC64;
     MNAWLLSVLC LLGALAVLVE GVTVQDGDLS FPLESVKQLK HLREVQEPTL MSHKKFALRL
     PKPVAPELCS QSAFPEALRP LCEKPNAEEI LQRLEAIAQD PNTCEICAYA ACTGC
 
 
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