GUC2B_DIDVI
ID GUC2B_DIDVI Reviewed; 109 AA.
AC Q28358;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Guanylate cyclase activator 2B;
DE Contains:
DE RecName: Full=Uroguanylin;
DE Short=UGN;
DE Flags: Precursor;
GN Name=GUCA2B;
OS Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=8605009; DOI=10.1006/bbrc.1996.0255;
RA Fan X., Hamra F.K., Freeman R.H., Eber S.L., Krause W.J., Lim R.W.,
RA Pace V.M., Currie M.G., Forte L.R.;
RT "Uroguanylin: cloning of preprouroguanylin cDNA, mRNA expression in the
RT intestine and heart and isolation of uroguanylin and prouroguanylin from
RT plasma.";
RL Biochem. Biophys. Res. Commun. 219:457-462(1996).
RN [2]
RP PROTEIN SEQUENCE OF 95-109.
RC TISSUE=Urine;
RX PubMed=7902563; DOI=10.1073/pnas.90.22.10464;
RA Hamra F.K., Forte L.R., Eber S.L., Pidhorodeckyj N.V., Krause W.J.,
RA Freeman R.H., Chin D.T., Tompkins J.A., Fok K.F., Smith C.E., Duffin K.L.,
RA Siegel N.R., Currie M.G.;
RT "Uroguanylin: structure and activity of a second endogenous peptide that
RT stimulates intestinal guanylate cyclase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10464-10468(1993).
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. May be a potent physiological regulator of
CC intestinal fluid and electrolyte transport. May be an
CC autocrine/paracrine regulator of intestinal salt and water transport.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Small and large intestine and atria and ventricles
CC of heart. Both uroguanylin and prouroguanylin are found in plasma.
CC -!- SIMILARITY: Belongs to the guanylin family. {ECO:0000305}.
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DR EMBL; U49353; AAB00553.1; -; mRNA.
DR AlphaFoldDB; Q28358; -.
DR SMR; Q28358; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030250; F:guanylate cyclase activator activity; IEA:InterPro.
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; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..94
FT /evidence="ECO:0000269|PubMed:7902563"
FT /id="PRO_0000013145"
FT PEPTIDE 95..109
FT /note="Uroguanylin"
FT /id="PRO_0000013146"
FT DISULFID 65..78
FT /evidence="ECO:0000250"
FT DISULFID 98..106
FT /evidence="ECO:0000250"
FT DISULFID 101..109
FT /evidence="ECO:0000250"
SQ SEQUENCE 109 AA; 12040 MW; AE948E210CA3AE7A CRC64;
MKVLALPVAV AAMLLVLAQN TQSVYIQYEG FQVKLDSVKK LDELLEQPRS FRHRMGTQRD
PSVLCSDPAL PSDLQPVCEN SQAANIFRAL RSISQEDCEL CINVACTGC