GUC2B_HUMAN
ID GUC2B_HUMAN Reviewed; 112 AA.
AC Q16661; Q52LV0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Guanylate cyclase activator 2B;
DE Contains:
DE RecName: Full=Guanylate cyclase C-activating peptide 2;
DE AltName: Full=Guanylate cyclase C-activating peptide II;
DE Short=GCAP-II;
DE Contains:
DE RecName: Full=Uroguanylin;
DE Short=UGN;
DE Flags: Precursor;
GN Name=GUCA2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=8605041; DOI=10.1006/bbrc.1996.0287;
RA Miyazato M., Nakazato M., Yamaguchi H., Date Y., Kojima M., Kangawa K.,
RA Matsuo H., Matsukura S.;
RT "Cloning and characterization of a cDNA encoding a precursor for human
RT uroguanylin.";
RL Biochem. Biophys. Res. Commun. 219:644-648(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=8519795; DOI=10.1016/0167-4838(95)00204-4;
RA Hill O., Cetin Y., Cieslak A., Maegert H.-J., Forssmann W.-G.;
RT "A new human guanylate cyclase-activating peptide (GCAP-II, uroguanylin):
RT precursor cDNA and colonic expression.";
RL Biochim. Biophys. Acta 1253:146-149(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RA Maegert H.-J., Hill O., Forssmann W.-G.;
RT "Structure of the human uroguanylin / GCAP-II gene and expression within
RT the gastrointestinal tract.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9268639; DOI=10.1006/geno.1997.4808;
RA Miyazato M., Nakazato M., Matsukura S., Kangawa K., Matsuo H.;
RT "Genomic structure and chromosomal localization of human uroguanylin.";
RL Genomics 43:359-365(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 89-112, AND DISULFIDE BONDS.
RC TISSUE=Blood;
RX PubMed=7589507; DOI=10.1016/0014-5793(95)01075-p;
RA Hess R., Kuhn M., Schulz-Knappe P., Raida M., Fuchs M., Klodt J.,
RA Adermann K., Kaever V., Cetin Y., Forssmann W.-G.;
RT "GCAP-II: isolation and characterization of the circulating form of human
RT uroguanylin.";
RL FEBS Lett. 374:34-38(1995).
RN [7]
RP PROTEIN SEQUENCE OF 97-112, AND DISULFIDE BONDS.
RX PubMed=8141334; DOI=10.1152/ajprenal.1994.266.2.f342;
RA Kita T., Smith C.E., Fok K.F., Duffin K.L., Moore W.M., Karabatsos P.J.,
RA Kachur J.F., Hamra F.K., Pidhorodeckyj N.V., Forte L.R., Currie M.G.;
RT "Characterization of human uroguanylin: a member of the guanylin peptide
RT family.";
RL Am. J. Physiol. 266:F342-F348(1994).
RN [8]
RP STRUCTURE BY NMR OF 97-112.
RX PubMed=9774236; DOI=10.1111/j.1399-3011.1998.tb01480.x;
RA Marx U.C., Klodt J., Meyer M., Gerlach H., Roesch P., Forssmann W.-G.,
RA Adermann K.;
RT "One peptide, two topologies: structure and interconversion dynamics of
RT human uroguanylin isomers.";
RL J. Pept. Res. 52:229-240(1998).
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 -!- INTERACTION:
CC Q16661; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12349759, EBI-741480;
CC Q16661; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12349759, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Stomach and intestine.
CC -!- SIMILARITY: Belongs to the guanylin family. {ECO:0000305}.
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DR EMBL; U34279; AAC50416.1; -; mRNA.
DR EMBL; Z50753; CAA90629.1; -; mRNA.
DR EMBL; Z70295; CAA94311.1; -; Genomic_DNA.
DR EMBL; U55058; AAC51729.1; -; Genomic_DNA.
DR EMBL; BC069301; AAH69301.1; -; mRNA.
DR EMBL; BC093779; AAH93779.1; -; mRNA.
DR EMBL; BC093781; AAH93781.1; -; mRNA.
DR CCDS; CCDS464.1; -.
DR PIR; JC4651; JC4651.
DR RefSeq; NP_009033.1; NM_007102.2.
DR PDB; 1UYA; NMR; -; A=97-112.
DR PDB; 1UYB; NMR; -; A=97-112.
DR PDBsum; 1UYA; -.
DR PDBsum; 1UYB; -.
DR AlphaFoldDB; Q16661; -.
DR SMR; Q16661; -.
DR BioGRID; 109236; 10.
DR IntAct; Q16661; 2.
DR STRING; 9606.ENSP00000361662; -.
DR BioMuta; GUCA2B; -.
DR DMDM; 2495130; -.
DR jPOST; Q16661; -.
DR MassIVE; Q16661; -.
DR PaxDb; Q16661; -.
DR PeptideAtlas; Q16661; -.
DR PRIDE; Q16661; -.
DR ProteomicsDB; 61019; -.
DR Antibodypedia; 18083; 195 antibodies from 25 providers.
DR DNASU; 2981; -.
DR Ensembl; ENST00000372581.2; ENSP00000361662.1; ENSG00000044012.4.
DR GeneID; 2981; -.
DR KEGG; hsa:2981; -.
DR MANE-Select; ENST00000372581.2; ENSP00000361662.1; NM_007102.3; NP_009033.1.
DR UCSC; uc001chc.1; human.
DR CTD; 2981; -.
DR DisGeNET; 2981; -.
DR GeneCards; GUCA2B; -.
DR HGNC; HGNC:4683; GUCA2B.
DR HPA; ENSG00000044012; Tissue enriched (intestine).
DR MIM; 601271; gene.
DR neXtProt; NX_Q16661; -.
DR OpenTargets; ENSG00000044012; -.
DR PharmGKB; PA29066; -.
DR VEuPathDB; HostDB:ENSG00000044012; -.
DR eggNOG; ENOG502S7QR; Eukaryota.
DR GeneTree; ENSGT00940000154436; -.
DR HOGENOM; CLU_166952_1_0_1; -.
DR InParanoid; Q16661; -.
DR OMA; CANPSCF; -.
DR OrthoDB; 1566411at2759; -.
DR PhylomeDB; Q16661; -.
DR TreeFam; TF330731; -.
DR PathwayCommons; Q16661; -.
DR Reactome; R-HSA-8935690; Digestion.
DR SignaLink; Q16661; -.
DR SIGNOR; Q16661; -.
DR BioGRID-ORCS; 2981; 10 hits in 1058 CRISPR screens.
DR ChiTaRS; GUCA2B; human.
DR EvolutionaryTrace; Q16661; -.
DR GenomeRNAi; 2981; -.
DR Pharos; Q16661; Tbio.
DR PRO; PR:Q16661; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16661; protein.
DR Bgee; ENSG00000044012; Expressed in ileal mucosa and 54 other tissues.
DR Genevisible; Q16661; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0030250; F:guanylate cyclase activator activity; IBA:GO_Central.
DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..88
FT /evidence="ECO:0000269|PubMed:7589507"
FT /id="PRO_0000013147"
FT PEPTIDE 89..112
FT /note="Guanylate cyclase C-activating peptide 2"
FT /id="PRO_0000013148"
FT PEPTIDE 97..112
FT /note="Uroguanylin"
FT /id="PRO_0000013149"
FT DISULFID 67..80
FT /evidence="ECO:0000250"
FT DISULFID 100..108
FT DISULFID 103..111
FT VARIANT 11
FT /note="P -> T (in dbSNP:rs2297567)"
FT /id="VAR_053362"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1UYA"
SQ SEQUENCE 112 AA; 12069 MW; AA3030BC3D4EE412 CRC64;
MGCRAASGLL PGVAVVLLLL LQSTQSVYIQ YQGFRVQLES MKKLSDLEAQ WAPSPRLQAQ
SLLPAVCHHP ALPQDLQPVC ASQEASSIFK TLRTIANDDC ELCVNVACTG CL
