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 24-JAN-2024, entry version 171. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9606-ENSP00000361662; -. DR PeptideAtlas; Q16661; -. DR ProteomicsDB; 61019; -. DR Antibodypedia; 18083; 215 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 AGR; HGNC:4683; -. 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; ITPLDPC; -. DR OrthoDB; 4867316at2759; -. 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 1136 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 cell types or tissues. 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; Guanylin; 1. DR InterPro; IPR000879; Guanylin. DR InterPro; IPR036382; Guanylin_sf. DR PANTHER; PTHR11318:SF4; GUANYLATE CYCLASE ACTIVATOR 2B; 1. DR PANTHER; PTHR11318; GUANYLIN FAMILY MEMBER; 1. DR Pfam; PF02058; Guanylin; 1. DR PIRSF; PIRSF001849; Guanylin; 1. DR PRINTS; PR00774; GUANYLIN. DR SUPFAM; SSF89890; Proguanylin; 1. DR Genevisible; Q16661; HS. 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 //