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Protein

Guanylate cyclase activator 2B

Gene

GUCA2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water transport.

GO - Molecular functioni

  • calcium sensitive guanylate cyclase activator activity Source: ProtInc

GO - Biological processi

  • body fluid secretion Source: Ensembl
  • cGMP biosynthetic process Source: Ensembl
  • excretion Source: ProtInc
  • negative regulation of blood pressure Source: Ensembl
  • positive regulation of guanylate cyclase activity Source: GOC
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase activator 2B
Cleaved into the following 2 chains:
Alternative name(s):
Guanylate cyclase C-activating peptide II
Short name:
GCAP-II
Uroguanylin
Short name:
UGN
Gene namesi
Name:GUCA2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4683. GUCA2B.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29066.

Polymorphism and mutation databases

BioMutaiGUCA2B.
DMDMi2495130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Propeptidei27 – 88621 PublicationPRO_0000013147Add
BLAST
Peptidei89 – 11224Guanylate cyclase C-activating peptide 2PRO_0000013148Add
BLAST
Peptidei97 – 11216UroguanylinPRO_0000013149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 80By similarity
Disulfide bondi100 ↔ 108
Disulfide bondi103 ↔ 111

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ16661.
PeptideAtlasiQ16661.
PRIDEiQ16661.

Expressioni

Tissue specificityi

Stomach and intestine.

Gene expression databases

BgeeiQ16661.
CleanExiHS_GUCA2B.
GenevisibleiQ16661. HS.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000361662.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi105 – 1073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UYANMR-A97-112[»]
1UYBNMR-A97-112[»]
ProteinModelPortaliQ16661.
SMRiQ16661. Positions 27-111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16661.

Family & Domainsi

Sequence similaritiesi

Belongs to the guanylin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45706.
GeneTreeiENSGT00730000111420.
HOGENOMiHOG000231183.
HOVERGENiHBG051861.
InParanoidiQ16661.
OMAiQSVYIQY.
OrthoDBiEOG75TMFM.
PhylomeDBiQ16661.
TreeFamiTF330731.

Family and domain databases

Gene3Di3.90.1450.10. 1 hit.
InterProiIPR000879. Guanylin.
[Graphical view]
PANTHERiPTHR11318. PTHR11318. 1 hit.
PfamiPF02058. Guanylin. 1 hit.
[Graphical view]
PIRSFiPIRSF001849. Guanylin. 1 hit.
PRINTSiPR00774. GUANYLIN.
ProDomiPD005588. Guanylin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF89890. SSF89890. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16661-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCRAASGLL PGVAVVLLLL LQSTQSVYIQ YQGFRVQLES MKKLSDLEAQ
60 70 80 90 100
WAPSPRLQAQ SLLPAVCHHP ALPQDLQPVC ASQEASSIFK TLRTIANDDC
110
ELCVNVACTG CL
Length:112
Mass (Da):12,069
Last modified:November 1, 1996 - v1
Checksum:iAA3030BC3D4EE412
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111P → T.
Corresponds to variant rs2297567 [ dbSNP | Ensembl ].
VAR_053362

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34279 mRNA. Translation: AAC50416.1.
Z50753 mRNA. Translation: CAA90629.1.
Z70295 Genomic DNA. Translation: CAA94311.1.
U55058 Genomic DNA. Translation: AAC51729.1.
BC069301 mRNA. Translation: AAH69301.1.
BC093779 mRNA. Translation: AAH93779.1.
BC093781 mRNA. Translation: AAH93781.1.
CCDSiCCDS464.1.
PIRiJC4651.
RefSeqiNP_009033.1. NM_007102.2.
UniGeneiHs.32966.

Genome annotation databases

EnsembliENST00000372581; ENSP00000361662; ENSG00000044012.
GeneIDi2981.
KEGGihsa:2981.
UCSCiuc001chc.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34279 mRNA. Translation: AAC50416.1.
Z50753 mRNA. Translation: CAA90629.1.
Z70295 Genomic DNA. Translation: CAA94311.1.
U55058 Genomic DNA. Translation: AAC51729.1.
BC069301 mRNA. Translation: AAH69301.1.
BC093779 mRNA. Translation: AAH93779.1.
BC093781 mRNA. Translation: AAH93781.1.
CCDSiCCDS464.1.
PIRiJC4651.
RefSeqiNP_009033.1. NM_007102.2.
UniGeneiHs.32966.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UYANMR-A97-112[»]
1UYBNMR-A97-112[»]
ProteinModelPortaliQ16661.
SMRiQ16661. Positions 27-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000361662.

Polymorphism and mutation databases

BioMutaiGUCA2B.
DMDMi2495130.

Proteomic databases

PaxDbiQ16661.
PeptideAtlasiQ16661.
PRIDEiQ16661.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372581; ENSP00000361662; ENSG00000044012.
GeneIDi2981.
KEGGihsa:2981.
UCSCiuc001chc.1. human.

Organism-specific databases

CTDi2981.
GeneCardsiGC01P042621.
HGNCiHGNC:4683. GUCA2B.
MIMi601271. gene.
neXtProtiNX_Q16661.
PharmGKBiPA29066.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45706.
GeneTreeiENSGT00730000111420.
HOGENOMiHOG000231183.
HOVERGENiHBG051861.
InParanoidiQ16661.
OMAiQSVYIQY.
OrthoDBiEOG75TMFM.
PhylomeDBiQ16661.
TreeFamiTF330731.

Miscellaneous databases

EvolutionaryTraceiQ16661.
GenomeRNAii2981.
NextBioi11824.
PROiQ16661.
SOURCEiSearch...

Gene expression databases

BgeeiQ16661.
CleanExiHS_GUCA2B.
GenevisibleiQ16661. HS.

Family and domain databases

Gene3Di3.90.1450.10. 1 hit.
InterProiIPR000879. Guanylin.
[Graphical view]
PANTHERiPTHR11318. PTHR11318. 1 hit.
PfamiPF02058. Guanylin. 1 hit.
[Graphical view]
PIRSFiPIRSF001849. Guanylin. 1 hit.
PRINTSiPR00774. GUANYLIN.
ProDomiPD005588. Guanylin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF89890. SSF89890. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a cDNA encoding a precursor for human uroguanylin."
    Miyazato M., Nakazato M., Yamaguchi H., Date Y., Kojima M., Kangawa K., Matsuo H., Matsukura S.
    Biochem. Biophys. Res. Commun. 219:644-648(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  2. "A new human guanylate cyclase-activating peptide (GCAP-II, uroguanylin): precursor cDNA and colonic expression."
    Hill O., Cetin Y., Cieslak A., Maegert H.-J., Forssmann W.-G.
    Biochim. Biophys. Acta 1253:146-149(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  3. "Structure of the human uroguanylin / GCAP-II gene and expression within the gastrointestinal tract."
    Maegert H.-J., Hill O., Forssmann W.-G.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  4. "Genomic structure and chromosomal localization of human uroguanylin."
    Miyazato M., Nakazato M., Matsukura S., Kangawa K., Matsuo H.
    Genomics 43:359-365(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  6. "GCAP-II: isolation and characterization of the circulating form of human uroguanylin."
    Hess R., Kuhn M., Schulz-Knappe P., Raida M., Fuchs M., Klodt J., Adermann K., Kaever V., Cetin Y., Forssmann W.-G.
    FEBS Lett. 374:34-38(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 89-112, DISULFIDE BONDS.
    Tissue: Blood.
  7. "Characterization of human uroguanylin: a member of the guanylin peptide family."
    Kita T., Smith C.E., Fok K.F., Duffin K.L., Moore W.M., Karabatsos P.J., Kachur J.F., Hamra F.K., Pidhorodeckyj N.V., Forte L.R., Currie M.G.
    Am. J. Physiol. 266:F342-F348(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 97-112, DISULFIDE BONDS.
  8. "One peptide, two topologies: structure and interconversion dynamics of human uroguanylin isomers."
    Marx U.C., Klodt J., Meyer M., Gerlach H., Roesch P., Forssmann W.-G., Adermann K.
    J. Pept. Res. 52:229-240(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 97-112.

Entry informationi

Entry nameiGUC2B_HUMAN
AccessioniPrimary (citable) accession number: Q16661
Secondary accession number(s): Q52LV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.