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Q16661

- GUC2B_HUMAN

UniProt

Q16661 - GUC2B_HUMAN

Protein

Guanylate cyclase activator 2B

Gene

GUCA2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    1. calcium sensitive guanylate cyclase activator activity Source: ProtInc

    GO - Biological processi

    1. body fluid secretion Source: Ensembl
    2. cGMP biosynthetic process Source: Ensembl
    3. excretion Source: ProtInc
    4. negative regulation of blood pressure Source: Ensembl
    5. positive regulation of guanylate cyclase activity Source: GOC

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4683. GUCA2B.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29066.

    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.
    GenevestigatoriQ16661.

    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 – 1073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MGCRAASGLL PGVAVVLLLL LQSTQSVYIQ YQGFRVQLES MKKLSDLEAQ    50
    WAPSPRLQAQ SLLPAVCHHP ALPQDLQPVC ASQEASSIFK TLRTIANDDC 100
    ELCVNVACTG CL 112
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi2495130.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS464.1.
    PIRi JC4651.
    RefSeqi NP_009033.1. NM_007102.2.
    UniGenei Hs.32966.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UYA NMR - A 97-112 [» ]
    1UYB NMR - A 97-112 [» ]
    ProteinModelPortali Q16661.
    SMRi Q16661. Positions 27-111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000361662.

    Polymorphism databases

    DMDMi 2495130.

    Proteomic databases

    PaxDbi Q16661.
    PeptideAtlasi Q16661.
    PRIDEi Q16661.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372581 ; ENSP00000361662 ; ENSG00000044012 .
    GeneIDi 2981.
    KEGGi hsa:2981.
    UCSCi uc001chc.1. human.

    Organism-specific databases

    CTDi 2981.
    GeneCardsi GC01P042621.
    HGNCi HGNC:4683. GUCA2B.
    MIMi 601271. gene.
    neXtProti NX_Q16661.
    PharmGKBi PA29066.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45706.
    HOGENOMi HOG000231183.
    HOVERGENi HBG051861.
    InParanoidi Q16661.
    OMAi QSVYIQY.
    OrthoDBi EOG75TMFM.
    PhylomeDBi Q16661.
    TreeFami TF330731.

    Miscellaneous databases

    EvolutionaryTracei Q16661.
    GenomeRNAii 2981.
    NextBioi 11824.
    PROi Q16661.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16661.
    CleanExi HS_GUCA2B.
    Genevestigatori Q16661.

    Family and domain databases

    Gene3Di 3.90.1450.10. 1 hit.
    InterProi IPR000879. Guanylin.
    [Graphical view ]
    PANTHERi PTHR11318. PTHR11318. 1 hit.
    Pfami PF02058. Guanylin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001849. Guanylin. 1 hit.
    PRINTSi PR00774. GUANYLIN.
    ProDomi PD005588. Guanylin. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF89890. SSF89890. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 115 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