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P16068

- GCYB1_BOVIN

UniProt

P16068 - GCYB1_BOVIN

Protein

Guanylate cyclase soluble subunit beta-1

Gene

GUCY1B1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    GTP = 3',5'-cyclic GMP + diphosphate.

    Cofactori

    Binds 1 or 2 heme groups per heterodimer.

    Enzyme regulationi

    Activated by nitric oxide in the presence of magnesium or manganese ions, binding of NO to the heme iron increases catalytic activity up to 400 folds.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi105 – 1051Iron (heme proximal ligand)

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. guanylate cyclase activity Source: UniProtKB-EC
    3. heme binding Source: AgBase
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. intracellular signal transduction Source: InterPro
    2. ion transport Source: UniProtKB-KW
    3. iron ion homeostasis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    cGMP biosynthesis, Ion transport, Iron transport, Transport

    Keywords - Ligandi

    GTP-binding, Heme, Iron, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_208097. Nitric oxide stimulates guanylate cyclase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanylate cyclase soluble subunit beta-1 (EC:4.6.1.2)
    Short name:
    GCS-beta-1
    Alternative name(s):
    Guanylate cyclase soluble subunit beta-3
    Short name:
    GCS-beta-3
    Soluble guanylate cyclase small subunit
    Gene namesi
    Name:GUCY1B1
    Synonyms:GUC1B3, GUCY1B3
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 17

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 619619Guanylate cyclase soluble subunit beta-1PRO_0000074115Add
    BLAST

    Proteomic databases

    PRIDEiP16068.

    Expressioni

    Tissue specificityi

    Lung and brain.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Structurei

    Secondary structure

    1
    619
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi415 – 42612
    Helixi428 – 4314
    Beta strandi437 – 4404
    Helixi441 – 4433
    Helixi444 – 46219
    Beta strandi469 – 4757
    Beta strandi478 – 4836
    Helixi490 – 4923
    Helixi493 – 50614
    Turni507 – 5093
    Beta strandi520 – 53314
    Beta strandi539 – 5413
    Helixi545 – 55612
    Helixi566 – 5694

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AWNmodel-B412-572[»]
    ProteinModelPortaliP16068.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini421 – 554134Guanylate cyclasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
    Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2114.
    GeneTreeiENSGT00750000117642.
    HOGENOMiHOG000220903.
    HOVERGENiHBG051715.
    InParanoidiP16068.
    KOiK12319.
    OMAiVLMSEQF.

    Family and domain databases

    Gene3Di3.30.70.1230. 1 hit.
    InterProiIPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR011645. Haem_no_assoc-bd.
    IPR011644. Heme_NO-bd.
    IPR024096. NO_sig/Golgi_transp_ligand-bd.
    [Graphical view]
    PfamiPF00211. Guanylate_cyc. 1 hit.
    PF07700. HNOB. 1 hit.
    PF07701. HNOBA. 1 hit.
    [Graphical view]
    SMARTiSM00044. CYCc. 1 hit.
    [Graphical view]
    SUPFAMiSSF111126. SSF111126. 1 hit.
    SSF55073. SSF55073. 1 hit.
    PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
    PS50125. GUANYLATE_CYCLASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16068-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD    50
    LVAAASKVLN LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN 100
    LDALHDHLAT IYPGMRAPSF RCTDADKGKG LILHYYSERE GLQDIVIGII 150
    KTVAQQIHGT EIDMKVIQQR NEECDHTQFL IEEKESKEED FYEDLDRFEE 200
    NGTQESRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL PQLQPGNCSL 250
    LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKS ECEDELTGTE 300
    ISCLRLKGQM IYLPEADSIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR 350
    DLVLLGEQFR EEYKLTQELE ILTDRLQLTL RALEDEKKKT DTLLYSVLPP 400
    SVANELRHKR PVPAKRYDNV TILFSGIVGF NAFCSKHASG EGAMKIVNLL 450
    NDLYTRFDTL TDSRKNPFVY KVETVGDKYM TVSGLPEPCI HHARSICHLA 500
    LDMMEIAGQV QVDGESVQIT IGIHTGEVVT GVIGQRMPRY CLFGNTVNLT 550
    SRTETTGEKG KINVSEYTYR CLMTPENSDP QFHLEHRGPV SMKGKKEPMQ 600
    VWFLSRKNTG TEETEQDEN 619
    Length:619
    Mass (Da):70,502
    Last modified:April 1, 1990 - v1
    Checksum:i8EFB14952B80F344
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00770 mRNA. Translation: CAA68739.1.
    BC133308 mRNA. Translation: AAI33309.1.
    PIRiS01653. OYBO70.
    RefSeqiNP_777066.1. NM_174641.1.
    UniGeneiBt.109786.

    Genome annotation databases

    EnsembliENSBTAT00000005009; ENSBTAP00000005009; ENSBTAG00000003840.
    GeneIDi282433.
    KEGGibta:282433.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00770 mRNA. Translation: CAA68739.1 .
    BC133308 mRNA. Translation: AAI33309.1 .
    PIRi S01653. OYBO70.
    RefSeqi NP_777066.1. NM_174641.1.
    UniGenei Bt.109786.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AWN model - B 412-572 [» ]
    ProteinModelPortali P16068.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P16068.

    Proteomic databases

    PRIDEi P16068.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000005009 ; ENSBTAP00000005009 ; ENSBTAG00000003840 .
    GeneIDi 282433.
    KEGGi bta:282433.

    Organism-specific databases

    CTDi 2983.

    Phylogenomic databases

    eggNOGi COG2114.
    GeneTreei ENSGT00750000117642.
    HOGENOMi HOG000220903.
    HOVERGENi HBG051715.
    InParanoidi P16068.
    KOi K12319.
    OMAi VLMSEQF.

    Enzyme and pathway databases

    Reactomei REACT_208097. Nitric oxide stimulates guanylate cyclase.

    Miscellaneous databases

    NextBioi 20806209.

    Family and domain databases

    Gene3Di 3.30.70.1230. 1 hit.
    InterProi IPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR011645. Haem_no_assoc-bd.
    IPR011644. Heme_NO-bd.
    IPR024096. NO_sig/Golgi_transp_ligand-bd.
    [Graphical view ]
    Pfami PF00211. Guanylate_cyc. 1 hit.
    PF07700. HNOB. 1 hit.
    PF07701. HNOBA. 1 hit.
    [Graphical view ]
    SMARTi SM00044. CYCc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111126. SSF111126. 1 hit.
    SSF55073. SSF55073. 1 hit.
    PROSITEi PS00452. GUANYLATE_CYCLASE_1. 1 hit.
    PS50125. GUANYLATE_CYCLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of the 70 kDa subunit of bovine soluble guanylate cyclase."
      Koesling D., Herz J., Gausepohl H., Niroomand F., Hinsch K.-D., Muelsch A., Boehme E., Schultz G., Frank R.
      FEBS Lett. 239:29-34(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Lung.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Brain cortex.
    3. "Mutation of His-105 in the beta 1 subunit yields a nitric oxide-insensitive form of soluble guanylyl cyclase."
      Wedel B., Humbert P., Harteneck C., Foerster J., Malkewitz J., Bohme E., Schultz G., Koesling D.
      Proc. Natl. Acad. Sci. U.S.A. 91:2592-2596(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HISTIDINE RESIDUES.
    4. "Identification of histidine 105 in the beta1 subunit of soluble guanylate cyclase as the heme proximal ligand."
      Zhao Y., Schelvis J.P., Babcock G.T., Marletta M.A.
      Biochemistry 37:4502-4509(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEME PROXIMAL LIGAND.
    5. "Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis."
      Liu Y., Ruoho A.E., Rao V.D., Hurley J.H.
      Proc. Natl. Acad. Sci. U.S.A. 94:13414-13419(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 412-572.

    Entry informationi

    Entry nameiGCYB1_BOVIN
    AccessioniPrimary (citable) accession number: P16068
    Secondary accession number(s): A2VDM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two types of guanylate cyclases: soluble forms and membrane-associated receptor forms.

    Keywords - Technical termi

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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3