GCYB1_BOVIN
ID GCYB1_BOVIN Reviewed; 619 AA.
AC P16068; A2VDM4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Guanylate cyclase soluble subunit beta-1;
DE Short=GCS-beta-1;
DE EC=4.6.1.2 {ECO:0000269|PubMed:7908439};
DE AltName: Full=Guanylate cyclase soluble subunit beta-3;
DE Short=GCS-beta-3;
DE AltName: Full=Soluble guanylate cyclase small subunit;
GN Name=GUCY1B1; Synonyms=GUC1B3, GUCY1B3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=2903071; DOI=10.1016/0014-5793(88)80539-8;
RA Koesling D., Herz J., Gausepohl H., Niroomand F., Hinsch K.-D., Muelsch A.,
RA Boehme E., Schultz G., Frank R.;
RT "The primary structure of the 70 kDa subunit of bovine soluble guanylate
RT cyclase.";
RL FEBS Lett. 239:29-34(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MUTAGENESIS OF HIS-105, CATALYTIC ACTIVITY, SUBUNIT, FUNCTION, COFACTOR,
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=7908439; DOI=10.1073/pnas.91.7.2592;
RA Wedel B., Humbert P., Harteneck C., Foerster J., Malkewitz J., Bohme E.,
RA Schultz G., Koesling D.;
RT "Mutation of His-105 in the beta 1 subunit yields a nitric oxide-
RT insensitive form of soluble guanylyl cyclase.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2592-2596(1994).
RN [4]
RP HEME PROXIMAL LIGAND, MUTAGENESIS OF HIS-105, COFACTOR, AND SUBUNIT.
RX PubMed=9521770; DOI=10.1021/bi972686m;
RA Zhao Y., Schelvis J.P., Babcock G.T., Marletta M.A.;
RT "Identification of histidine 105 in the beta1 subunit of soluble guanylate
RT cyclase as the heme proximal ligand.";
RL Biochemistry 37:4502-4509(1998).
RN [5]
RP 3D-STRUCTURE MODELING OF 412-572.
RX PubMed=9391039; DOI=10.1073/pnas.94.25.13414;
RA Liu Y., Ruoho A.E., Rao V.D., Hurley J.H.;
RT "Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and
RT mutational analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13414-13419(1997).
CC -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the
CC biosynthesis of the signaling molecule cGMP.
CC {ECO:0000269|PubMed:7908439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:7908439};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:7908439, ECO:0000269|PubMed:9521770};
CC Note=Binds 1 or 2 heme groups per heterodimer. Heme is required for
CC responding to nitric oxide, but not for catalytic activity.
CC {ECO:0000269|PubMed:7908439, ECO:0000269|PubMed:9521770};
CC -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC magnesium or manganese ions, binding of NO to the heme iron increases
CC catalytic activity up to 400 folds. {ECO:0000269|PubMed:7908439}.
CC -!- SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a
CC beta subunit (PubMed:7908439, PubMed:9521770). Heterodimer with
CC GUCY1A1. Can also form inactive homodimers in vitro.
CC {ECO:0000250|UniProtKB:Q02153, ECO:0000269|PubMed:7908439,
CC ECO:0000269|PubMed:9521770}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7908439}.
CC -!- TISSUE SPECIFICITY: Lung and brain.
CC -!- MISCELLANEOUS: There are two types of guanylate cyclases: soluble forms
CC and membrane-associated receptor forms.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; Y00770; CAA68739.1; -; mRNA.
DR EMBL; BC133308; AAI33309.1; -; mRNA.
DR PIR; S01653; OYBO70.
DR RefSeq; NP_777066.1; NM_174641.1.
DR AlphaFoldDB; P16068; -.
DR SMR; P16068; -.
DR STRING; 9913.ENSBTAP00000055570; -.
DR PaxDb; P16068; -.
DR PRIDE; P16068; -.
DR Ensembl; ENSBTAT00000005009; ENSBTAP00000005009; ENSBTAG00000003840.
DR GeneID; 282433; -.
DR KEGG; bta:282433; -.
DR CTD; 2983; -.
DR VEuPathDB; HostDB:ENSBTAG00000003840; -.
DR VGNC; VGNC:29721; GUCY1B1.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000157483; -.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; P16068; -.
DR OMA; PCEDHAK; -.
DR OrthoDB; 531253at2759; -.
DR BRENDA; 4.6.1.2; 908.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000003840; Expressed in occipital lobe and 108 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
DR GO; GO:0099555; P:trans-synaptic signaling by nitric oxide, modulating synaptic transmission; IEA:Ensembl.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.450.260; -; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.90.1520.10; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR038158; H-NOX_domain_sf.
DR InterPro; IPR011644; Heme_NO-bd.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR042463; HNOB_dom_associated_sf.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07700; HNOB; 1.
DR Pfam; PF07701; HNOBA; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 1: Evidence at protein level;
KW cGMP biosynthesis; Cytoplasm; Direct protein sequencing; GTP-binding; Heme;
KW Iron; Lyase; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..619
FT /note="Guanylate cyclase soluble subunit beta-1"
FT /id="PRO_0000074115"
FT DOMAIN 421..554
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 105
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:7908439,
FT ECO:0000269|PubMed:9521770"
FT MUTAGEN 105
FT /note="H->A,G: Abolishes heme binding."
FT /evidence="ECO:0000269|PubMed:9521770"
FT MUTAGEN 105
FT /note="H->F: Does not affect basal levels of enzyme
FT activity, but abolishes stimulation by nitric oxide."
FT /evidence="ECO:0000269|PubMed:7908439"
SQ SEQUENCE 619 AA; 70502 MW; 8EFB14952B80F344 CRC64;
MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN
LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN LDALHDHLAT IYPGMRAPSF
RCTDADKGKG LILHYYSERE GLQDIVIGII KTVAQQIHGT EIDMKVIQQR NEECDHTQFL
IEEKESKEED FYEDLDRFEE NGTQESRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL
PQLQPGNCSL LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKS ECEDELTGTE
ISCLRLKGQM IYLPEADSIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR DLVLLGEQFR
EEYKLTQELE ILTDRLQLTL RALEDEKKKT DTLLYSVLPP SVANELRHKR PVPAKRYDNV
TILFSGIVGF NAFCSKHASG EGAMKIVNLL NDLYTRFDTL TDSRKNPFVY KVETVGDKYM
TVSGLPEPCI HHARSICHLA LDMMEIAGQV QVDGESVQIT IGIHTGEVVT GVIGQRMPRY
CLFGNTVNLT SRTETTGEKG KINVSEYTYR CLMTPENSDP QFHLEHRGPV SMKGKKEPMQ
VWFLSRKNTG TEETEQDEN
