GCYB1_CANLF
ID GCYB1_CANLF Reviewed; 619 AA.
AC Q4ZHR9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Guanylate cyclase soluble subunit beta-1;
DE Short=GCS-beta-1;
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q02153};
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, GUCSB3, GUCY1B3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16113048; DOI=10.1152/ajplung.00186.2005;
RA Kwak Y.L., Jones K.A., Warner D.O., Perkins W.J.;
RT "NO responsiveness in pulmonary artery and airway smooth muscle: the role
RT of cGMP regulation.";
RL Am. J. Physiol. 290:L200-L208(2006).
CC -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the
CC biosynthesis of the signaling molecule cGMP.
CC {ECO:0000250|UniProtKB:P16068}.
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:0000250|UniProtKB:Q02153};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P16068};
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:0000250|UniProtKB:P16068};
CC -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC magnesium or manganese ions. {ECO:0000250|UniProtKB:Q02153}.
CC -!- SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a
CC beta subunit. Heterodimer with GUCY1A1. Can also form inactive
CC homodimers in vitro. {ECO:0000250|UniProtKB:Q02153}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}.
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; DQ008576; AAY26557.1; -; mRNA.
DR RefSeq; NP_001018044.1; NM_001018034.2.
DR AlphaFoldDB; Q4ZHR9; -.
DR SMR; Q4ZHR9; -.
DR STRING; 9612.ENSCAFP00000012587; -.
DR PaxDb; Q4ZHR9; -.
DR Ensembl; ENSCAFT00000013605; ENSCAFP00000012587; ENSCAFG00000008566.
DR Ensembl; ENSCAFT00030013161; ENSCAFP00030011502; ENSCAFG00030006818.
DR Ensembl; ENSCAFT00040025344; ENSCAFP00040022034; ENSCAFG00040013291.
DR Ensembl; ENSCAFT00845018777; ENSCAFP00845014661; ENSCAFG00845010585.
DR GeneID; 553102; -.
DR KEGG; cfa:553102; -.
DR CTD; 2983; -.
DR VEuPathDB; HostDB:ENSCAFG00845010585; -.
DR VGNC; VGNC:41568; GUCY1B1.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000157483; -.
DR InParanoid; Q4ZHR9; -.
DR OrthoDB; 531253at2759; -.
DR Proteomes; UP000002254; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; ISS: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; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW cGMP biosynthesis; Cytoplasm; GTP-binding; Heme; Iron; Lyase;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..619
FT /note="Guanylate cyclase soluble subunit beta-1"
FT /id="PRO_0000289600"
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:0000250|UniProtKB:P16068"
SQ SEQUENCE 619 AA; 70500 MW; 78AE4E661F769C7A CRC64;
MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN
LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN LDALHDHLAT IYPGMRAPSF
RCTDAEKGKG LILHYYSERE GLQDIVIGII KTVAQQIHGT EIDMKVIQQR NEECDHTQFL
IEEKESKEED FYEDLDRFEE NGTQESRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL
PQLQPGNCSL LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKL 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 TEETTQDDN
