GCYB1_RAT
ID GCYB1_RAT Reviewed; 619 AA.
AC P20595; Q8CH88;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 170.
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, Gucy1b3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2905128; DOI=10.1016/s0006-291x(88)80992-6;
RA Nakane M., Saheki S., Kuno T., Ishii K., Murad F.;
RT "Molecular cloning of a cDNA coding for 70 kilodalton subunit of soluble
RT guanylate cyclase from rat lung.";
RL Biochem. Biophys. Res. Commun. 157:1139-1147(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain cortex;
RA Nakamura I., Suzuki N.;
RT "Rat soluble guanylyl cyclase beta 1 subunit.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 348-409, AND SUBUNIT.
RX PubMed=20105301; DOI=10.1186/1472-6807-10-2;
RA Ma X., Beuve A., van den Akker F.;
RT "Crystal structure of the signaling helix coiled-coil domain of the beta1
RT subunit of the soluble guanylyl cyclase.";
RL BMC Struct. Biol. 10:2-2(2010).
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. Homotetramer; dimer of dimers (in vitro)
CC (PubMed:20105301). Heterodimer with GUCY1A1. Can also form inactive
CC homodimers in vitro (By similarity). {ECO:0000250|UniProtKB:Q02153,
CC ECO:0000269|PubMed:20105301}.
CC -!- INTERACTION:
CC P20595; P31016: Dlg4; NbExp=2; IntAct=EBI-7980539, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}.
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; M22562; AAA41204.1; -; mRNA.
DR EMBL; AB098025; BAC44989.1; -; mRNA.
DR EMBL; BC081840; AAH81840.1; -; mRNA.
DR PIR; A31871; OYRTB1.
DR RefSeq; NP_036901.2; NM_012769.2.
DR PDB; 3HLS; X-ray; 2.15 A; A/B/C/D/E/F/G/H=348-409.
DR PDBsum; 3HLS; -.
DR AlphaFoldDB; P20595; -.
DR SMR; P20595; -.
DR IntAct; P20595; 3.
DR MINT; P20595; -.
DR STRING; 10116.ENSRNOP00000062785; -.
DR iPTMnet; P20595; -.
DR jPOST; P20595; -.
DR PaxDb; P20595; -.
DR PRIDE; P20595; -.
DR Ensembl; ENSRNOT00000064930; ENSRNOP00000062785; ENSRNOG00000012060.
DR GeneID; 25202; -.
DR KEGG; rno:25202; -.
DR UCSC; RGD:2769; rat.
DR CTD; 2983; -.
DR RGD; 2769; Gucy1b1.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000157483; -.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; P20595; -.
DR OMA; PCEDHAK; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; P20595; -.
DR TreeFam; TF351403; -.
DR BRENDA; 4.6.1.2; 5301.
DR EvolutionaryTrace; P20595; -.
DR PRO; PR:P20595; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012060; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P20595; RN.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IDA:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:SynGO.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; ISO:RGD.
DR GO; GO:0020037; F:heme binding; IDA:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:RGD.
DR GO; GO:0043167; F:ion binding; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISO:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:RGD.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS: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; ISO:RGD.
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 3D-structure; 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_0000074118"
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"
FT CONFLICT 33
FT /note="E -> Q (in Ref. 1; AAA41204)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="D -> H (in Ref. 1; AAA41204)"
FT /evidence="ECO:0000305"
FT HELIX 349..396
FT /evidence="ECO:0007829|PDB:3HLS"
FT HELIX 400..407
FT /evidence="ECO:0007829|PDB:3HLS"
SQ SEQUENCE 619 AA; 70456 MW; 9F4B49E341975184 CRC64;
MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN
LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN LDALHDHLAT IYPGMRAPSF
RCTDAEKGKG LILHYYSERE GLQDIVIGII KTVAQQIHGT EIDMKVIQQR SEECDHTQFL
IEEKESKEED FYEDLDRFEE NGTQDSRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL
PQLQPGKCSL LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKL ECEDELTGAE
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 CLMSPENSDP QFHLEHRGPV SMKGKKEPMQ
VWFLSRKNTG TEETNQDEN
