GCYA1_BOVIN
ID GCYA1_BOVIN Reviewed; 691 AA.
AC P19687;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Guanylate cyclase soluble subunit alpha-1;
DE Short=GCS-alpha-1;
DE EC=4.6.1.2;
DE AltName: Full=Soluble guanylate cyclase large subunit;
GN Name=GUCY1A1; Synonyms=GUC1A1;
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=Adrenal medulla;
RX PubMed=1973124; DOI=10.1016/0014-5793(90)81523-q;
RA Koesling D., Harteneck C., Humbert P., Bosserhoff A., Frank R., Schultz G.,
RA Boehme E.;
RT "The primary structure of the larger subunit of soluble guanylyl cyclase
RT from bovine lung. Homology between the two subunits of the enzyme.";
RL FEBS Lett. 266:128-132(1990).
RN [2]
RP 3D-STRUCTURE MODELING OF 472-628.
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 -!- 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 -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC magnesium or manganese ions.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X54014; CAA37960.1; -; mRNA.
DR PIR; S10713; OYBO77.
DR RefSeq; NP_786972.1; NM_175778.2.
DR RefSeq; XP_005217697.1; XM_005217640.3.
DR RefSeq; XP_005217698.1; XM_005217641.3.
DR RefSeq; XP_005217699.1; XM_005217642.3.
DR RefSeq; XP_005217700.1; XM_005217643.3.
DR RefSeq; XP_010812116.1; XM_010813814.2.
DR RefSeq; XP_015330913.1; XM_015475427.1.
DR AlphaFoldDB; P19687; -.
DR SMR; P19687; -.
DR STRING; 9913.ENSBTAP00000019398; -.
DR ChEMBL; CHEMBL3915; -.
DR PaxDb; P19687; -.
DR PRIDE; P19687; -.
DR Ensembl; ENSBTAT00000019398; ENSBTAP00000019398; ENSBTAG00000014576.
DR Ensembl; ENSBTAT00000072427; ENSBTAP00000073199; ENSBTAG00000014576.
DR Ensembl; ENSBTAT00000074007; ENSBTAP00000064987; ENSBTAG00000014576.
DR Ensembl; ENSBTAT00000080766; ENSBTAP00000070720; ENSBTAG00000014576.
DR GeneID; 281216; -.
DR KEGG; bta:281216; -.
DR CTD; 2982; -.
DR VEuPathDB; HostDB:ENSBTAG00000014576; -.
DR VGNC; VGNC:29720; GUCY1A1.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000158285; -.
DR HOGENOM; CLU_011614_5_1_1; -.
DR InParanoid; P19687; -.
DR OMA; SQTWFQK; -.
DR OrthoDB; 531253at2759; -.
DR TreeFam; TF351403; -.
DR BRENDA; 4.6.1.2; 908.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000014576; Expressed in oviduct epithelium and 106 other tissues.
DR ExpressionAtlas; P19687; baseline and differential.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
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; 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; 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;
KW Lyase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..691
FT /note="Guanylate cyclase soluble subunit alpha-1"
FT /id="PRO_0000074108"
FT DOMAIN 482..609
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 26..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 77533 MW; 5D1FE4D2204E8683 CRC64;
MFCAKLKDLQ ITGDCPFSLL APGQVPREPL GEATGSGPAS TPGQPGVCPG VPDKNPPGRL
PRRKTSRSRV YLHTLAESIC KLIFPEFERL NLALQRTLAK HKIKENRKSL EREDFEKIVV
DQAIAAGVPV EIIKESLGEE LFKICYEEDE YILGVVGGTL KDFLNSFSTL LKQSSHCQEA
EKKGRFEDAS ILCLDKDPDV LYVYYFFPKR ITSLILPGII KAAARILYET EVEVSSTPSR
FHQDCREFVD QPCELYSVHI RSARPHPPPG KPVSSLVIPA SLFCKTFPFH FMLDRDMSIL
QLGHGIRRLM SRRDVQGKPH FDEYFEILTP KISQTFSGIM TMLNMQFLVR VRRWDNSMKK
SSRVMDLKGQ MIYMVESSSI LFLGSPCVDR LEDFTGRGLY LSDIPIHNAL RDVVLIGEQA
RAQDGLKKRL GKLKATLEQA HQALEEEKRK TVDLLCSIFP SEVARQLWQG HAVQAKRFGN
VTMLFSDIVG FTAICSQCSP LQVITMLNAL YTRFDRQCGE LDVYKVETIG DAYCVAGGLH
KESDTHAVQI ALMALKMMEL SHEVVSPHGE PIKMRIGLHS GSVFAGVVGV KMPRYCLFGN
NVTLANKFES CSVPRKINVS PTTYRLLKDC PGFVFTPRSR EELPPNFPSD IPGICHFLEA
YQQGTTSKPW FQKKDVEEAN ANFLGKASGI D
