GCYA1_HUMAN
ID GCYA1_HUMAN Reviewed; 690 AA.
AC Q02108; D3DP19; D6RDW3; O43843; Q8TAH3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Guanylate cyclase soluble subunit alpha-1 {ECO:0000305};
DE Short=GCS-alpha-1;
DE EC=4.6.1.2 {ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844, ECO:0000269|PubMed:9742212};
DE AltName: Full=Guanylate cyclase soluble subunit alpha-3 {ECO:0000303|PubMed:1352257};
DE Short=GCS-alpha-3;
DE AltName: Full=Soluble guanylate cyclase large subunit;
GN Name=GUCY1A1 {ECO:0000312|HGNC:HGNC:4685};
GN Synonyms=GUC1A3, GUCSA3, GUCY1A3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1352257; DOI=10.1016/0014-5793(92)80594-7;
RA Giuili G., Scholl U., Bulle F., Guellaeen G.;
RT "Molecular cloning of the cDNAs coding for the two subunits of soluble
RT guanylyl cyclase from human brain.";
RL FEBS Lett. 304:83-88(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Gansemans Y., Brouckaert P., Fiers W.;
RT "Human soluble guanylate cyclase large subunit mRNA, alpha3-like.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, INTERACTION WITH GUCY1B1, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9742212; DOI=10.1042/bj3350051;
RA Zabel U., Weeger M., La M., Schmidt H.H.;
RT "Human soluble guanylate cyclase: functional expression and revised
RT isoenzyme family.";
RL Biochem. J. 335:51-57(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8] {ECO:0007744|PDB:3UVJ}
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 468-690 IN COMPLEX WITH GUCY1B1,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, AND INTERACTION WITH
RP GUCY1B1.
RX PubMed=23505436; DOI=10.1371/journal.pone.0057644;
RA Allerston C.K., von Delft F., Gileadi O.;
RT "Crystal structures of the catalytic domain of human soluble guanylate
RT cyclase.";
RL PLoS ONE 8:E57644-E57644(2013).
RN [9]
RP INVOLVEMENT IN MYMY6.
RX PubMed=24581742; DOI=10.1016/j.ajhg.2014.01.018;
RA Herve D., Philippi A., Belbouab R., Zerah M., Chabrier S.,
RA Collardeau-Frachon S., Bergametti F., Essongue A., Berrou E., Krivosic V.,
RA Sainte-Rose C., Houdart E., Adam F., Billiemaz K., Lebret M., Roman S.,
RA Passemard S., Boulday G., Delaforge A., Guey S., Dray X., Chabriat H.,
RA Brouckaert P., Bryckaert M., Tournier-Lasserve E.;
RT "Loss of alpha1beta1 soluble guanylate cyclase, the major nitric oxide
RT receptor, leads to moyamoya and achalasia.";
RL Am. J. Hum. Genet. 94:385-394(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 468-662 IN COMPLEX WITH GUCY1B1,
RP INTERACTION WITH GUCY1B1, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=24669844; DOI=10.1021/bi500129k;
RA Seeger F., Quintyn R., Tanimoto A., Williams G.J., Tainer J.A.,
RA Wysocki V.H., Garcin E.D.;
RT "Interfacial residues promote an optimal alignment of the catalytic center
RT in human soluble guanylate cyclase: heterodimerization is required but not
RT sufficient for activity.";
RL Biochemistry 53:2153-2165(2014).
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:23505436, ECO:0000269|PubMed:24669844,
CC ECO:0000269|PubMed:9742212};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844};
CC Note=Has also activity with Mn(2+) (in vitro).
CC {ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844};
CC -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC magnesium or manganese ions. {ECO:0000269|PubMed:9742212}.
CC -!- SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a
CC beta subunit. Heterodimer with GUCY1B1 (PubMed:9742212,
CC PubMed:23505436, PubMed:24669844). {ECO:0000269|PubMed:23505436,
CC ECO:0000269|PubMed:24669844, ECO:0000269|PubMed:9742212}.
CC -!- INTERACTION:
CC Q02108; Q02153: GUCY1B1; NbExp=2; IntAct=EBI-3910037, EBI-6911707;
CC Q02108-1; Q02153-1: GUCY1B1; NbExp=2; IntAct=EBI-25372173, EBI-25372164;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02108-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02108-2; Sequence=VSP_045477;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex and lung (at protein
CC level). {ECO:0000269|PubMed:1352257}.
CC -!- DISEASE: Moyamoya disease 6 with or without achalasia (MYMY6)
CC [MIM:615750]: A form of Moyamoya disease, a progressive cerebral
CC angiopathy characterized by bilateral intracranial carotid artery
CC stenosis and telangiectatic vessels in the region of the basal ganglia.
CC The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral
CC angiogram. Affected individuals can develop transient ischemic attacks
CC and/or cerebral infarction, and rupture of the collateral vessels can
CC cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic
CC seizures constitute the prevailing presentation in childhood, while
CC subarachnoid bleeding occurs more frequently in adults. MYMY6 is
CC characterized by severe cerebral angiopathy and onset of severe
CC achalasia in infancy or early childhood. {ECO:0000269|PubMed:24581742}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA47145.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X66534; CAA47145.1; ALT_FRAME; mRNA.
DR EMBL; U58855; AAB94794.1; -; mRNA.
DR EMBL; Y15723; CAA75738.1; -; mRNA.
DR EMBL; AK309950; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC104083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04892.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04895.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04896.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04897.1; -; Genomic_DNA.
DR EMBL; BC028384; AAH28384.1; -; mRNA.
DR CCDS; CCDS34085.1; -. [Q02108-1]
DR CCDS; CCDS54812.1; -. [Q02108-2]
DR PIR; S23098; S23098.
DR RefSeq; NP_000847.2; NM_000856.5. [Q02108-1]
DR RefSeq; NP_001124154.1; NM_001130682.2. [Q02108-1]
DR RefSeq; NP_001124155.1; NM_001130683.3. [Q02108-1]
DR RefSeq; NP_001124156.1; NM_001130684.2. [Q02108-1]
DR RefSeq; NP_001124159.1; NM_001130687.2. [Q02108-2]
DR RefSeq; NP_001243378.1; NM_001256449.1. [Q02108-1]
DR RefSeq; XP_005263012.1; XM_005262955.2.
DR RefSeq; XP_006714259.1; XM_006714196.2.
DR RefSeq; XP_006714260.1; XM_006714197.2.
DR PDB; 3UVJ; X-ray; 2.08 A; A/C=468-690.
DR PDB; 4NI2; X-ray; 1.90 A; A=468-662.
DR PDB; 6JT0; EM; 4.00 A; A=1-690.
DR PDB; 6JT1; EM; 3.90 A; A=1-690.
DR PDB; 6JT2; EM; 3.80 A; A=1-690.
DR PDB; 7D9R; EM; 3.30 A; A=1-690.
DR PDB; 7D9S; EM; 3.40 A; A=1-690.
DR PDB; 7D9T; EM; 4.10 A; A=1-690.
DR PDB; 7D9U; EM; 3.80 A; A=1-690.
DR PDBsum; 3UVJ; -.
DR PDBsum; 4NI2; -.
DR PDBsum; 6JT0; -.
DR PDBsum; 6JT1; -.
DR PDBsum; 6JT2; -.
DR PDBsum; 7D9R; -.
DR PDBsum; 7D9S; -.
DR PDBsum; 7D9T; -.
DR PDBsum; 7D9U; -.
DR AlphaFoldDB; Q02108; -.
DR SMR; Q02108; -.
DR BioGRID; 109237; 44.
DR ComplexPortal; CPX-928; Soluble guanylate cyclase complex, SGCalpha1-SGCbeta1 variant.
DR CORUM; Q02108; -.
DR IntAct; Q02108; 5.
DR STRING; 9606.ENSP00000296518; -.
DR BindingDB; Q02108; -.
DR ChEMBL; CHEMBL3137281; -.
DR DrugBank; DB09401; Isosorbide.
DR DrugCentral; Q02108; -.
DR GuidetoPHARMACOLOGY; 1288; -.
DR iPTMnet; Q02108; -.
DR PhosphoSitePlus; Q02108; -.
DR BioMuta; GUCY1A3; -.
DR DMDM; 7404351; -.
DR jPOST; Q02108; -.
DR MassIVE; Q02108; -.
DR MaxQB; Q02108; -.
DR PaxDb; Q02108; -.
DR PeptideAtlas; Q02108; -.
DR PRIDE; Q02108; -.
DR ProteomicsDB; 14181; -.
DR ProteomicsDB; 58050; -. [Q02108-1]
DR Antibodypedia; 4394; 307 antibodies from 35 providers.
DR DNASU; 2982; -.
DR Ensembl; ENST00000296518.11; ENSP00000296518.7; ENSG00000164116.17. [Q02108-1]
DR Ensembl; ENST00000455639.6; ENSP00000412201.2; ENSG00000164116.17. [Q02108-1]
DR Ensembl; ENST00000506455.6; ENSP00000424361.1; ENSG00000164116.17. [Q02108-1]
DR Ensembl; ENST00000511108.5; ENSP00000421493.1; ENSG00000164116.17. [Q02108-1]
DR Ensembl; ENST00000511507.5; ENSP00000426968.1; ENSG00000164116.17. [Q02108-2]
DR Ensembl; ENST00000513574.1; ENSP00000426040.1; ENSG00000164116.17. [Q02108-1]
DR GeneID; 2982; -.
DR KEGG; hsa:2982; -.
DR MANE-Select; ENST00000506455.6; ENSP00000424361.1; NM_001130682.3; NP_001124154.1.
DR UCSC; uc003iov.4; human. [Q02108-1]
DR CTD; 2982; -.
DR DisGeNET; 2982; -.
DR GeneCards; GUCY1A1; -.
DR HGNC; HGNC:4685; GUCY1A1.
DR HPA; ENSG00000164116; Low tissue specificity.
DR MalaCards; GUCY1A1; -.
DR MIM; 139396; gene.
DR MIM; 615750; phenotype.
DR neXtProt; NX_Q02108; -.
DR OpenTargets; ENSG00000164116; -.
DR Orphanet; 401945; Moyamoya disease with early-onset achalasia.
DR PharmGKB; PA29067; -.
DR VEuPathDB; HostDB:ENSG00000164116; -.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000158285; -.
DR HOGENOM; CLU_011614_5_0_1; -.
DR InParanoid; Q02108; -.
DR OMA; SQTWFQK; -.
DR OrthoDB; 63831at2759; -.
DR PhylomeDB; Q02108; -.
DR TreeFam; TF351403; -.
DR BRENDA; 4.6.1.2; 2681.
DR PathwayCommons; Q02108; -.
DR Reactome; R-HSA-392154; Nitric oxide stimulates guanylate cyclase.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; Q02108; -.
DR SIGNOR; Q02108; -.
DR BioGRID-ORCS; 2982; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; GUCY1A3; human.
DR GeneWiki; GUCY1A3; -.
DR GenomeRNAi; 2982; -.
DR Pharos; Q02108; Tclin.
DR PRO; PR:Q02108; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q02108; protein.
DR Bgee; ENSG00000164116; Expressed in urethra and 204 other tissues.
DR ExpressionAtlas; Q02108; baseline and differential.
DR Genevisible; Q02108; HS.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IDA:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; TAS:ProtInc.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IEA:Ensembl.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
DR GO; GO:0098925; P:retrograde 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 3D-structure; Alternative splicing; cGMP biosynthesis; Cytoplasm;
KW GTP-binding; Lyase; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..690
FT /note="Guanylate cyclase soluble subunit alpha-1"
FT /id="PRO_0000074110"
FT DOMAIN 481..608
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERL9"
FT VAR_SEQ 625..690
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045477"
FT VARIANT 25
FT /note="V -> I (in dbSNP:rs2170646)"
FT /id="VAR_049257"
FT CONFLICT 44
FT /note="V -> M (in Ref. 7; AAH28384)"
FT /evidence="ECO:0000305"
FT CONFLICT 124..127
FT /note="AAGV -> QQS (in Ref. 1; CAA47145)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="Missing (in Ref. 1; CAA47145)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="C -> R (in Ref. 4; AK309950)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="L -> V (in Ref. 7; AAH28384)"
FT /evidence="ECO:0000305"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 165..170
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 364..373
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 409..457
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 460..467
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 472..487
FT /evidence="ECO:0007829|PDB:4NI2"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:4NI2"
FT HELIX 499..519
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 533..540
FT /evidence="ECO:0007829|PDB:4NI2"
FT HELIX 545..560
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 573..587
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:4NI2"
FT HELIX 599..609
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:4NI2"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:4NI2"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:4NI2"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 655..660
FT /evidence="ECO:0007829|PDB:4NI2"
SQ SEQUENCE 690 AA; 77452 MW; DA1E14A5E11451CF CRC64;
MFCTKLKDLK ITGECPFSLL APGQVPNESS EEAAGSSESC KATVPICQDI PEKNIQESLP
QRKTSRSRVY LHTLAESICK LIFPEFERLN VALQRTLAKH KIKESRKSLE REDFEKTIAE
QAVAAGVPVE VIKESLGEEV FKICYEEDEN ILGVVGGTLK DFLNSFSTLL KQSSHCQEAG
KRGRLEDASI LCLDKEDDFL HVYYFFPKRT TSLILPGIIK AAAHVLYETE VEVSLMPPCF
HNDCSEFVNQ PYLLYSVHMK STKPSLSPSK PQSSLVIPTS LFCKTFPFHF MFDKDMTILQ
FGNGIRRLMN RRDFQGKPNF EEYFEILTPK INQTFSGIMT MLNMQFVVRV RRWDNSVKKS
SRVMDLKGQM IYIVESSAIL FLGSPCVDRL EDFTGRGLYL SDIPIHNALR DVVLIGEQAR
AQDGLKKRLG KLKATLEQAH QALEEEKKKT VDLLCSIFPC EVAQQLWQGQ VVQAKKFSNV
TMLFSDIVGF TAICSQCSPL QVITMLNALY TRFDQQCGEL DVYKVETIGD AYCVAGGLHK
ESDTHAVQIA LMALKMMELS DEVMSPHGEP IKMRIGLHSG SVFAGVVGVK MPRYCLFGNN
VTLANKFESC SVPRKINVSP TTYRLLKDCP GFVFTPRSRE ELPPNFPSEI PGICHFLDAY
QQGTNSKPCF QKKDVEDGNA NFLGKASGID
