GCYA1_MOUSE
ID GCYA1_MOUSE Reviewed; 691 AA.
AC Q9ERL9; Q6GTG0; Q9DBQ3;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Guanylate cyclase soluble subunit alpha-1;
DE Short=GCS-alpha-1;
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q02108};
DE AltName: Full=Guanylate cyclase soluble subunit alpha-3;
DE Short=GCS-alpha-3;
DE AltName: Full=Soluble guanylate cyclase large subunit;
GN Name=Gucy1a1; Synonyms=Gucy1a3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=10984516; DOI=10.1073/pnas.190331697;
RA Sharina I.G., Krumenacker J.S., Martin E., Murad F.;
RT "Genomic organization of alpha 1 and beta 1 subunits of the mammalian
RT soluble guanylyl cyclase genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10878-10883(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:Q02108};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q02108};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q02108};
CC Note=Has also activity with Mn(2+) (in vitro).
CC {ECO:0000250|UniProtKB:Q02108};
CC -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC magnesium or manganese ions. {ECO:0000250|UniProtKB:Q02108}.
CC -!- SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a
CC beta subunit. Heterodimer with GUCY1B1. {ECO:0000250|UniProtKB:Q02108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; AF297082; AAG17446.1; -; mRNA.
DR EMBL; AK004815; BAB23586.1; -; mRNA.
DR EMBL; AK028558; BAC26009.1; -; mRNA.
DR EMBL; BC057327; AAH57327.1; -; mRNA.
DR EMBL; BC094310; AAH94310.1; -; mRNA.
DR CCDS; CCDS17429.1; -.
DR RefSeq; NP_068696.2; NM_021896.5.
DR RefSeq; XP_006501906.1; XM_006501843.3.
DR RefSeq; XP_011238486.1; XM_011240184.1.
DR AlphaFoldDB; Q9ERL9; -.
DR SMR; Q9ERL9; -.
DR STRING; 10090.ENSMUSP00000048918; -.
DR GlyConnect; 2364; 1 N-Linked glycan (1 site).
DR GlyGen; Q9ERL9; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9ERL9; -.
DR PhosphoSitePlus; Q9ERL9; -.
DR SwissPalm; Q9ERL9; -.
DR MaxQB; Q9ERL9; -.
DR PaxDb; Q9ERL9; -.
DR PeptideAtlas; Q9ERL9; -.
DR PRIDE; Q9ERL9; -.
DR ProteomicsDB; 267783; -.
DR Antibodypedia; 4394; 307 antibodies from 35 providers.
DR DNASU; 60596; -.
DR Ensembl; ENSMUST00000048976; ENSMUSP00000048918; ENSMUSG00000033910.
DR Ensembl; ENSMUST00000193924; ENSMUSP00000142138; ENSMUSG00000033910.
DR GeneID; 60596; -.
DR KEGG; mmu:60596; -.
DR UCSC; uc008pou.2; mouse.
DR CTD; 2982; -.
DR MGI; MGI:1926562; Gucy1a1.
DR VEuPathDB; HostDB:ENSMUSG00000033910; -.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000158285; -.
DR HOGENOM; CLU_011614_5_0_1; -.
DR InParanoid; Q9ERL9; -.
DR OMA; SQTWFQK; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q9ERL9; -.
DR TreeFam; TF351403; -.
DR BioGRID-ORCS; 60596; 7 hits in 71 CRISPR screens.
DR PRO; PR:Q9ERL9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9ERL9; protein.
DR Bgee; ENSMUSG00000033910; Expressed in olfactory tubercle and 274 other tissues.
DR ExpressionAtlas; Q9ERL9; baseline and differential.
DR Genevisible; Q9ERL9; MM.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004016; F:adenylate cyclase activity; ISO:MGI.
DR GO; GO:0047805; F:cytidylate cyclase activity; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0043167; F:ion binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006182; P:cGMP biosynthetic process; IMP:MGI.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IMP:MGI.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IMP:MGI.
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; IDA:SynGO.
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; GTP-binding; Lyase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..691
FT /note="Guanylate cyclase soluble subunit alpha-1"
FT /id="PRO_0000074111"
FT DOMAIN 480..607
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 690
FT /note="I -> V (in Ref. 1; AAG17446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 77588 MW; FF8DD0C3CB0BBD7F CRC64;
MFCRKFKDLK ITGECPFSLL APGQVPKEPT EEVAGGSEGC QATLPICQYF PEKNAEGSLP
QRKTSRNRVY LHTLAESICK LIFPECERLN LALQRTLAKH KIEENRKSSE KEDLEKIIAE
EAIAAGAPVE ALKDSLGEEL FKICYEEDEH ILGVVGGTLK DFLNSFSTLL KQSSHCQEAE
RRGRLEDASI LCLDKDQDFL NVYYFFPKRT TALLLPGIIK AAARILYESH VEVSLMPPCF
RSDCTEFVNQ PYLLYSVHVK STKPSLSPGK PQSSLVIPAS LFCKTFPFHF MLDRDLAILQ
LGNGIRRLVN KRDFQGKPNF EEFFEILTPK INQTFSGIMT MLNMQFVIRV RRWDNSVKKS
SRVMDLKGQM IYIVESSAIL FLGSPCVDRL EDFTGRGLYL SDIPIHNALR DVVLIGEQAR
AQDGLKKRLG KLKATLEHAH QALEEEKKRT VDLLCSIFPS EVAQQLWQGQ IVQAKKFSEV
TMLFSDIVGF TAICSQCSPL QVITMLNALY TRFDQQCGEL DVYKVETIGD AYCVAGGLHR
ESDTHAVQIA LMALKMMELS NEVMSPHGEP IKMRIGLHSG SVFAGVVGVK MPRYCLFGNN
VTLANKFESC SVPRKINVSP TTYRLLKDCP GFVFTPRSRE ELPPNFPSDI PGICHFLDAY
HHQGPNSKPW FQDKDVEDGN ANFLGKASGI D
