ID B7Z6G8_HUMAN Unreviewed; 641 AA.
AC B7Z6G8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Guanylate cyclase soluble subunit beta-1 {ECO:0000256|ARBA:ARBA00039698};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
DE AltName: Full=Guanylate cyclase soluble subunit beta-3 {ECO:0000256|ARBA:ARBA00041698};
DE AltName: Full=Soluble guanylate cyclase small subunit {ECO:0000256|ARBA:ARBA00043208};
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 {ECO:0000313|EMBL:BAH13254.1};
RN [1] {ECO:0000313|EMBL:BAH13254.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Placenta {ECO:0000313|EMBL:BAH13254.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the
CC biosynthesis of the signaling molecule cGMP.
CC {ECO:0000256|ARBA:ARBA00037442}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK300296; BAH13254.1; -; mRNA.
DR RefSeq; NP_001278880.1; NM_001291951.1.
DR AlphaFoldDB; B7Z6G8; -.
DR PeptideAtlas; B7Z6G8; -.
DR DNASU; 2983; -.
DR GeneID; 2983; -.
DR CTD; 2983; -.
DR OrthoDB; 2898719at2759; -.
DR BioGRID-ORCS; 2983; 8 hits in 1143 CRISPR screens.
DR GenomeRNAi; 2983; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 6.10.250.780; -; 1.
DR Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 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 PANTHER; PTHR45655:SF2; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1; 1.
DR PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07700; HNOB; 2.
DR Pfam; PF07701; HNOBA; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134}.
FT DOMAIN 443..576
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 641 AA; 73058 MW; 2BE988D59B2E91AC CRC64;
MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR ILYDDSKTYD LVAAASKVLN
LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQK NESKHISDLH HCFLGIYLCC
NNLDALHDHL ATIYPGMRAP SFRCTDAEKG KGLILHYYSE REGLQDIVIG IIKTVAQQIH
GTEVDMKVIQ QRNEECDHTQ FLIEEKESKE EDFYEDLDRF EENGTQESRI SPYTFCKAFP
FHIIFDRDLV VTQCGNAIYR VLPQLQPGNC SLLSVFSLVR PHIDISFHGI LSHINTVFVL
RSKEGLLDVE KLECEDELTG TEISCLRLKG QMIYLPEADS ILFLCSPSVM NLDDLTRRGL
YLSDIPLHDA TRDLVLLGEQ FREEYKLTQE LEILTDRLQL TLRALEDEKK KTDTLLYSVL
PPSVANELRH KRPVPAKRYD NVTILFSGIV GFNAFCSKHA SGEGAMKIVN LLNDLYTRFD
TLTDSRENPF VYKVETVGDK YMTVSGLPEP CIHHARSICH LALDMMEIAG QVQVDGESVQ
ITIGIHTGEV VTGVIGQRMP RYCLFGNTVN LTSRTETTGE KGKINVSEYT YRCLMSPENS
DPQFHLEHRG PVSMKGKKEP MQVWFLSRKN TGTEETKQDD D
//
