ID   GCYB2_RAT               Reviewed;         682 AA.
AC   P22717;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Guanylate cyclase soluble subunit beta-2;
DE            Short=GCS-beta-2;
DE            EC=4.6.1.2;
GN   Name=Gucy1b2;
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].
RC   TISSUE=Kidney;
RX   PubMed=1980215; DOI=10.1021/bi00501a002;
RA   Yuen P.S.T., Potter L.R., Garbers D.L.;
RT   "A new form of guanylyl cyclase is preferentially expressed in rat
RT   kidney.";
RL   Biochemistry 29:10872-10878(1990).
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 or 2 heme groups per heterodimer. {ECO:0000250};
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   -!- TISSUE SPECIFICITY: Kidney and liver.
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; M57507; AAA41207.1; -; mRNA.
DR   PIR; A36228; OYRTB2.
DR   RefSeq; NP_001257640.1; NM_001270711.1.
DR   RefSeq; NP_036902.2; NM_012770.2.
DR   AlphaFoldDB; P22717; -.
DR   SMR; P22717; -.
DR   STRING; 10116.ENSRNOP00000012948; -.
DR   PaxDb; P22717; -.
DR   PRIDE; P22717; -.
DR   GeneID; 25206; -.
DR   KEGG; rno:25206; -.
DR   UCSC; RGD:2770; rat.
DR   CTD; 2974; -.
DR   RGD; 2770; Gucy1b2.
DR   eggNOG; KOG4171; Eukaryota.
DR   InParanoid; P22717; -.
DR   OrthoDB; 531253at2759; -.
DR   PhylomeDB; P22717; -.
DR   PRO; PR:P22717; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0043167; F:ion binding; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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   2: Evidence at transcript level;
KW   cGMP biosynthesis; Cytoplasm; GTP-binding; Heme; Iron; Lyase;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..682
FT                   /note="Guanylate cyclase soluble subunit beta-2"
FT                   /id="PRO_0000074120"
FT   DOMAIN          408..536
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          592..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
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"
SQ   SEQUENCE   682 AA;  76197 MW;  98C173C1A1CC7715 CRC64;
     MEAILKLFGE YFFKFCKMSG YDRMLRTLGG NLTEFIENLD ALHSYLALSY QEMNAPSFRV
     EEGADGAMLL HYYSDRHGLC HIVPGIIEAV AKDFFDTDVA MSILDMNEEV ERTGKKEHVV
     FLVVQKAHRQ IRGAKASRPQ GSEDSQADQE ALQGTLLRMK ERYLNIPVCP GEKSHSTAVR
     ASVLFGKGPL RDTFQPVYPE RLWVEEEVFC DAFPFHIVFD EALRVKQAGV NIQKYVPGIL
     TQKFALDEYF SIIHPQVTFN ISSICKFINS QFVLKTRKEM MPKARKSQPM LKLRGQMIWM
     ESLRCMIFMC SPNVRSLQEL EESKMHLSDI APHDTTRDLI LLNQQRLAEM ELSCQLEKKK
     EELRVLSNHL AIEKKKTETL LYAMLPEHVA NQLKEGRKVA AGEFETCTIL FSDVVTFTNI
     CAACEPIQIV NMLNSMYSKF DRLTSVHDVY KVETIGDAYM VVGGVPVPVE SHAQRVANFA
     LGMRISAKEV MNPVTGEPIQ IRVGIHTGPV LAGVVGDKMP RYCLFGDTVN TASRMESHGL
     PSKVHLSPTA HRALKNKGFE IVRRGEIEVK GKGKMTTYFL IQNLNATEDE IMGRPSAPAD
     GKEVCTPGNQ VRKSPAVPRN TDHQQQVYKG DPADASNEVT LAGSPVAGRN STDAVNNQPS
     PDETKTSVVA SGPVLSAFCV VL