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Database: UniProt
Entry: I3LIP7_PIG
LinkDB: I3LIP7_PIG
Original site: I3LIP7_PIG 
ID   I3LIP7_PIG              Unreviewed;       767 AA.
AC   I3LIP7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 3.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   Name=LOC100625149 {ECO:0000313|Ensembl:ENSSSCP00000023953.3};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000023953.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000023953.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000023953.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000023953.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; I3LIP7; -.
DR   STRING; 9823.ENSSSCP00000023953; -.
DR   Ensembl; ENSSSCT00000026007.4; ENSSSCP00000023953.3; ENSSSCG00000024765.4.
DR   GeneTree; ENSGT00940000162114; -.
DR   HOGENOM; CLU_011614_4_0_1; -.
DR   InParanoid; I3LIP7; -.
DR   OrthoDB; 2898719at2759; -.
DR   TreeFam; TF351403; -.
DR   Reactome; R-SSC-445355; Smooth Muscle Contraction.
DR   Proteomes; UP000008227; Chromosome 11.
DR   Bgee; ENSSSCG00000024765; Expressed in testis and 4 other cell types or tissues.
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: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; 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; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   PANTHER; PTHR45655:SF17; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07700; HNOB; 1.
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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          493..621
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          714..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          427..461
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        721..749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  86877 MW;  67DA91B30002B917 CRC64;
     MSTGNSSETG NRESSFPQED AIARFLKAST QYGFINTCLQ SLVIEKFGEE TWEKLKARVD
     VQDAFMTYTV YDDVITIKLI QEACSVLGVS MEAILKLFGE YFFKFCKMSG YDRMLRTLGG
     NLTEFIENLD ALHSYLALSY QEMNAPSFRV ERAADEKMLL HYYSDRSGLC HIVPGIIEAV
     AKDFFDVDVT LEILDVHQEE ERTAKKEHVV FLIVQKSHRQ MRRAKPKDSQ RDQEVQGLLS
     FLRMKEKYLS VSVCPVKKSR WEVVRRIVMF GKRHLRNTFE PIYPERLWIE ERTFCNAFPF
     HLVFDASLRV KQAGVNIQKY IPGLRTPKIR LDTYFSIVHP PVAFDIFSIC QFINSPFVLK
     ARGERLPEAG RSRPPLKLRG QMIWMESTRC MVYLCSPKLR SLRELEERQM HLSDIAPHDT
     TRDLILLNQQ RLAEMELSNQ LERKKEELRV LSKHLAIEKK KTEALLYAML PKHVANQLKE
     GRKVAAGEFK TCTILFSDVV TFTTICAACE PIQIVNMLNS MYSKFDRLTS VHDVYKVETI
     GDAYMVVGGV PVPIGSHAQR VANFALGMRL SAKEVMNPVT GEPIQIRVGI HTGPVLAGVV
     GDKMPRYCLF GDTVNTASRM ESHGLPNKVH LSPTAYRALE NQGFEITERG EIEVKGKGKM
     TTYFLIRNVN ASEDELMGRP RTPLHPEEAS APGNQDRTLA VMRYADSCQR LPEGDAARAS
     DQSTPRESPA ASGQDSVEAA NGQRSSDETK TQRLPGEPLP SGFCALL
//
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