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Database: UniProt
Entry: A0A455BG10_PHYMC
LinkDB: A0A455BG10_PHYMC
Original site: A0A455BG10_PHYMC 
ID   A0A455BG10_PHYMC        Unreviewed;       990 AA.
AC   A0A455BG10;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE            EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
GN   Name=GUCY2C {ECO:0000313|RefSeq:XP_028346848.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028346848.1};
RN   [1] {ECO:0000313|RefSeq:XP_028346848.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028346848.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036920};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC         Evidence={ECO:0000256|ARBA:ARBA00036920};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   RefSeq; XP_028346848.1; XM_028491047.2.
DR   AlphaFoldDB; A0A455BG10; -.
DR   Proteomes; UP000248484; Chromosome 6.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd06369; PBP1_GC_C_enterotoxin_receptor; 1.
DR   CDD; cd14044; PK_GC-C; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR042822; GC-C_PK.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF347; GUANYLYL CYCLASE C; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW   ECO:0000256|RuleBase:RU003431};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..990
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019789746"
FT   TRANSMEM        431..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          489..749
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          824..954
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   990 AA;  113754 MW;  8F6373A9E69E664B CRC64;
     MKTPLLALAL WSLLLRPGLL FWTSHMSQNC HNGSYKISVL MMNNSAFPES RVNLEEVVNA
     GLEIVRQRLL QAGLNVTVNA TFIYSEGMIY KSSDCRSSTC EGLELLRMIS RDKQMGCVLM
     GPTCTYSTFQ IYLDTDLNYP MISAGSFGLS CDYKETLTRL MSPARKLMYF LVDFWKVNYF
     PFKTSSWNTA YVFKNGTESE DCFWYLNALE AGVSYFSQKL SFKEMLRGDN EFQRILLDQN
     RKSNVIVMCG TPNTINVLKG DRAVAEDTVI ILVDLFNEYY FMDNVTAPDY MKNVLVLTLP
     PGNSVSNSSF AKNLSLAKND FAAAYFDGVL LFGHMLKIFL ENGEEVTTPK FAHAFRNVTF
     EGHVGPVTLD DCGDIDNTMF LLYTSVDTNK YKVLLTYDTR INQTNPVDKS PTFIWKNHKL
     PNDIPGRGPQ ILMVAVFTLT GAVVLVLLIA LLVLRKYKGE YALRQKKWSH IPPENIFPLE
     SNETNHVSLK IDDDKRRDTI QRLRQCKYDK KRVILKDLKH NDGNFTEKQK IELNKLLQID
     YYNLTKFYGT VKLDSMIFGV IEYCERGSLR EVLNDTISYP DGTFMDWEFK ISVLYDIAKG
     MSYLHSSKTE VHGRLKSTNC VVDSRMVVKI TDFGCNSILP PRKDLWTAPE HLRQANISQK
     GDVYSYGIIA QEIILRRETF YTLSCRDQKE KIFRVENSNG VKPFRPDLFL ETAEEKELEV
     YLLVKNCWEE DPEKRPDFKK IENTLAKIFG LFHDQKNETY MDTLIRRLQL YSRNLEHLVE
     ERTQLYKAER DRADRLNFML LPRLVVKSLK EKGIVEPELY EEVTIYFSDI VGFTTICKYS
     TPMEVVDMLN DIYKNFDHIL DHHDVYKVET IGDAYMVASG LPKRNGNRHA IDIAKMALDI
     LSFMGTFELE HLPGLPIWIR IGIHSGPCAA GVVGIKMPRY CLFGDTVNTA SRMESTGLPL
     RIHVSGSTIS ILKRTECQFL YEVRGETYLK
//
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