GUC2C_PIG
ID GUC2C_PIG Reviewed; 1073 AA.
AC P55204; Q29050;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Guanylyl cyclase C;
DE Short=GC-C;
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:P25092};
DE AltName: Full=Heat-stable enterotoxin receptor;
DE Short=STA receptor;
DE AltName: Full=Intestinal guanylate cyclase;
DE Flags: Precursor;
GN Name=GUCY2C; Synonyms=GUC2C;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Small intestine;
RX PubMed=7968686; DOI=10.1111/j.1348-0421.1994.tb01819.x;
RA Wada A., Hirayama T., Kitao S., Fujisawa J., Hidaka Y., Shimonishi Y.;
RT "Pig intestinal membrane-bound receptor (guanylyl cyclase) for heat-stable
RT enterotoxin: cDNA cloning, functional expression, and characterization.";
RL Microbiol. Immunol. 38:535-541(1994).
RN [2]
RP SEQUENCE REVISION TO 238 AND 509.
RA Wada A.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanylyl cyclase that catalyzes synthesis of cyclic GMP
CC (cGMP) from GTP. {ECO:0000250|UniProtKB:P25092}.
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:P25092};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000250|UniProtKB:P25092};
CC -!- SUBUNIT: Homotrimer. Interacts via its C-terminal region with PDZK2.
CC Interacts with the lectin chaperone VIP36.
CC {ECO:0000250|UniProtKB:P25092}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25092};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25092}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P25092}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P25092}. Note=The
CC 145 kDa plasma membrane form of GUCY2C contains sialic acid and
CC galactose residues, while a differencially glycosylated 130 Kda form is
CC a high mannose form that is resident in the endoplasmic reticulum and
CC may serve as the precursor for the cell surface form.
CC {ECO:0000250|UniProtKB:P25092}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000305}.
CC -!- PTM: Glycosylation at Asn-79 is required for interaction with VIP36
CC while glycosylation at Asn-402 modulates ligand-mediated GC-C
CC activation. {ECO:0000250|UniProtKB:P25092}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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; D17513; BAA04465.1; -; mRNA.
DR RefSeq; NP_999270.1; NM_214105.1.
DR AlphaFoldDB; P55204; -.
DR SMR; P55204; -.
DR STRING; 9823.ENSSSCP00000024152; -.
DR iPTMnet; P55204; -.
DR PaxDb; P55204; -.
DR PeptideAtlas; P55204; -.
DR PRIDE; P55204; -.
DR Ensembl; ENSSSCT00000042247; ENSSSCP00000037539; ENSSSCG00000026724.
DR Ensembl; ENSSSCT00005026009; ENSSSCP00005015756; ENSSSCG00005016055.
DR Ensembl; ENSSSCT00025063019; ENSSSCP00025026816; ENSSSCG00025046365.
DR Ensembl; ENSSSCT00035061423; ENSSSCP00035024761; ENSSSCG00035046191.
DR Ensembl; ENSSSCT00040078365; ENSSSCP00040033792; ENSSSCG00040057669.
DR Ensembl; ENSSSCT00045035453; ENSSSCP00045024621; ENSSSCG00045020756.
DR Ensembl; ENSSSCT00050057385; ENSSSCP00050024516; ENSSSCG00050042236.
DR Ensembl; ENSSSCT00055027347; ENSSSCP00055021755; ENSSSCG00055013873.
DR Ensembl; ENSSSCT00065106523; ENSSSCP00065047383; ENSSSCG00065077037.
DR Ensembl; ENSSSCT00070044459; ENSSSCP00070037460; ENSSSCG00070022312.
DR GeneID; 397193; -.
DR KEGG; ssc:397193; -.
DR CTD; 2984; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000155955; -.
DR InParanoid; P55204; -.
DR OrthoDB; 229634at2759; -.
DR BRENDA; 4.6.1.2; 6170.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Chromosome 5.
DR Bgee; ENSSSCG00000026724; Expressed in ovary and 41 other tissues.
DR ExpressionAtlas; P55204; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR CDD; cd14044; PK_GC-C; 1.
DR Gene3D; 3.30.70.1230; -; 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 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; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; cGMP biosynthesis; Endoplasmic reticulum; Glycoprotein;
KW GTP-binding; Lyase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1073
FT /note="Guanylyl cyclase C"
FT /id="PRO_0000012377"
FT TOPO_DOM 24..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..1073
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 489..749
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 824..954
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1073 AA; 123220 MW; E6F4FC1327BA9F43 CRC64;
MKTPLLALAL WSLLLQLGLT FWPSSVSQNC HNGSYEISVL MMNNSAFPES LDNLKAVVNE
GVNIVRQRLL EAGLTVTVNA TFVYSEGVIY KSSDCRSSTC EGLDLLRTIS SEKRMGCVLL
GPSCTYSTFQ MYLDTDLNYP MISAGSFGLS CDYKETLTRL MSPARKLMYF LVDFWKVNNF
PFKPFSWNTA YVFKNSTESE DCFWYLNALE AGVSYFSQKL SFKEMLRGNE EFQNILMDQN
RKSNVIIMCG APETVHTLKG GRAVAEDTVI ILVDLFNDHY FMDNVTAPDY MKNVLVLTLP
PENSVSNSSF SKDLSLVKND FTLAYMNGVL LFGHMLKIFL EKREDVTTSK FAHAFRNITF
EGHMGPVTLD NCGDIDNTMF LLYTSVDTSK YKVLLTYDTR KNYTNPVDKS PTFIWKNHKL
PNDIPGRGPQ ILMIAVFTLT GTIVLLLLIA LLVLRKYKRE YALRQKKWSH IPPENIFPLE
SNETNHVSLK IDDDRRRDTI QRLRQCKYDK KRVILKDLKH NDGNFTEKQK IELNKLLQID
YYNLTKFYGT VKLDSMIFGV IEYCERGSLR EVLNDTISYP DGTFMDWEFK ISVLYDIAKG
MSYLHSSKTE VHGRLKSTNC VVDSRMVVKI TDFGCNSILA PKKDLWTAPE HLRRASVSQK
GDVYSYGIIA QEIILRRETF YTLSCRDQKE KIFRVENSNG VKPFRPDLFL ETAEEKELEV
YLLVKNCWEE DPEKRPDFKK IENTLAKIFG LFHDQKNESY MDTLIRRLQL YSRNLEHLVE
ERTQLYKAER DRADRLNFML LPRLVVKSLK EKGIVEPELY EEVTIYFSDI VGFTTICKYS
TPMEVVDMLN DIYKSFDHIL DHHDVYKVET IGDAYMVASG LPKRNGNRHA IDIAKMALDI
LSFMGTFELE HLPGLPIWIR IGIHSGPCAA GVVGIKMPRY CLFGDTVNTA SRMESTGLPL
RIHVSGSTIA ILKRTECQFL YEVRGETYLK GRGTETTYWL TGVKDQEYNL PTPPTAENQQ
RLQAEFVDMI ASSLQKRQAS GIKNRKPTRV ASYKKGTLEY LQLNTTDNES THF
