GUC2C_CAVPO
ID GUC2C_CAVPO Reviewed; 1076 AA.
AC P70106;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RA Kruhoeffer M., Cetin Y., Kaempf U., Forssmann W.-G.;
RT "Sequence of guinea pig guanylin and guanylyl cyclase C (GC-C) cDNA:
RT expression and tissue distribution.";
RL Submitted (AUG-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-62 is required for interaction with VIP36
CC while glycosylation at Asn-348 and Asn-405 modulates ligand-mediated
CC GC-C activation. {ECO:0000250|UniProtKB:P25092}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; Z74734; CAA98989.1; -; mRNA.
DR RefSeq; NP_001166430.1; NM_001172959.2.
DR AlphaFoldDB; P70106; -.
DR SMR; P70106; -.
DR STRING; 10141.ENSCPOP00000018324; -.
DR GeneID; 100135536; -.
DR KEGG; cpoc:100135536; -.
DR CTD; 2984; -.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; P70106; -.
DR OrthoDB; 229634at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd07302; CHD; 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; 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..1076
FT /note="Guanylyl cyclase C"
FT /id="PRO_0000012375"
FT TOPO_DOM 24..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..1076
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 492..752
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 827..957
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1076 AA; 123120 MW; 9B53F16E05E80EB9 CRC64;
MKSPLLGLVV WSLLLQLLQP GLAFWNSQIS QNCHNGSYEI TVLMMNNYAF QESLESLKTA
VNKGLDIVKQ RLQEAALYVT VNATFIHSDG LIHKSGDCRS STCEGLDLLR EIARQKRMGC
ALMGPSCTYS TYQMYLDTEL NYPMISAGSF GLSCDHKETL TRMMSPARKL MYFLVDFWKA
SNLPFKSFSW NTSYVFKNGT ESEHCFWYIN ALEAGVSYFS QVLGFKEMLR GNEELQKILK
DPNRRSNVIV MCGTPQTMES LKIDWTATED TVIILVDLFN NYYLEENATA PDYMKNVLVL
TLPPGNSTIN TSLSKESLQE FSDFALAYLD GILLFGHMLK TFLRNGENTT AHKFAHAFRN
LTFEGSTGPV TLDDSGDIDN TMVLLYTSVD TKKFKPLLFY DTRINQTTPI DTHPTFIWKN
HRLPHDIPGL GPHILLIAVC TLAGVVVLIL LIALLVLRKY KKDNELRQKK WSHIPPEKIL
PLETNEANHV SLKIDDDKKR DTVQRLRQCK YDPKRAILKD LKYSDGNFSE KQKIELDKLL
PSDFYSLTKF YGTVKLDTRI FGVIEYCERG SLREVLNETI SYPDGTIMGW EFKISVLYDI
AKGMSYLHSS KIEVHGRLKS TNCVVDSRMV VKITDFGYNS ILPPKKDLWT APEHLRQAST
SQKGDVYSFG IIAQEIIMRR ETFYTLSCRD QKEKIFRVEH PDGLKPFRPD LFLETAEEKE
LEVFLLVKNC WEEDPEKRPD FKKIENTLAK IFGLFHDQKN ESYMDTLIRR LQLYSRNLEH
LVEERTQLYK AERDRADRLN FMLLPRPVVQ SLKEKGIVEP ELYEEVTVYF SDIVGFTTIC
KYSTPMEVVD MLNDLYKSFD QIVDHHDVHK VETIGDAYVV ASGLPTRNGN RHAIDISKMA
LDILSFIGTF ELEHLPGLPV WIRIGVHSGP CAAGVVGIKI PRYCLFGDTV NTASRMESTG
LPLRIHMSSS TIAILKRVQC QFLYEMRGET YLKGKGTETT YCLTGMKDQE YNLPTPPTVE
NQQRLQAEFS DMITNSLQKR QATGIKSRKP ARVASYKKGT LEYLQLNTTD QDSTYF
