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Protein

Heat-stable enterotoxin receptor

Gene

Gucy2c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptide guanylin (By similarity).By similarity

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. guanylate cyclase activity Source: MGI
  4. protein kinase activity Source: InterPro
  5. toxic substance binding Source: Ensembl

GO - Biological processi

  1. cGMP biosynthetic process Source: MGI
  2. intracellular signal transduction Source: InterPro
  3. regulation of cell proliferation Source: MGI
  4. response to toxic substance Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Receptor

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat-stable enterotoxin receptor (EC:4.6.1.2)
Short name:
STA receptor
Alternative name(s):
Guanylyl cyclase C
Short name:
GC-C
Intestinal guanylate cyclase
Gene namesi
Name:Gucy2c
Synonyms:Guc2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:106903. Gucy2c.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein
Note: The 145 kDa plasma membrane form of GC-C contains sialic acid and galactose residues, while a differencially glycosylated 130 Kda form is a high mannose form that is resident in the endoplasmic reticulum and may serve as the precursor for the cell surface form.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 433414ExtracellularSequence AnalysisAdd
BLAST
Transmembranei434 – 45421HelicalSequence AnalysisAdd
BLAST
Topological domaini455 – 1072618CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 10721053Heat-stable enterotoxin receptorPRO_0000280396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ3UWA6.
PRIDEiQ3UWA6.

PTM databases

PhosphoSiteiQ3UWA6.

Expressioni

Gene expression databases

BgeeiQ3UWA6.
CleanExiMM_GUCY2C.
GenevestigatoriQ3UWA6.

Interactioni

Subunit structurei

Homotrimer. Interacts via its C-terminal region with PDZK2. Interacts with the lectin chaperone VIP36 (By similarity).By similarity

Protein-protein interaction databases

BioGridi200125. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ3UWA6.
SMRiQ3UWA6. Positions 119-374, 540-748, 813-988.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini489 – 748260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini823 – 953131Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000112833.
HOVERGENiHBG106967.
InParanoidiQ3UWA6.
KOiK12320.
OMAiAYHDAVL.
OrthoDBiEOG72VH58.
PhylomeDBiQ3UWA6.
TreeFamiTF106338.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3UWA6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSLLGLAVR LLLFQPALMV FWASQVRQNC RNGSYEISVL MMDNSAYKEP
60 70 80 90 100
MQNLREAVEE GLDIVRKRLR EADLNVTVNA TFIYSDGLIH KSGDCRSSTC
110 120 130 140 150
EGLDLLREIT RDHKMGCALM GPSCTYSTFQ MYLDTELNYP MISAGSYGLS
160 170 180 190 200
CDYKETLTRI LPPARKLMYF LVDFWKVNNA SFKPFSWNSS YVYKNGSEPE
210 220 230 240 250
DCFWYLNALE AGVSYFSEVL NFKDVLRRSE QFQEILTGHN RKSNVIVMCG
260 270 280 290 300
TPESFYDVKG DLQVAEDTVV ILVDLFSNHY FEENTTAPEY MDNVLVLTLP
310 320 330 340 350
SEQSTSNTSV AERFSSGRSD FSLAYLEGTL LFGHMLQTFL ENGENVTGPK
360 370 380 390 400
FARAFRNLTF QGFAGPVTLD DSGDIDNIMS LLYVSLDTRK YKVLMKYDTH
410 420 430 440 450
KNKTIPVAEN PNFIWKNHKL PNDVPGLGPQ ILMIAVFTLT GILVVLLLIA
460 470 480 490 500
LLVLRKYRRD HALRQKKWSH IPSENIFPLE TNETNHISLK IDDDRRRDTI
510 520 530 540 550
QRVRQCKYDK KKVILKDLKH SDGNFSEKQK IDLNKLLQSD YYNLTKFYGT
560 570 580 590 600
VKLDTRIFGV VEYCERGSLR EVLNDTISYP DGTFMDWEFK ISVLNDIAKG
610 620 630 640 650
MSYLHSSKIE VHGRLKSTNC VVDSRMVVKI TDFGCNSILP PKKDLWTAPE
660 670 680 690 700
HLRQATISQK GDVYSFAIIA QEIILRKETF YTLSCRDHNE KIFRVENSYG
710 720 730 740 750
KPFRPDLFLE TADEKELEVY LLVKSCWEED PEKRPDFKKI ESTLAKIFGL
760 770 780 790 800
FHDQKNESYM DTLIRRLQLY SRNLEHLVEE RTQLYKAERD RADHLNFMLL
810 820 830 840 850
PRLVVKSLKE KGIVEPELYE EVTIYFSDIV GFTTICKYST PMEVVDMLND
860 870 880 890 900
IYKSFDQIVD HHDVYKVETI GDAYVVASGL PMRNGNRHAV DISKMALDIL
910 920 930 940 950
SFIGTFELEH LPGLPVWIRI GVHSGPCAAG VVGIKMPRYC LFGDTVNTAS
960 970 980 990 1000
RMESTGLPLR IHMSSSTITI LKRTDCQFLY EVRGETYLKG RGTETTYWLT
1010 1020 1030 1040 1050
GMKDQEYNLP SPPTVENQQR LQTEFSDMIV SALQKRQASG KKSRRPTRVA
1060 1070
SYKKGFLEYM QLNNSDHDST YF
Length:1,072
Mass (Da):123,232
Last modified:October 11, 2005 - v1
Checksum:i7129508166E7790A
GO
Isoform 2 (identifier: Q3UWA6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     512-535: Missing.

Note: No experimental confirmation available.

Show »
Length:1,048
Mass (Da):120,452
Checksum:i3F3B0D2056C5B79A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti381 – 3811L → F in AAH34064. (PubMed:15489334)Curated
Sequence conflicti969 – 9691T → A in AAH34064. (PubMed:15489334)Curated
Sequence conflicti969 – 9691T → A in AAH99968. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei512 – 53524Missing in isoform 2. 1 PublicationVSP_023652Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK136496 mRNA. Translation: BAE23010.1.
BC034064 mRNA. Translation: AAH34064.1.
BC099968 mRNA. Translation: AAH99968.1.
CCDSiCCDS20653.1. [Q3UWA6-2]
CCDS51941.1. [Q3UWA6-1]
RefSeqiNP_001120790.1. NM_001127318.1. [Q3UWA6-1]
NP_659504.2. NM_145067.3. [Q3UWA6-2]
UniGeneiMm.222729.

Genome annotation databases

EnsembliENSMUST00000032338; ENSMUSP00000032338; ENSMUSG00000042638. [Q3UWA6-1]
ENSMUST00000078095; ENSMUSP00000077236; ENSMUSG00000042638. [Q3UWA6-2]
GeneIDi14917.
KEGGimmu:14917.
UCSCiuc009emb.2. mouse. [Q3UWA6-2]
uc009emc.2. mouse. [Q3UWA6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK136496 mRNA. Translation: BAE23010.1.
BC034064 mRNA. Translation: AAH34064.1.
BC099968 mRNA. Translation: AAH99968.1.
CCDSiCCDS20653.1. [Q3UWA6-2]
CCDS51941.1. [Q3UWA6-1]
RefSeqiNP_001120790.1. NM_001127318.1. [Q3UWA6-1]
NP_659504.2. NM_145067.3. [Q3UWA6-2]
UniGeneiMm.222729.

3D structure databases

ProteinModelPortaliQ3UWA6.
SMRiQ3UWA6. Positions 119-374, 540-748, 813-988.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200125. 2 interactions.

PTM databases

PhosphoSiteiQ3UWA6.

Proteomic databases

MaxQBiQ3UWA6.
PRIDEiQ3UWA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032338; ENSMUSP00000032338; ENSMUSG00000042638. [Q3UWA6-1]
ENSMUST00000078095; ENSMUSP00000077236; ENSMUSG00000042638. [Q3UWA6-2]
GeneIDi14917.
KEGGimmu:14917.
UCSCiuc009emb.2. mouse. [Q3UWA6-2]
uc009emc.2. mouse. [Q3UWA6-1]

Organism-specific databases

CTDi2984.
MGIiMGI:106903. Gucy2c.

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000112833.
HOVERGENiHBG106967.
InParanoidiQ3UWA6.
KOiK12320.
OMAiAYHDAVL.
OrthoDBiEOG72VH58.
PhylomeDBiQ3UWA6.
TreeFamiTF106338.

Miscellaneous databases

NextBioi287217.
PROiQ3UWA6.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UWA6.
CleanExiMM_GUCY2C.
GenevestigatoriQ3UWA6.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cecum.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-1072 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon and Pancreas.

Entry informationi

Entry nameiGUC2C_MOUSE
AccessioniPrimary (citable) accession number: Q3UWA6
Secondary accession number(s): Q499D2, Q8JZQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2005
Last modified: January 7, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.