GUC2E_RAT
ID GUC2E_RAT Reviewed; 1108 AA.
AC P51840;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Retinal guanylyl cyclase 1;
DE Short=RETGC-1;
DE EC=4.6.1.2 {ECO:0000269|PubMed:7831337};
DE AltName: Full=Guanylate cyclase 2E;
DE AltName: Full=Guanylyl cyclase GC-E;
DE Flags: Precursor;
GN Name=Gucy2e; Synonyms=Guc2e, Gucy2d {ECO:0000312|RGD:620438};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Eye;
RX PubMed=7831337; DOI=10.1073/pnas.92.2.602;
RA Yang R.-B., Foster D.C., Garbers D.L., Fuelle H.-J.;
RT "Two membrane forms of guanylyl cyclase found in the eye.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:602-606(1995).
RN [2]
RP SUBUNIT, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9153227; DOI=10.1074/jbc.272.21.13738;
RA Yang R.B., Garbers D.L.;
RT "Two eye guanylyl cyclases are expressed in the same photoreceptor cells
RT and form homomers in preference to heteromers.";
RL J. Biol. Chem. 272:13738-13742(1997).
RN [3]
RP PROTEIN SEQUENCE OF 203-209, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
CC -!- FUNCTION: Catalyzes the synthesis of cyclic GMP (cGMP) in rods and
CC cones of photoreceptors. Plays an essential role in phototransduction,
CC by mediating cGMP replenishment. May also participate in the
CC trafficking of membrane-asociated proteins to the photoreceptor outer
CC segment membrane. {ECO:0000250|UniProtKB:P52785}.
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:0000269|PubMed:7831337};
CC -!- ACTIVITY REGULATION: Activated by GUCA1A when free calcium ions
CC concentration is low, and inhibited by GUCA1A when free calcium ions
CC concentration is high (By similarity). Negatively regulated by RD3;
CC inhibits the basal and GUCA1A-stimulated guanylate cyclase activity (By
CC similarity). {ECO:0000250|UniProtKB:P52785,
CC ECO:0000250|UniProtKB:Q02846}.
CC -!- SUBUNIT: Homodimer; requires homodimerization for guanylyl cyclase
CC activity (PubMed:9153227). Interacts (via C-terminus) with RD3 (via C-
CC terminus); promotes the exit of GUCY2E from the endoplasmic reticulum
CC and its trafficking to the photoreceptor outer segments (By
CC similarity). Interaction with RD3 negatively regulates GUCY2E guanylate
CC cyclase activity (By similarity). {ECO:0000250|UniProtKB:Q02846,
CC ECO:0000269|PubMed:9153227}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7831337}; Single-
CC pass type I membrane protein. Photoreceptor outer segment membrane
CC {ECO:0000269|PubMed:7831337, ECO:0000269|PubMed:9153227}; Single-pass
CC type I membrane protein. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in retina and enriched in photoreceptor
CC outer segments. {ECO:0000269|PubMed:9153227}.
CC -!- PTM: There are 9 conserved cysteine residues in sensory guanylate
CC cyclases, 6 in the extracellular domain, which may be involved in
CC intra- or interchain disulfide bonds.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; L36029; AAA65510.1; -; mRNA.
DR PIR; A55915; A55915.
DR RefSeq; NP_077356.1; NM_024380.1.
DR AlphaFoldDB; P51840; -.
DR SMR; P51840; -.
DR STRING; 10116.ENSRNOP00000010790; -.
DR GlyGen; P51840; 1 site.
DR iPTMnet; P51840; -.
DR PhosphoSitePlus; P51840; -.
DR PaxDb; P51840; -.
DR PRIDE; P51840; -.
DR Ensembl; ENSRNOT00000010790; ENSRNOP00000010790; ENSRNOG00000007931.
DR GeneID; 79222; -.
DR KEGG; rno:79222; -.
DR UCSC; RGD:620438; rat.
DR CTD; 3000; -.
DR RGD; 620438; Gucy2e.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; P51840; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; P51840; -.
DR TreeFam; TF106338; -.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:P51840; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISO:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; IDA:RGD.
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 GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; IPR011645; HNOB_dom_associated.
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; PF07701; HNOBA; 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 1: Evidence at protein level;
KW Cell projection; cGMP biosynthesis; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; GTP-binding; Lyase;
KW Membrane; Nucleotide-binding; Reference proteome; Sensory transduction;
KW Signal; Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..54
FT /evidence="ECO:0000250|UniProtKB:P55203"
FT CHAIN 55..1108
FT /note="Retinal guanylyl cyclase 1"
FT /id="PRO_0000012384"
FT TOPO_DOM 55..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..1108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 520..811
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 883..1013
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 520..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..136
FT /evidence="ECO:0000250"
FT DISULFID 452
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 460
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1108 AA; 120801 MW; 4FA1BE9325A2A979 CRC64;
MSAWLLPAGG FPGAGFCIPA WQSRSSLSRV LRWPGPGLPG LLLLLLLPSP SAFSAVFKVG
VLGPWACDPI FARARPDLAA RLATDRLNRD LALDGGPWFE VTLLPEPCLT PGSLGAVSSA
LTRVSGLVGP VNPAACRPAE LLAQEAGVAL VPWGCPGTRA AGTTAPAVTP AADALYVLLK
AFRWARVALI TAPQDLWVEA GRALSTALRA RGLPVALVTS MVPSDLSGAR EALRRIRDGP
RVRVVIMVMH SVLLGGEEQR YLLEAAEELG LTDGSLVFLP FDTLHYALSP GPEALAAFVN
SSKLRRAHDA VLTLTRRCPP GGSVQDSLRR AQEHQELPLD LDLKQVSPLF GTIYDAVFLL
AGGVTRARAA VGGGWVSGAS VARQMREAQV FGFCGILGRT EEPSFVLLDT DAAGERLFTT
HLLDPVLGSL RSAGTPVHFP RGAPAPGPDP SCWFDPDVIC NGGVEPGLVF VGFLLVIVVG
LTGAFLAHYL RHRLLHMQMV SGPNKIILTL EDVTFLHPQG GSSRKVAQGS RSSLATRSTS
DIRSVPSQPQ ESTNIGLYEG DWVWLKKFPG EHHMAIRPAT KMAFSKLREL RHENVALYLG
LFLAGTADSP ATPGEGILAV VSEHCARGSL HDLLAQRDIK LDWMFKSSLL LDLIKGMRYL
HHRGVAHGRL KSRNCVVDGR FVLKVTDHGH GRLLEAQRVL PEPPSAEDQL WTAPELLRDP
ALERRGTLAG DVFSLGIIMQ EVVCRSTPYA MLELTPEEVI QRVRSPPPLC RPLVSMDQAP
MECIQLMAQC WAEHPELRPS MDLTFDLFKG INKGRKTNII DSMLRMLEQY SSNLEDLIRE
RTEELEQEKQ KTDRLLTQML PPSVAEALKM GTSVEPEYFE EVTLYFSDIV GFTTISAMSE
PIEVVDLLND LYTLFDAIIG SHDVYKVETI GDAYMVASGL PQRNGQRHAA EIANMSLDIL
SAVGSFRMRH MPEVPVRIRI GLHSGPCVAG VVGLTMPRYC LFGDTVNTAS RMESTGLPYR
IHVNMSTVRI LRALDQGFQM ECRGRTELKG KGVEDTYWLV GRVGFNKPIP KPPDLQPGAS
NHGISLQEIP PERRKKLEKA RPGQFTGK
