GUC2F_RAT
ID GUC2F_RAT Reviewed; 1108 AA.
AC P51842;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Retinal guanylyl cyclase 2;
DE Short=RETGC-2;
DE EC=4.6.1.2 {ECO:0000269|PubMed:7831337};
DE AltName: Full=Guanylate cyclase 2F, retinal;
DE AltName: Full=Guanylate cyclase F;
DE Short=GC-F;
DE AltName: Full=Rod outer segment membrane guanylate cyclase 2;
DE Short=ROS-GC2;
DE Flags: Precursor;
GN Name=Gucy2f; Synonyms=Guc2f;
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], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND FUNCTION.
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).
CC -!- FUNCTION: Responsible for the synthesis of cyclic GMP (cGMP) in rods
CC and cones of photoreceptors. Plays an essential role in
CC phototransduction, by mediating cGMP replenishment (PubMed:7831337).
CC May also participate in the trafficking of membrane-asociated proteins
CC to the photoreceptor outer segment membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q5SDA5, ECO:0000269|PubMed:7831337}.
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 GUCA1B when free calcium ions
CC concentration is low, and inhibited by GUCA1B when free calcium ions
CC concentration is high (By similarity). Inhibited by RD3 (By
CC similarity). {ECO:0000250|UniProtKB:O02740,
CC ECO:0000250|UniProtKB:P51841}.
CC -!- SUBUNIT: Homodimer (PubMed:9153227). Interacts with RD3; promotes the
CC exit of GUCY2F from the endoplasmic reticulum and its trafficking to
CC the photoreceptor outer segments (By similarity).
CC {ECO:0000250|UniProtKB:Q5SDA5, 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:0000250|UniProtKB:O02740}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed only in the eye.
CC {ECO:0000269|PubMed:7831337}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
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; L36030; AAA65511.1; -; mRNA.
DR PIR; B55915; B55915.
DR RefSeq; NP_446283.1; NM_053831.1.
DR AlphaFoldDB; P51842; -.
DR SMR; P51842; -.
DR STRING; 10116.ENSRNOP00000049500; -.
DR PhosphoSitePlus; P51842; -.
DR PaxDb; P51842; -.
DR PRIDE; P51842; -.
DR Ensembl; ENSRNOT00000046804; ENSRNOP00000049500; ENSRNOG00000019086.
DR GeneID; 116556; -.
DR KEGG; rno:116556; -.
DR CTD; 2986; -.
DR RGD; 620439; Gucy2f.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000162146; -.
DR HOGENOM; CLU_001072_1_0_1; -.
DR InParanoid; P51842; -.
DR OMA; ICRGGID; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; P51842; -.
DR TreeFam; TF106338; -.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:P51842; -.
DR Proteomes; UP000002494; Chromosome X.
DR Genevisible; P51842; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0120200; C:rod photoreceptor outer segment; ISS:UniProtKB.
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: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; IBA:GO_Central.
DR GO; GO:0019934; P:cGMP-mediated signaling; IDA:RGD.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO: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 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; IPR033484; GUCY2F.
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 PANTHER; PTHR11920:SF349; PTHR11920:SF349; 1.
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; Disulfide bond; GTP-binding; Lyase;
KW Membrane; Nucleotide-binding; Reference proteome; Sensory transduction;
KW Signal; Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..1108
FT /note="Retinal guanylyl cyclase 2"
FT /id="PRO_0000012387"
FT TOPO_DOM 51..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 532..812
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 884..1014
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DISULFID 104..132
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; 124411 MW; 2A9147AF2202E4E3 CRC64;
MFLGPWPFSR LLSWFAISSR LSGQHGLTSS KFLRYLCLLA LLPLIWWGQA LPYKIGVIGP
WTCDPFFSKA LPEVAAALAI ERISRDMSFD RSYSFEYVIL NEDCQTSKAL TSFISHQQMA
SGFVGPANPG YCEAASLLGN SWDKGIFSWA CVNHELDNKH SYPTFSRTLP SPIRVLVTVM
KYFQWAHAGV ISSDEDIWVH TANQVSSALR SHGLPVGVVL TSGQDSRSIQ KALQQIRQAD
RIRIIIMCMH SALIGGETQT HFLELAHDLK MTDGTYVFVP YDVLLYSLPY KHSPYQVLRN
NQKLREAYDA VLTITVESHE KTFYEAFTEA AAGGEIPEKL DSHQVSPLFG TIYNSIYFIA
QAMSNALKEN GQASAASLTR HSRNMQFYGF NQLIRTDSNG NGISEYVILD TNGKEWELRG
TYTVDMETEL LRFRGTPIHF PGGRPTSADA KCWFAQGKIC QGGIDPALAM MVCFALLLAL
LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQIISEVQS
GRSPRLSFSS GSLTPATYEN SNIAIYQGDW VWLKKFPPGD FGDIKSIKSS ASDVFEMMKD
LRHENVNPLL GFFYDSGMFA IVSEFCSRRS LEDILTQDDV KLDWMFKSSL LLDLIKGMKY
LHHREFIHGR LKSRNCVVDG RFVLKVTDYG FNNILEMLRL SEEEPSEEEL LWTAPELLRA
PGGIRLGSFA GDVYSFAIIM QEVMVRGAPF CMMDLSAKEV IDRLKMPPPV YRPVVSPEFA
PPECLQLMKQ CWAEAAEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR
ERTEELEIEK QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI
LSSVGTFKMR HMPEVPVRIR IGLHTGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
RIHVSLSTVT ILRTLSEGYE VELRGRTELK GKGTEETFWL VGKKGFTKPL PVPPPVGKDG
QVGHGLQPAE IAAFQRRKAE RQLVRNKP
