GUC2F_BOVIN
ID GUC2F_BOVIN Reviewed; 1103 AA.
AC O02740;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Retinal guanylyl cyclase 2;
DE Short=RETGC-2;
DE EC=4.6.1.2 {ECO:0000269|PubMed:9175772, ECO:0000269|PubMed:9571173};
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 {ECO:0000303|PubMed:9175772, ECO:0000303|PubMed:9571173};
DE Short=ROS-GC2 {ECO:0000303|PubMed:9175772, ECO:0000303|PubMed:9571173};
DE Flags: Precursor;
GN Name=GUCY2F; Synonyms=GUC2F;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=9175772; DOI=10.1006/bbrc.1997.6579;
RA Goraczniak R., Duda T., Sharma R.K.;
RT "Structural and functional characterization of a second subfamily member of
RT the calcium-modulated bovine rod outer segment membrane guanylate cyclase,
RT ROS-GC2.";
RL Biochem. Biophys. Res. Commun. 234:666-670(1997).
RN [2]
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=9571173; DOI=10.1006/bbrc.1998.8455;
RA Goraczniak R.M., Duda T., Sharma R.K.;
RT "Calcium modulated signaling site in type 2 rod outer segment membrane
RT guanylate cyclase (ROS-GC2).";
RL Biochem. Biophys. Res. Commun. 245:447-453(1998).
CC -!- FUNCTION: Responsible for the synthesis of cyclic GMP (cGMP) in rods
CC and cones of photoreceptors (PubMed:9571173, PubMed:9175772). Plays an
CC essential role in phototransduction, by mediating cGMP replenishment
CC (PubMed:9571173, PubMed:9175772). May also participate in the
CC trafficking of membrane-asociated proteins to the photoreceptor outer
CC segment membrane (By similarity). {ECO:0000250|UniProtKB:Q5SDA5,
CC ECO:0000269|PubMed:9175772, ECO:0000269|PubMed:9571173}.
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:9175772, ECO:0000269|PubMed:9571173};
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 (PubMed:9571173). Inhibited by RD3 (By
CC similarity). {ECO:0000250|UniProtKB:P51841,
CC ECO:0000269|PubMed:9571173}.
CC -!- SUBUNIT: Homodimer (By similarity). 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:P51842, ECO:0000250|UniProtKB:Q5SDA5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9175772}; Single-
CC pass type I membrane protein {ECO:0000255}. Photoreceptor outer segment
CC membrane {ECO:0000250|UniProtKB:Q5SDA5}; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in retina.
CC {ECO:0000269|PubMed:9175772}.
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; U95958; AAB53864.1; -; mRNA.
DR PIR; JC5581; JC5581.
DR RefSeq; NP_776974.1; NM_174549.2.
DR AlphaFoldDB; O02740; -.
DR SMR; O02740; -.
DR STRING; 9913.ENSBTAP00000036727; -.
DR PaxDb; O02740; -.
DR PRIDE; O02740; -.
DR GeneID; 282246; -.
DR KEGG; bta:282246; -.
DR CTD; 2986; -.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; O02740; -.
DR OrthoDB; 229634at2759; -.
DR BRENDA; 4.6.1.2; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB.
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 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; 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..46
FT /evidence="ECO:0000250"
FT CHAIN 47..1103
FT /note="Retinal guanylyl cyclase 2"
FT /id="PRO_0000012385"
FT TOPO_DOM 47..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..1103
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:0000305"
FT DISULFID 460
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1103 AA; 124262 MW; EB731E1D8C642AA4 CRC64;
MFLAPWPFSH LMLWFVTLGR QRGQHGLASF KLLWCLWLLV LMSLPLQVWA PPYKIGVVGP
WTCDPLFSKA LPEIAAQLAT ERINKDPALD LGHSLEYVIF NEDCQASRAL SSFISHHQMA
SGFIGPANPG YCEAASLLGN SWDKGIFSWA CVNYELDSKN SHPTFSRTLP SPIRVLLTVM
KYFQWAHAGV ISSDEDIWVH TAYRVASALR SRGLPVGVVL TTGQDSQSIQ KALQQIRQAD
RIRIIIMCMH STLIGGETQT HLLEWAHDLQ MTDGTYVFVP YDTLLYSLPY KHTPYKVLRN
NPKLREAYDA VLTITVESQE KTFYQAFEEA AARGEIPEKL ESDQVSPLFG TIYNSIYFIA
QAMNNAMKEN GWASAASLVQ HSRNVQFYGF NQLIRTDANG NGISEYVILD TNWKEWELHS
TYTVDMETEL LRFGETPIHF PGGRPPRADA QCWFADGRIC QGGINPTFAL MVCLALLIAL
LSINGFAYFI RHRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSHASV SFQITSEVQS
GRSPRLSFSS GSLTPATCEN SNIAIYEGDW VWLKKFPSGN FGDIKSVESS ASDIFEMMKD
LRHENINPLV GFFYDSGVFA IVTEFCSRRS LEDILMNQDV KLDWMFKSSL LLDLIKGMKY
LHHREFAHGR LKSRNCVVDG RFVLKVTDYG FNDILETLRL SQEEPSAEEL LWTAPELLRA
PRGSRLRSFA GDVYSFAIIM QEVMVRGTPF CMMDLPAKEI IERIKKPPPV YRPVVPPEHA
PPECLQLMKQ CWAEAAEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIQ
ERTEELEIEK QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGMRHA AEIANMSLDI
LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
RIHVSHSTVT ILRTLGEGYE VELRGRTELK GKGTEETFWL VGKKGFTKPL PVPPPVGKDG
QVGHGLQSVE IAAFQRRKQK SSW
