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Database: UniProt
Entry: GUC2F_BOVIN
LinkDB: GUC2F_BOVIN
Original site: 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   08-NOV-2023, entry version 154.
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; 9913-ENSBTAP00000036727; -.
DR   GeneID; 282246; -.
DR   KEGG; bta:282246; -.
DR   CTD; 2986; -.
DR   eggNOG; KOG1023; Eukaryota.
DR   InParanoid; O02740; -.
DR   BRENDA; 4.6.1.2; 908.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0120200; C:rod photoreceptor outer segment; ISS:UniProtKB.
DR   GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
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:0001653; F:peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd06371; PBP1_sensory_GC_DEF-like; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF349; RETINAL GUANYLYL CYCLASE 2; 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; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
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