GUC2F_MOUSE
ID GUC2F_MOUSE Reviewed; 1108 AA.
AC Q5SDA5; Q8BLL8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Retinal guanylyl cyclase 2 {ECO:0000303|PubMed:17255100};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:O02740};
DE AltName: Full=Guanylate cyclase 2F;
DE Flags: Precursor;
GN Name=Gucy2f {ECO:0000312|MGI:MGI:105119};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15718098; DOI=10.1016/j.ygeno.2004.11.001;
RA Shearstone J.R., Wang Y.E., Clement A., Allaire N.E., Yang C., Worley D.S.,
RA Carulli J.P., Perrin S.;
RT "Application of functional genomic technologies in a mouse model of retinal
RT degeneration.";
RL Genomics 85:309-321(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-846.
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17255100; DOI=10.1074/jbc.m610369200;
RA Baehr W., Karan S., Maeda T., Luo D.G., Li S., Bronson J.D., Watt C.B.,
RA Yau K.W., Frederick J.M., Palczewski K.;
RT "The function of guanylate cyclase 1 and guanylate cyclase 2 in rod and
RT cone photoreceptors.";
RL J. Biol. Chem. 282:8837-8847(2007).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH RD3, AND TISSUE SPECIFICITY.
RX PubMed=21078983; DOI=10.1073/pnas.1010460107;
RA Azadi S., Molday L.L., Molday R.S.;
RT "RD3, the protein associated with Leber congenital amaurosis type 12, is
RT required for guanylate cyclase trafficking in photoreceptor cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21158-21163(2010).
CC -!- FUNCTION: Responsible for the synthesis of cyclic GMP (cGMP) in rods
CC and cones of photoreceptors (By similarity). Plays an essential role in
CC phototransduction, by mediating cGMP replenishment. May also
CC participate in the trafficking of membrane-asociated proteins to the
CC photoreceptor outer segment membrane (PubMed:17255100).
CC {ECO:0000250|UniProtKB:O02740, ECO:0000269|PubMed:17255100}.
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:0000250|UniProtKB:O02740};
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 (By similarity). Interacts with RD3; promotes the
CC exit of GUCY2F from the endoplasmic reticulum and its trafficking to
CC the photoreceptor outer segments (PubMed:21078983).
CC {ECO:0000250|UniProtKB:P51842, ECO:0000269|PubMed:21078983}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P51842}; Single-
CC pass type I membrane protein {ECO:0000255}. Photoreceptor outer segment
CC membrane {ECO:0000269|PubMed:21078983}; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:21078983}.
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. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit normal retinal morphology.
CC Electroretinography shows slower recovery of rod from intense
CC illumination. GUCY2F and GUCY2E double knockout mice does not show any
CC photoresponse at 4 weeks of age, rods and cones degenerate at about 2
CC month of age and the intracellular transport of some phototransduction
CC proteins is impaired. {ECO:0000269|PubMed:17255100}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AY651761; AAV54098.1; -; mRNA.
DR EMBL; AL671916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX324191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115714; AAI15715.1; -; mRNA.
DR EMBL; AK044234; BAC31833.1; -; mRNA.
DR CCDS; CCDS30446.1; -.
DR RefSeq; NP_001007577.1; NM_001007576.2.
DR RefSeq; XP_006528904.1; XM_006528841.3.
DR AlphaFoldDB; Q5SDA5; -.
DR SMR; Q5SDA5; -.
DR IntAct; Q5SDA5; 1.
DR STRING; 10090.ENSMUSP00000044521; -.
DR iPTMnet; Q5SDA5; -.
DR PhosphoSitePlus; Q5SDA5; -.
DR MaxQB; Q5SDA5; -.
DR PaxDb; Q5SDA5; -.
DR PRIDE; Q5SDA5; -.
DR ProteomicsDB; 271368; -.
DR Antibodypedia; 29460; 106 antibodies from 18 providers.
DR DNASU; 245650; -.
DR Ensembl; ENSMUST00000042530; ENSMUSP00000044521; ENSMUSG00000042282.
DR GeneID; 245650; -.
DR KEGG; mmu:245650; -.
DR UCSC; uc009ulq.2; mouse.
DR CTD; 2986; -.
DR MGI; MGI:105119; Gucy2f.
DR VEuPathDB; HostDB:ENSMUSG00000042282; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000162146; -.
DR HOGENOM; CLU_001072_1_0_1; -.
DR InParanoid; Q5SDA5; -.
DR OMA; ICRGGID; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; Q5SDA5; -.
DR TreeFam; TF106338; -.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 245650; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q5SDA5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q5SDA5; protein.
DR Bgee; ENSMUSG00000042282; Expressed in layer of retina and 10 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0120200; C:rod photoreceptor outer segment; IDA: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; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:CACAO.
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; 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; 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_0000280445"
FT TOPO_DOM 51..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..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; 124425 MW; 8A1456FCB384FA90 CRC64;
MFLGPWPFSR LLSWFAISSR LSGQHGLPSS KFLRCLCLLA LLPLLRWGQA LPYKIGVIGP
WTCDPFFSKA LPEVAAALAI ERISRDKTFD RSYSFEYVIL NEDCQTSKAL ASFISHQQMA
SGFVGPANPG FCEAASLLGT SWDKGIFSWA CVNHELDNKH SFPTFSRTLP SPIRVLVTVM
KYFQWAHAGV ISSDEDIWMH TANRVSSALR SQGLPVGVVL TSGRDSQSIQ KALQQIRQAD
RIRIIIMCMH SALIGGETQT HFLELAHDLK MTDGTYVFVP YDVLLYSLPY KHSPYQVLRN
NPKLREAYDA VLTITVESHE KTFYEAYAEA AARGEIPEKP DSNQVSPLFG TIYNSIYFIA
QAMNNAMKKN GRASAASLVQ HSRNMQFYGF NQLIKTDSNG NGISEYVILD TNGKEWELRG
TYTVDMETEL LRFRGTPIHF PGGRPTSADA KCWFAERKIC QGGIDPALAM MVCFALLIAL
LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQIISEVQS
GRSPRLSFSS GSLTPATYEN SNIAIYEGDW VWLKKFPPGD FGDIKSIKSS ASDVFEMMKD
LRHENVNPLL GFFYDSGMFA IVSEFCSRRS LEDILTNDDV KLDWMFKSSL LLDLIKGMKY
LHHREFIHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL SEEEPSEEEL LWTAPELLRA
PGGIRLGSFA GDVYSFAIIM QEVMVRGAPF CMMDLPAKEI IDRLKMPPPV YRPVVSPEYA
PAECLQLMKQ CWAEASEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR
ERTEELEIEK QKTEKLLTQM LPLSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI
LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
RIHVSLSTVT ILQTLSEGYE VELRGRTELK GKGTEETFWL VGKKGFTKPL PVPPPVGKDG
QVGHGLQPAE IAAFQRRKAE RQLVRNKP
