LOCUS       NP_001007577            1108 aa            linear   ROD 27-APR-2025
DEFINITION  retinal guanylyl cyclase 2 precursor [Mus musculus].
ACCESSION   NP_001007577 XP_142224
VERSION     NP_001007577.1
DBSOURCE    REFSEQ: accession NM_001007576.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Dizhoor,A.M., Olshevskaya,E.V. and Peshenko,I.V.
  TITLE     Retinal guanylyl cyclase activation by calcium sensor proteins
            mediates photoreceptor degeneration in an rd3 mouse model of
            congenital human blindness
  JOURNAL   J Biol Chem 294 (37), 13729-13739 (2019)
   PUBMED   31346032
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Vinberg,F., Peshenko,I.V., Chen,J., Dizhoor,A.M. and Kefalov,V.J.
  TITLE     Guanylate cyclase-activating protein 2 contributes to
            phototransduction and light adaptation in mouse cone photoreceptors
  JOURNAL   J Biol Chem 293 (19), 7457-7465 (2018)
   PUBMED   29549122
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Peshenko,I.V., Olshevskaya,E.V. and Dizhoor,A.M.
  TITLE     Functional Study and Mapping Sites for Interaction with the Target
            Enzyme in Retinal Degeneration 3 (RD3) Protein
  JOURNAL   J Biol Chem 291 (37), 19713-19723 (2016)
   PUBMED   27471269
REFERENCE   4  (residues 1 to 1108)
  AUTHORS   Olshevskaya,E.V., Peshenko,I.V., Savchenko,A.B. and Dizhoor,A.M.
  TITLE     Retinal guanylyl cyclase isozyme 1 is the preferential in vivo
            target for constitutively active GCAP1 mutants causing congenital
            degeneration of photoreceptors
  JOURNAL   J Neurosci 32 (21), 7208-7217 (2012)
   PUBMED   22623665
REFERENCE   5  (residues 1 to 1108)
  AUTHORS   Makino,C.L., Wen,X.H., Olshevskaya,E.V., Peshenko,I.V.,
            Savchenko,A.B. and Dizhoor,A.M.
  TITLE     Enzymatic relay mechanism stimulates cyclic GMP synthesis in rod
            photoresponse: biochemical and physiological study in guanylyl
            cyclase activating protein 1 knockout mice
  JOURNAL   PLoS One 7 (10), e47637 (2012)
   PUBMED   23082185
REFERENCE   6  (residues 1 to 1108)
  AUTHORS   Baehr,W., Karan,S., Maeda,T., Luo,D.G., Li,S., Bronson,J.D.,
            Watt,C.B., Yau,K.W., Frederick,J.M. and Palczewski,K.
  TITLE     The function of guanylate cyclase 1 and guanylate cyclase 2 in rod
            and cone photoreceptors
  JOURNAL   J Biol Chem 282 (12), 8837-8847 (2007)
   PUBMED   17255100
  REMARK    GeneRIF: guanylate cyclase 1 and guanylate cyclase 2 have roles in
            function of rod and cone photoreceptors
REFERENCE   7  (residues 1 to 1108)
  AUTHORS   Corbo,J.C. and Cepko,C.L.
  TITLE     A hybrid photoreceptor expressing both rod and cone genes in a
            mouse model of enhanced S-cone syndrome
  JOURNAL   PLoS Genet 1 (2), e11 (2005)
   PUBMED   16110338
  REMARK    Erratum:[PLoS Genet. 2008 Jan;4(1):e18]
REFERENCE   8  (residues 1 to 1108)
  AUTHORS   Yamazaki,K., Okada,T., Mori,Y. and Tanaka,I.
  TITLE     Genetic mapping of mouse transient receptor potential (Trrp) genes
            responsible for capacitative calcium entry channels to chromosomes
            3, 7, 9, and X
  JOURNAL   Genomics 51 (2), 303-305 (1998)
   PUBMED   9722956
REFERENCE   9  (residues 1 to 1108)
  AUTHORS   Li,Y., Lemaire,P. and Behringer,R.R.
  TITLE     Esx1, a novel X chromosome-linked homeobox gene expressed in mouse
            extraembryonic tissues and male germ cells
  JOURNAL   Dev Biol 188 (1), 85-95 (1997)
   PUBMED   9245514
REFERENCE   10 (residues 1 to 1108)
  AUTHORS   Yang,R.B., Fulle,H.J. and Garbers,D.L.
  TITLE     Chromosomal localization and genomic organization of genes encoding
            guanylyl cyclase receptors expressed in olfactory sensory neurons
            and retina
  JOURNAL   Genomics 31 (3), 367-372 (1996)
   PUBMED   8838319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK044234.1, AY651761.1 and AL671916.5.
            
            On Dec 15, 2004 this sequence version replaced XP_142224.4.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY651761.1, SRR17784643.47345.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849381,
                                           SAMN00849383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="X"
                     /map="X 62.85 cM"
     Protein         1..1108
                     /product="retinal guanylyl cyclase 2 precursor"
                     /EC_number="4.6.1.2"
                     /note="retinal guanylyl cyclase 2"
                     /calculated_mol_wt=118771
     sig_peptide     1..50
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5673
     mat_peptide     51..1108
                     /product="Retinal guanylyl cyclase 2. /id=PRO_0000280445"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SDA5.1)"
                     /calculated_mol_wt=118771
     Region          54..435
                     /region_name="PBP1_sensory_GC_DEF-like"
                     /note="ligand-binding domain of membrane guanylyl cyclases
                     (GC-D, GC-E, and GC-F) that are specifically expressed in
                     sensory tissues; cd06371"
                     /db_xref="CDD:380594"
     Site            order(102,127..128)
                     /site_type="other"
                     /note="putative Cl binding site [ion binding]"
                     /db_xref="CDD:380594"
     Site            order(111,115,133,137,142,199..200,203,206)
                     /site_type="other"
                     /note="putative dimer interface (closed form) [polypeptide
                     binding]"
                     /db_xref="CDD:380594"
     Site            order(133,137,199..200,203,206..207,218)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380594"
     Site            order(236..237,261,268)
                     /site_type="other"
                     /note="putative dimer interface (open form) [polypeptide
                     binding]"
                     /db_xref="CDD:380594"
     Site            470..490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SDA5.1)"
     Region          545..815
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(546..549,552,554,583,585,607,623..626,670,674..675,
                     677,687..688)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <824..869
                     /region_name="HNOBA"
                     /note="Heme NO binding associated; pfam07701"
                     /db_xref="CDD:462234"
     Region          848..1040
                     /region_name="CYCc"
                     /note="Adenylyl- / guanylyl cyclase, catalytic domain;
                     smart00044"
                     /db_xref="CDD:214485"
     Site            order(887,889..894,929,931..933,936,1001..1003,1007..1008,
                     1011..1012,1050)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(889,933)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(894,906,909..910,913,917,929..930,989,992,
                     1002..1005,1008,1050)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     CDS             1..1108
                     /gene="Gucy2f"
                     /gene_synonym="A930002I06; GC-F; GC2"
                     /coded_by="NM_001007576.2:246..3572"
                     /db_xref="CCDS:CCDS30446.1"
                     /db_xref="GeneID:245650"
                     /db_xref="MGI:MGI:105119"
ORIGIN      
        1 mflgpwpfsr llswfaissr lsgqhglpss kflrclclla llpllrwgqa lpykigvigp
       61 wtcdpffska lpevaaalai erisrdktfd rsysfeyvil nedcqtskal asfishqqma
      121 sgfvgpanpg fceaasllgt swdkgifswa cvnheldnkh sfptfsrtlp spirvlvtvm
      181 kyfqwahagv issdediwmh tanrvssalr sqglpvgvvl tsgrdsqsiq kalqqirqad
      241 ririiimcmh saliggetqt hflelahdlk mtdgtyvfvp ydvllyslpy khspyqvlrn
      301 npklreayda vltitveshe ktfyeayaea aargeipekp dsnqvsplfg tiynsiyfia
      361 qamnnamkkn grasaaslvq hsrnmqfygf nqliktdsng ngiseyvild tngkewelrg
      421 tytvdmetel lrfrgtpihf pggrptsada kcwfaerkic qggidpalam mvcfallial
      481 lsingfayfi rrrinkiqli kgpnrilltl edvtfinphf gskrgsrasv sfqiisevqs
      541 grsprlsfss gsltpatyen sniaiyegdw vwlkkfppgd fgdiksikss asdvfemmkd
      601 lrhenvnpll gffydsgmfa ivsefcsrrs lediltnddv kldwmfkssl lldlikgmky
      661 lhhrefihgr lksrncvvdg rfvlkvtdyg fndilemlrl seeepseeel lwtapellra
      721 pggirlgsfa gdvysfaiim qevmvrgapf cmmdlpakei idrlkmpppv yrpvvspeya
      781 paeclqlmkq cwaeaseqrp tfdeifnqfk tfnkgkktni idsmlrmleq yssnledlir
      841 erteeleiek qkteklltqm lplsvaeslk kgctvepegf dlvtlyfsdi vgfttisams
      901 epievvdlln dlytlfdaii gshdvykvet igdaymvasg lpkrngsrha aeianmsldi
      961 lssvgtfkmr hmpevpvrir iglhsgpvva gvvgltmpry clfgdtvnta srmestglpy
     1021 rihvslstvt ilqtlsegye velrgrtelk gkgteetfwl vgkkgftkpl pvpppvgkdg
     1081 qvghglqpae iaafqrrkae rqlvrnkp
//
