GUC1A_MOUSE
ID GUC1A_MOUSE Reviewed; 202 AA.
AC P43081; Q8R0H3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Guanylyl cyclase-activating protein 1;
DE Short=GCAP 1;
DE AltName: Full=Guanylate cyclase activator 1A;
GN Name=Guca1a; Synonyms=Gcap, Gcap1, Guca1;
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=BALB/cJ; TISSUE=Retina;
RX PubMed=7983048; DOI=10.1016/s0021-9258(18)47393-0;
RA Subbaraya I., Ruiz C.C., Helekar B.S., Zhao X., Gorczyca W.A.,
RA Pettenati M.J., Rao P.N., Palczewski K., Baehr W.;
RT "Molecular characterization of human and mouse photoreceptor guanylate
RT cyclase-activating protein (GCAP) and chromosomal localization of the human
RT gene.";
RL J. Biol. Chem. 269:31080-31089(1994).
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9620085;
RA Cuenca N., Lopez S., Howes K., Kolb H.;
RT "The localization of guanylyl cyclase-activating proteins in the mammalian
RT retina.";
RL Invest. Ophthalmol. Vis. Sci. 39:1243-1250(1998).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15961391; DOI=10.1074/jbc.m501789200;
RA Strissel K.J., Lishko P.V., Trieu L.H., Kennedy M.J., Hurley J.B.,
RA Arshavsky V.Y.;
RT "Recoverin undergoes light-dependent intracellular translocation in rod
RT photoreceptors.";
RL J. Biol. Chem. 280:29250-29255(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25673692; DOI=10.1074/jbc.m115.639591;
RA Sakurai K., Chen J., Khani S.C., Kefalov V.J.;
RT "Regulation of mammalian cone phototransduction by recoverin and rhodopsin
RT kinase.";
RL J. Biol. Chem. 290:9239-9250(2015).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=29435986; DOI=10.1113/jp275779;
RA Morshedian A., Woodruff M.L., Fain G.L.;
RT "Role of recoverin in rod photoreceptor light adaptation.";
RL J. Physiol. (Lond.) 596:1513-1526(2018).
CC -!- FUNCTION: Stimulates retinal guanylyl cyclase when free calcium ions
CC concentration is low and inhibits guanylyl cyclase when free calcium
CC ions concentration is elevated (By similarity). This Ca(2+)-sensitive
CC regulation of retinal guanylyl cyclase is a key event in recovery of
CC the dark state of rod photoreceptors following light exposure (By
CC similarity). May be involved in cone photoreceptor light response and
CC recovery of response in bright light (PubMed:25673692).
CC {ECO:0000250|UniProtKB:P46065, ECO:0000269|PubMed:25673692}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P43080}.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor
CC {ECO:0000250|UniProtKB:P46065}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:9620085}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:15961391,
CC ECO:0000269|PubMed:9620085}. Note=Subcellular location is not affected
CC by light or dark conditions.
CC -!- TISSUE SPECIFICITY: In the retina, expressed in rod photoreceptors (at
CC protein level) (PubMed:9620085). Expressed in cone photoreceptors
CC (PubMed:9620085). {ECO:0000269|PubMed:15961391,
CC ECO:0000269|PubMed:9620085}.
CC -!- DOMAIN: Binds three calcium ions (via EF-hands 2, 3 and 4) when calcium
CC levels are high. Binds Mg(2+) when calcium levels are low.
CC {ECO:0000250|UniProtKB:P46065}.
CC -!- DISRUPTION PHENOTYPE: Guca1a and Guca1b double knockout mice show an
CC increase in response to light in dark-adapted cone photoreceptors
CC (PubMed:25673692). Dark-adapted cone photoreceptors show a delayed
CC response time and a delayed recovery time in response to light
CC (PubMed:25673692). Guca1a, Guca1b and Rcvrn triple knockout mice show
CC rod photoreceptors have a reduced current decay during light response
CC (PubMed:29435986). {ECO:0000269|PubMed:25673692,
CC ECO:0000269|PubMed:29435986}.
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DR EMBL; L36860; AAA60716.1; -; mRNA.
DR EMBL; AC112683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466559; EDL23558.1; -; Genomic_DNA.
DR EMBL; CH466559; EDL23559.1; -; Genomic_DNA.
DR EMBL; CH466559; EDL23560.1; -; Genomic_DNA.
DR EMBL; BC026834; AAH26834.1; -; mRNA.
DR EMBL; BC031810; AAH31810.1; -; mRNA.
DR CCDS; CCDS28848.1; -.
DR PIR; B55331; B55331.
DR RefSeq; NP_032215.2; NM_008189.3.
DR RefSeq; XP_011244598.1; XM_011246296.2.
DR AlphaFoldDB; P43081; -.
DR SMR; P43081; -.
DR STRING; 10090.ENSMUSP00000060027; -.
DR PaxDb; P43081; -.
DR PRIDE; P43081; -.
DR ProteomicsDB; 271490; -.
DR Antibodypedia; 30136; 193 antibodies from 29 providers.
DR DNASU; 14913; -.
DR Ensembl; ENSMUST00000059348; ENSMUSP00000060027; ENSMUSG00000023982.
DR GeneID; 14913; -.
DR KEGG; mmu:14913; -.
DR UCSC; uc008cvc.1; mouse.
DR CTD; 2978; -.
DR MGI; MGI:102770; Guca1a.
DR VEuPathDB; HostDB:ENSMUSG00000023982; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000160607; -.
DR HOGENOM; CLU_072366_4_1_1; -.
DR InParanoid; P43081; -.
DR OMA; IRTINPC; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; P43081; -.
DR TreeFam; TF333971; -.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 14913; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Guca1a; mouse.
DR PRO; PR:P43081; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P43081; protein.
DR Bgee; ENSMUSG00000023982; Expressed in layer of retina and 65 other tissues.
DR Genevisible; P43081; MM.
DR GO; GO:0120199; C:cone photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; IDA:MGI.
DR GO; GO:0030249; F:guanylate cyclase regulator activity; IGI:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IMP:MGI.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; ISO:MGI.
DR GO; GO:0031282; P:regulation of guanylate cyclase activity; IGI:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR033022; GUCA1A.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR PANTHER; PTHR23055:SF13; PTHR23055:SF13; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..202
FT /note="Guanylyl cyclase-activating protein 1"
FT /id="PRO_0000073804"
FT DOMAIN 31..49
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 51..86
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 87..122
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 131..166
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 3
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P46065"
FT CONFLICT 4
FT /note="I -> V (in Ref. 1; AAA60716)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="C -> V (in Ref. 1; AAA60716)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="G -> S (in Ref. 1; AAA60716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22986 MW; EC76CBF7C518C76B CRC64;
MGNIMEGKSV EELSSTECHQ WYKKFMTECP SGQLTLYEFR QFFGLKNLSP SASQYVEQMF
ETFDFNKDGY IDFMEYVAAL SLVLKGKVEQ KLRWYFKLYD VDGNGCIDRD ELLTIIRAIR
TINPWSDSSM SAEEFTDTVF AKIDINGDGE LSLEEFMEGV QKDQMLLDTL TRSLDLTGIV
RRLQNGEHEE AGTGDLAAEA AG
