GUC1A_CHICK
ID GUC1A_CHICK Reviewed; 199 AA.
AC P79880;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Guanylyl cyclase-activating protein 1;
DE Short=GCAP 1;
DE AltName: Full=Guanylate cyclase activator 1A;
GN Name=GUCA1A; Synonyms=GCAP1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8641465; DOI=10.1016/0014-5793(96)00345-6;
RA Semple-Rowland S.L., Gorczyca W.A., Buczylko J., Helekar B.S., Ruiz C.C.,
RA Subbaraya I., Palczewski K., Baehr W.;
RT "Expression of GCAP1 and GCAP2 in the retinal degeneration (rd) mutant
RT chicken retina.";
RL FEBS Lett. 385:47-52(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=10427104;
RA Semple-Rowland S.L., Larkin P., Bronson J.D., Nykamp K., Streit W.J.,
RA Baehr W.;
RT "Characterization of the chicken GCAP gene array and analyses of GCAP1,
RT GCAP2, and GC1 gene expression in normal and rd chicken pineal.";
RL Mol. Vis. 5:14-14(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-199, CALCIUM-BINDING,
RP MYRISTOYLATION AT GLY-2, AND DOMAIN.
RX PubMed=17997965; DOI=10.1016/j.str.2007.09.013;
RA Stephen R., Bereta G., Golczak M., Palczewski K., Sousa M.C.;
RT "Stabilizing function for myristoyl group revealed by the crystal structure
RT of a neuronal calcium sensor, guanylate cyclase-activating protein 1.";
RL Structure 15:1392-1402(2007).
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. This Ca(2+)-sensitive regulation of
CC retinal guanylyl cyclase is a key event in recovery of the dark state
CC of rod photoreceptors following light exposure.
CC {ECO:0000250|UniProtKB:P46065}.
CC -!- TISSUE SPECIFICITY: Retina, in rod and cone outer segments, and pineal
CC gland.
CC -!- DOMAIN: Binds three calcium ions (via EF-hands 2, 3 and 4) when calcium
CC levels are high (PubMed:17997965). Binds Mg(2+) when calcium levels are
CC low. {ECO:0000250|UniProtKB:P46065, ECO:0000269|PubMed:17997965}.
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DR EMBL; S82199; AAB47111.1; -; mRNA.
DR EMBL; AF172707; AAD47879.1; -; Genomic_DNA.
DR PIR; S68838; S68838.
DR RefSeq; NP_989651.1; NM_204320.2.
DR PDB; 2R2I; X-ray; 2.00 A; A=2-199.
DR PDBsum; 2R2I; -.
DR AlphaFoldDB; P79880; -.
DR SMR; P79880; -.
DR STRING; 9031.ENSGALP00000028327; -.
DR iPTMnet; P79880; -.
DR PaxDb; P79880; -.
DR Ensembl; ENSGALT00000002179; ENSGALP00000002177; ENSGALG00000001431.
DR GeneID; 374216; -.
DR KEGG; gga:374216; -.
DR CTD; 2978; -.
DR VEuPathDB; HostDB:geneid_374216; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000160607; -.
DR HOGENOM; CLU_072366_4_1_1; -.
DR InParanoid; P79880; -.
DR OMA; IRTINPC; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; P79880; -.
DR TreeFam; TF333971; -.
DR Reactome; R-GGA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR EvolutionaryTrace; P79880; -.
DR PRO; PR:P79880; -.
DR Proteomes; UP000000539; Chromosome 26.
DR Bgee; ENSGALG00000001431; Expressed in liver and 1 other tissue.
DR GO; GO:0120199; C:cone photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; ISS:UniProtKB.
DR GO; GO:0030249; F:guanylate cyclase regulator activity; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IEA:Ensembl.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
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 3D-structure; Calcium; Lipoprotein; Metal-binding; Myristate;
KW Reference proteome; Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..199
FT /note="Guanylyl cyclase-activating protein 1"
FT /id="PRO_0000073805"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 86..121
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 129..164
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
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 ECO:0000269|PubMed:17997965"
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 ECO:0000269|PubMed:17997965"
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 ECO:0000269|PubMed:17997965"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17997965"
FT MOD_RES 3
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:17997965"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:2R2I"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2R2I"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:2R2I"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:2R2I"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:2R2I"
SQ SEQUENCE 199 AA; 22808 MW; 2F4ED65CF471F9F6 CRC64;
MGNMDGKAVE ELSATECHQW YKKFMTECPS GQLTLYEFKQ FFGLKNLSPS ANKYVEQMFE
TFDFNKDGYI DFMEYVAALS LVLKGKVDQK LRWYFKLYDV DGNGCIDRGE LLNIIKAIRA
INRCNEAMTA EEFTNMVFDK IDINGDGELS LEEFMEGVQK DEVLLDILTR SLDLTHIVKL
IQNDGKNPHA PEEAEEAAQ
