GUC1B_CHICK
ID GUC1B_CHICK Reviewed; 198 AA.
AC P79881;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Guanylyl cyclase-activating protein 2;
DE Short=GCAP 2;
DE AltName: Full=Guanylate cyclase activator 1B;
GN Name=GUCA1B; Synonyms=GCAP2;
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], AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Stimulates synthesis of cGMP in photoreceptors. Thought to
CC mediate Ca(2+)-sensitive regulation of retinal guanylyl cyclase (GC), a
CC key event in recovery of the dark state of rod photoreceptors following
CC light exposure (By similarity). {ECO:0000250|UniProtKB:P51177}.
CC -!- SUBUNIT: Undergoes dimerization at low calcium ions concentration,
CC while the presence of calcium ions inhibits its dimerization.
CC Dimerization correlates with its ability to activate GC.
CC -!- TISSUE SPECIFICITY: Retina and pineal gland.
CC {ECO:0000269|PubMed:10427104}.
CC -!- MISCELLANEOUS: Binds three calcium ions. {ECO:0000250}.
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DR EMBL; S82200; AAB47112.1; -; mRNA.
DR EMBL; AF172708; AAD47880.1; -; Genomic_DNA.
DR PIR; S68839; S68839.
DR RefSeq; NP_001007882.1; NM_001007881.2.
DR AlphaFoldDB; P79881; -.
DR SMR; P79881; -.
DR STRING; 9031.ENSGALP00000034499; -.
DR PaxDb; P79881; -.
DR Ensembl; ENSGALT00000090927; ENSGALP00000069354; ENSGALG00000001418.
DR GeneID; 419864; -.
DR KEGG; gga:419864; -.
DR CTD; 2979; -.
DR VEuPathDB; HostDB:geneid_419864; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000157530; -.
DR HOGENOM; CLU_072366_4_0_1; -.
DR InParanoid; P79881; -.
DR OMA; HEFKGFF; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; P79881; -.
DR TreeFam; TF333971; -.
DR Reactome; R-GGA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:P79881; -.
DR Proteomes; UP000000539; Chromosome 26.
DR Bgee; ENSGALG00000001418; Expressed in testis and 2 other tissues.
DR ExpressionAtlas; P79881; baseline.
DR GO; GO:0120199; C:cone photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; IBA:GO_Central.
DR GO; GO:0031282; P:regulation of guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
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; IPR015756; GCAP-2.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR PANTHER; PTHR23055:SF11; PTHR23055:SF11; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Lipoprotein; Metal-binding; Myristate; Reference proteome; Repeat;
KW Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..198
FT /note="Guanylyl cyclase-activating protein 2"
FT /id="PRO_0000073810"
FT DOMAIN 16..51
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 52..87
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 88..123
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 139..174
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 198 AA; 23128 MW; 7A2B475FCD34964F CRC64;
MGQQFTNAEG EQTEIDVAEL QEWYKKFVVE CPSGTLFMHE FKRFFGVQDN HEAAEYIENM
FRAFDKNGDN TIDFLEYVAA LNLVLRGKLE HKLRWTFKVY DKDGNGCIDK PELLEIVESI
YKLKKVCRSE VEERTPLLTP EEVVDRIFQL VDENGDGQLS LDEFIDGARK DKWVMKMLQM
DVNPGGWISE QRRKSALF
