GUC1B_BOVIN
ID GUC1B_BOVIN Reviewed; 204 AA.
AC P51177;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Guanylyl cyclase-activating protein 2;
DE Short=GCAP 2;
DE AltName: Full=Guanylate cyclase activator 1B;
DE AltName: Full=Retinal guanylyl cyclase activator protein p24;
GN Name=GUCA1B; Synonyms=GCAP-2, GCAP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Retina;
RX PubMed=7559656; DOI=10.1074/jbc.270.42.25200;
RA Dizhoor A.M., Olshevskaya E.V., Henzel W.J., Wong S.C., Stults J.T.,
RA Ankoudinova I., Hurley J.B.;
RT "Cloning, sequencing, and expression of a 24-kDa Ca(2+)-binding protein
RT activating photoreceptor guanylyl cyclase.";
RL J. Biol. Chem. 270:25200-25206(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-81, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Retina;
RX PubMed=7665624; DOI=10.1074/jbc.270.37.22029;
RA Gorczyca W.A., Polans A.S., Surgucheva I.G., Subbaraya I., Baehr W.,
RA Palczewski K.;
RT "Guanylyl cyclase activating protein. A calcium-sensitive regulator of
RT phototransduction.";
RL J. Biol. Chem. 270:22029-22036(1995).
RN [3]
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 [4]
RP STRUCTURE BY NMR, MYRISTOYLATION AT GLY-2, AND CALCIUM-BINDING.
RX PubMed=10383444; DOI=10.1074/jbc.274.27.19329;
RA Ames J.B., Dizhoor A.M., Ikura M., Palczewski K., Stryer L.;
RT "Three-dimensional structure of guanylyl cyclase activating protein-2, a
RT calcium-sensitive modulator of photoreceptor guanylyl cyclases.";
RL J. Biol. Chem. 274:19329-19337(1999).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF TYR-104.
RX PubMed=9651312; DOI=10.1074/jbc.273.28.17311;
RA Dizhoor A.M., Boikov S.G., Olshevskaya E.V.;
RT "Constitutive activation of photoreceptor guanylate cyclase by Y99C mutant
RT of GCAP-1. Possible role in causing human autosomal dominant cone
RT degeneration.";
RL J. Biol. Chem. 273:17311-17314(1998).
CC -!- FUNCTION: Stimulates two retinal guanylyl cyclases (GCs) GUCY2D and
CC GUCY2F when free calcium ions concentration is low, and inhibits GUCY2D
CC and GUCY2F when free calcium ions concentration is elevated
CC (PubMed:7665624). This Ca(2+)-sensitive regulation of GCs is a key
CC event in recovery of the dark state of rod photoreceptors following
CC light exposure (PubMed:9651312). May be involved in cone photoreceptor
CC response and recovery of response in bright light (By similarity).
CC {ECO:0000250|UniProtKB:Q8VBV8, ECO:0000269|PubMed:7665624,
CC ECO:0000269|PubMed:9651312}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7665624};
CC Lipid-anchor {ECO:0000269|PubMed:7665624}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:9620085}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:7665624, ECO:0000269|PubMed:9620085}.
CC Note=Subcellular location is not affected by light or dark conditions.
CC {ECO:0000250|UniProtKB:Q8VBV8}.
CC -!- TISSUE SPECIFICITY: In the retina, expressed in rod and cone
CC photoreceptor cells. Appears to be more abundant in rods.
CC {ECO:0000269|PubMed:9620085}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Binds three calcium ions.
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DR EMBL; U32856; AAC48478.1; -; mRNA.
DR EMBL; L43001; AAA83214.1; -; mRNA.
DR PIR; A57604; A57604.
DR RefSeq; NP_777211.1; NM_174786.1.
DR PDB; 1JBA; NMR; -; A=1-204.
DR PDBsum; 1JBA; -.
DR AlphaFoldDB; P51177; -.
DR BMRB; P51177; -.
DR SMR; P51177; -.
DR ELM; P51177; -.
DR STRING; 9913.ENSBTAP00000035936; -.
DR iPTMnet; P51177; -.
DR PaxDb; P51177; -.
DR GeneID; 286851; -.
DR KEGG; bta:286851; -.
DR CTD; 2979; -.
DR eggNOG; KOG0044; Eukaryota.
DR InParanoid; P51177; -.
DR OrthoDB; 1271942at2759; -.
DR EvolutionaryTrace; P51177; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 2.
DR DisProt; DP01010; -.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cell projection;
KW Direct protein sequencing; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:10383444"
FT CHAIN 2..204
FT /note="Guanylyl cyclase-activating protein 2"
FT /id="PRO_0000073807"
FT DOMAIN 19..54
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 56..91
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 92..127
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 145..180
FT /note="EF-hand 4"
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 73
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 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 109
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 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
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:0000305|PubMed:10383444"
FT MUTAGEN 104
FT /note="Y->C: Partial loss of activity but no loss of
FT calcium sensitivity."
FT /evidence="ECO:0000269|PubMed:9651312"
FT HELIX 8..12
FT /evidence="ECO:0007829|PDB:1JBA"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:1JBA"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:1JBA"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:1JBA"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:1JBA"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:1JBA"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:1JBA"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1JBA"
SQ SEQUENCE 204 AA; 23728 MW; BA375D54960E5F75 CRC64;
MGQQFSWEEA EENGAVGAAD AAQLQEWYKK FLEECPSGTL FMHEFKRFFK VPDNEEATQY
VEAMFRAFDT NGDNTIDFLE YVAALNLVLR GTLEHKLKWT FKIYDKDRNG CIDRQELLDI
VESIYKLKKA CSVEVEAEQQ GKLLTPEEVV DRIFLLVDEN GDGQLSLNEF VEGARRDKWV
MKMLQMDLNP SSWISQQRRK SAMF
