GUC1A_LITPI
ID GUC1A_LITPI Reviewed; 205 AA.
AC O73761;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 94.
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 Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8404;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9546678; DOI=10.1046/j.1432-1327.1998.2520591.x;
RA Li N., Fariss R.N., Zhang K., Otto-Bruc A.E., Haeseleer F., Bronson J.D.,
RA Qin N., Yamazaki A., Subbaraya I., Milam A.H., Palczewski K., Baehr W.;
RT "Guanylate-cyclase-inhibitory protein is a frog retinal Ca2+-binding
RT protein related to mammalian guanylate-cyclase-activating proteins.";
RL Eur. J. Biochem. 252:591-599(1998).
CC -!- FUNCTION: Regulatory protein that inhibits guanylyl cyclase when free
CC calcium ions concentration is elevated. 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.
CC {ECO:0000250|UniProtKB:P46065}.
CC -!- TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:9546678}.
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}.
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DR EMBL; AF047882; AAC15876.1; -; mRNA.
DR AlphaFoldDB; O73761; -.
DR SMR; O73761; -.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; 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 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 2: Evidence at transcript level;
KW Calcium; Lipoprotein; Metal-binding; Myristate; Repeat;
KW Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..205
FT /note="Guanylyl cyclase-activating protein 1"
FT /id="PRO_0000073806"
FT DOMAIN 30..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 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 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 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 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 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 153
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"
SQ SEQUENCE 205 AA; 23840 MW; 00C6564F0D3434BD CRC64;
MGNMDGKTVE ELSATEIHRW YKKFMTECPS GQLTQHEFKQ FFGLKNLSPA SNQYIEQMFD
TFDFNKDGYM DFMEYVAALS LVLKGKVEQK LRWYFKLYDV DGNGCIDRGE LLNIIKAIRA
INRCNDEMTA EEFTDMVFDK IDINGDGELS LEEFIEGVQK DELLLEVLTR SLDLKHIVYM
IQNDGKRMEI SERPRQEITT GNSLP
