GenomeNet

Database: UniProt
Entry: O73763
LinkDB: O73763
Original site: O73763 
ID   GCIP_LITPI              Reviewed;         206 AA.
AC   O73763;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   22-FEB-2023, entry version 93.
DE   RecName: Full=Guanylyl cyclase inhibitory protein;
GN   Name=GCIP;
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].
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: Does not stimulate guanylyl cyclase (GC) when free calcium
CC       ion concentration is low, but inhibits GC when free calcium ions
CC       concentration is elevated.
CC   -!- TISSUE SPECIFICITY: Retina; inner segments, somata and synaptic
CC       terminals of cone receptors.
CC   -!- MISCELLANEOUS: Binds two calcium ions. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF047884; AAC15878.1; -; mRNA.
DR   AlphaFoldDB; O73763; -.
DR   SMR; O73763; -.
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   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR028846; Recoverin.
DR   PANTHER; PTHR23055; CALCIUM BINDING PROTEINS; 1.
DR   PANTHER; PTHR23055:SF85; SI:CH211-245J22.3; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
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..206
FT                   /note="Guanylyl cyclase inhibitory protein"
FT                   /id="PRO_0000073813"
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          135..170
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         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         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   206 AA;  23653 MW;  FDCD8F6BE17DA7D9 CRC64;
     MGQVASMPHR CGTYVLELHE WYRKFVEECP SGLITLHEFR QFFSDVTVGE NSSEYAEQIF
     RALDNNGDGI VDFREYVTAI SMLAHGTPED KLKWSFKLYD KDGDGAITRS EMLEIMRAVY
     KMSVVASLTK VNPMTAEECT NRIFVRLDKD QNAIISLQEF VDGSLGDEWV RQMLECDLST
     VEIQKMTKHS HLPARSSRER LFHANT
//
DBGET integrated database retrieval system