VISL1_PONAB
ID VISL1_PONAB Reviewed; 191 AA.
AC Q5RD22; Q5R6Z3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Visinin-like protein 1;
DE Short=VILIP;
GN Name=VSNL1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates (in vitro) the inhibition of rhodopsin
CC phosphorylation in a calcium-dependent manner. {ECO:0000250}.
CC -!- MISCELLANEOUS: Probably binds three calcium ions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; CR858096; CAH90335.1; -; mRNA.
DR EMBL; CR860330; CAH92467.1; -; mRNA.
DR RefSeq; NP_001126454.1; NM_001132982.1.
DR AlphaFoldDB; Q5RD22; -.
DR SMR; Q5RD22; -.
DR STRING; 9601.ENSPPYP00000023634; -.
DR Ensembl; ENSPPYT00000014673; ENSPPYP00000014102; ENSPPYG00000012631.
DR GeneID; 100173440; -.
DR KEGG; pon:100173440; -.
DR CTD; 7447; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000156513; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; Q5RD22; -.
DR OMA; ALFTCSC; -.
DR OrthoDB; 1369072at2759; -.
DR TreeFam; TF300009; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
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; IPR028846; Recoverin.
DR InterPro; IPR029533; VILIP-1.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR PANTHER; PTHR23055:SF101; PTHR23055:SF101; 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; 4.
PE 2: Evidence at transcript level;
KW Calcium; Lipoprotein; Metal-binding; Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..191
FT /note="Visinin-like protein 1"
FT /id="PRO_0000269887"
FT DOMAIN 40..58
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..131
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 146..181
FT /note="EF-hand 4"
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 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
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 BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
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:0000250"
FT CONFLICT 109
FT /note="D -> G (in Ref. 1; CAH92467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 22142 MW; ACDC3B4FE8C79265 CRC64;
MGKQNSKLAP EVMEDLVKST EFNEHELKQW YKGFLKDCPS GRLNLEEFQQ LYVKFFPYGD
ASKFAQHAFR TFDKNGDGTI DFREFICALS ITSRGSFEQK LNWAFNMYDL DGDGKITRVE
MLEIIEAIYK MVGTVIMMKM NEDGLTPEQR VDKIFSKMDK NKDDQITLDE FKEAAKSDPS
IVLLLQCDIQ K
