VISL1_MOUSE
ID VISL1_MOUSE Reviewed; 191 AA.
AC P62761; P28677; P29103; P42323; Q9UM20;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Visinin-like protein 1;
DE Short=VILIP;
DE AltName: Full=Neural visinin-like protein 1;
DE Short=NVL-1;
DE Short=NVP-1;
GN Name=Vsnl1; Synonyms=Visl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Shirai Y., Asami M., Mukai H., Chang C., Shuntoh H., Kuno T., Tanaka C.;
RT "cDNA cloning and primary structure of mouse neural visinin-like CA2+-
RT binding protein type 1 (NVP-1).";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Anton B., Matus M., Leff P., Calva J.C., Acevedo R., Hernandez A.,
RA Medecigo M., Valdez A., Sanchez Lopez R., Vergara P., Torner C.,
RA Segovia J., Alagon A.;
RT "Searching for the endomorphin-1-2 pro-peptide precursor(s) protein(s):
RT cloning of a protein encoding an endomorphin-2-like peptide sequence.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 8-18; 43-63 AND 119-150, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; D21165; BAA04701.1; -; mRNA.
DR EMBL; AY101375; AAM48292.1; -; mRNA.
DR EMBL; BC046226; AAH46226.1; -; mRNA.
DR CCDS; CCDS25816.1; -.
DR RefSeq; NP_036168.1; NM_012038.4.
DR AlphaFoldDB; P62761; -.
DR SMR; P62761; -.
DR BioGRID; 205085; 5.
DR IntAct; P62761; 1.
DR MINT; P62761; -.
DR STRING; 10090.ENSMUSP00000072145; -.
DR iPTMnet; P62761; -.
DR PhosphoSitePlus; P62761; -.
DR SwissPalm; P62761; -.
DR PaxDb; P62761; -.
DR PeptideAtlas; P62761; -.
DR PRIDE; P62761; -.
DR ProteomicsDB; 297922; -.
DR Antibodypedia; 27025; 1393 antibodies from 35 providers.
DR DNASU; 26950; -.
DR Ensembl; ENSMUST00000072299; ENSMUSP00000072145; ENSMUSG00000054459.
DR Ensembl; ENSMUST00000220506; ENSMUSP00000152711; ENSMUSG00000054459.
DR GeneID; 26950; -.
DR KEGG; mmu:26950; -.
DR UCSC; uc011ykf.1; mouse.
DR CTD; 7447; -.
DR MGI; MGI:1349453; Vsnl1.
DR VEuPathDB; HostDB:ENSMUSG00000054459; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000156513; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P62761; -.
DR OMA; ALFTCSC; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P62761; -.
DR TreeFam; TF300009; -.
DR BioGRID-ORCS; 26950; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Vsnl1; mouse.
DR PRO; PR:P62761; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P62761; protein.
DR Bgee; ENSMUSG00000054459; Expressed in retrosplenial region and 161 other tissues.
DR ExpressionAtlas; P62761; baseline and differential.
DR Genevisible; P62761; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; IDA:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:MGI.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Lipoprotein; Metal-binding; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..191
FT /note="Visinin-like protein 1"
FT /id="PRO_0000073764"
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"
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
