VISL1_CHICK
ID VISL1_CHICK Reviewed; 191 AA.
AC P62764; 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 119.
DE RecName: Full=Visinin-like protein 1;
DE Short=VILIP;
DE AltName: Full=OZ1;
GN Name=VSNL1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=1359372; DOI=10.1016/0169-328x(92)90160-d;
RA Lenz S., Henschel Y., Zopf D., Voss B., Gundelfinger E.D.;
RT "VILIP, a cognate protein of the retinal calcium binding proteins visinin
RT and recoverin, is expressed in the developing chicken brain.";
RL Brain Res. Mol. Brain Res. 15:133-140(1992).
CC -!- FUNCTION: Regulates (in vitro) the inhibition of rhodopsin
CC phosphorylation in a calcium-dependent manner. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed in the brain but not detectable in
CC liver, heart or skeletal muscle. {ECO:0000269|PubMed:1359372}.
CC -!- MISCELLANEOUS: Probably binds three calcium ions.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; X63530; CAA45093.1; -; mRNA.
DR PIR; A48979; A48979.
DR RefSeq; NP_990586.1; NM_205255.1.
DR RefSeq; XP_015140438.1; XM_015284952.1.
DR RefSeq; XP_015140439.1; XM_015284953.1.
DR RefSeq; XP_015140440.1; XM_015284954.1.
DR RefSeq; XP_015140441.1; XM_015284955.1.
DR RefSeq; XP_015140442.1; XM_015284956.1.
DR AlphaFoldDB; P62764; -.
DR SMR; P62764; -.
DR BioGRID; 676449; 2.
DR IntAct; P62764; 1.
DR STRING; 9031.ENSGALP00000026514; -.
DR PaxDb; P62764; -.
DR Ensembl; ENSGALT00000026565; ENSGALP00000026514; ENSGALG00000016464.
DR GeneID; 396189; -.
DR KEGG; gga:396189; -.
DR CTD; 7447; -.
DR VEuPathDB; HostDB:geneid_396189; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000156513; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P62764; -.
DR PhylomeDB; P62764; -.
DR TreeFam; TF300009; -.
DR PRO; PR:P62764; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000016464; Expressed in brain and 9 other tissues.
DR ExpressionAtlas; P62764; baseline and differential.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 /evidence="ECO:0000250"
FT CHAIN 2..191
FT /note="Visinin-like protein 1"
FT /id="PRO_0000073766"
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
