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VISL1_BOVIN
ID   VISL1_BOVIN             Reviewed;         191 AA.
AC   P62763; P28677; P29103; P42323; Q3ZBI8; Q9UM20;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Visinin-like protein 1;
DE   AltName: Full=Neurocalcin-alpha;
GN   Name=VSNL1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9560316; DOI=10.1042/bj3310871;
RA   Kato M., Watanabe Y., Iino S., Takaoka Y., Kobayashi S., Haga T.,
RA   Hidaka H.;
RT   "Cloning and expression of a cDNA encoding a new neurocalcin isoform
RT   (neurocalcin alpha) from bovine brain.";
RL   Biochem. J. 331:871-876(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 8-27 AND 100-130.
RC   TISSUE=Brain;
RX   PubMed=1527077; DOI=10.1016/s0021-9258(18)41816-9;
RA   Terasawa M., Nakano A., Kobayashi R., Hidaka H.;
RT   "Neurocalcin: a novel calcium-binding protein from bovine brain.";
RL   J. Biol. Chem. 267:19596-19599(1992).
CC   -!- FUNCTION: Regulates (in vitro) the inhibition of rhodopsin
CC       phosphorylation in a calcium-dependent manner.
CC   -!- TISSUE SPECIFICITY: Brain and retina. Neuron-specific in the central
CC       and peripheral nervous system.
CC   -!- MISCELLANEOUS: Probably binds three calcium ions.
CC   -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR   EMBL; AB006006; BAA28716.1; -; mRNA.
DR   EMBL; BC103271; AAI03272.1; -; mRNA.
DR   RefSeq; NP_776915.1; NM_174490.3.
DR   AlphaFoldDB; P62763; -.
DR   SMR; P62763; -.
DR   STRING; 9913.ENSBTAP00000022814; -.
DR   PaxDb; P62763; -.
DR   Ensembl; ENSBTAT00000022814; ENSBTAP00000022814; ENSBTAG00000017158.
DR   GeneID; 282124; -.
DR   KEGG; bta:282124; -.
DR   CTD; 7447; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017158; -.
DR   VGNC; VGNC:36841; VSNL1.
DR   eggNOG; KOG0044; Eukaryota.
DR   GeneTree; ENSGT00940000156513; -.
DR   HOGENOM; CLU_072366_1_0_1; -.
DR   InParanoid; P62763; -.
DR   OMA; ALFTCSC; -.
DR   OrthoDB; 1369072at2759; -.
DR   TreeFam; TF300009; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000017158; Expressed in occipital lobe and 91 other tissues.
DR   ExpressionAtlas; P62763; 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   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_0000073762"
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        25
FT                   /note="H -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="R -> P (in Ref. 3; AA sequence)"
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
 
 
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