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Database: UniProt
Entry: W5NI98_LEPOC
LinkDB: W5NI98_LEPOC
Original site: W5NI98_LEPOC 
ID   W5NI98_LEPOC            Unreviewed;       204 AA.
AC   W5NI98;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Visinin-like protein 1 {ECO:0000256|ARBA:ARBA00018066};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020357.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000020357.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Regulates (in vitro) the inhibition of rhodopsin
CC       phosphorylation in a calcium-dependent manner.
CC       {ECO:0000256|ARBA:ARBA00002143}.
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC       {ECO:0000256|ARBA:ARBA00006049}.
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DR   EMBL; AHAT01009116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01009117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01009118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01009119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NI98; -.
DR   STRING; 7918.ENSLOCP00000020357; -.
DR   Ensembl; ENSLOCT00000020391.1; ENSLOCP00000020357.1; ENSLOCG00000016480.1.
DR   eggNOG; KOG0044; Eukaryota.
DR   GeneTree; ENSGT00940000156513; -.
DR   HOGENOM; CLU_072366_1_0_1; -.
DR   InParanoid; W5NI98; -.
DR   OMA; HISRREM; -.
DR   Proteomes; UP000018468; Linkage group LG1.
DR   Bgee; ENSLOCG00000016480; Expressed in brain and 8 other cell types or tissues.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   CDD; cd00051; EFh; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
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:SF101; VISININ-LIKE PROTEIN 1; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          73..108
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          109..144
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          159..194
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   204 AA;  23676 MW;  081E00F2FD1220C6 CRC64;
     MSLWHGFLEE TETMGKQNSK LAPEVMEDLV KSTEFNEHEL KQWYKGFLKD CPSGRLNLDE
     FQQLYVKFFP YGDASKFAQH AFRTFDKNGD GTIDFREFIC ALSITSRGSF EQKLNWAFNM
     YDLDGDGKIT RVEMLEIIEA IYKMVGTVIM MKMNEDGLTP EQRVDKIFSK MDKNNDDQIT
     LDEFKEAAKS DPSIVLLLQC DIQK
//
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