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Database: UniProt
Entry: W5MVZ1_LEPOC
LinkDB: W5MVZ1_LEPOC
Original site: W5MVZ1_LEPOC 
ID   W5MVZ1_LEPOC            Unreviewed;       260 AA.
AC   W5MVZ1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Calbindin {ECO:0000256|ARBA:ARBA00018599};
GN   Name=CALB1 {ECO:0000313|Ensembl:ENSLOCP00000012550.1};
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:ENSLOCP00000012550.1, 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:ENSLOCP00000012550.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-
CC       ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
CC       {ECO:0000256|ARBA:ARBA00025400}.
CC   -!- SIMILARITY: Belongs to the calbindin family.
CC       {ECO:0000256|ARBA:ARBA00007217}.
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DR   EMBL; AHAT01004672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01004673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006636064.1; XM_006636001.2.
DR   AlphaFoldDB; W5MVZ1; -.
DR   Ensembl; ENSLOCT00000012573.1; ENSLOCP00000012550.1; ENSLOCG00000010243.1.
DR   GeneID; 102691626; -.
DR   KEGG; loc:102691626; -.
DR   CTD; 793; -.
DR   GeneTree; ENSGT00950000183108; -.
DR   HOGENOM; CLU_054826_1_1_1; -.
DR   OrthoDB; 3218718at2759; -.
DR   Proteomes; UP000018468; Linkage group LG11.
DR   Bgee; ENSLOCG00000010243; Expressed in mesonephros and 9 other cell types or tissues.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.238.10; EF-hand; 3.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR19972; CALBINDIN; 1.
DR   PANTHER; PTHR19972:SF14; CALBINDIN; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
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};
KW   Vitamin D {ECO:0000256|ARBA:ARBA00022897}.
FT   DOMAIN          11..46
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          97..132
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          141..176
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          185..220
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   260 AA;  30128 MW;  CA1ABCA5E6D2B4A9 CRC64;
     MANAYLQGVE ISATQFLDIF RHYDNDGNGY IEGKELQNFI KELQQARKQA GLELTEQMKA
     FVEEYEQNAG GKIGIVELVQ ILPTEENFLL FFRQQLKSCA EFMQAWRKYD ADHSGYIEAD
     ELKNFLRDLL LKAKKTYDDK KLDEYTQTTL KIFDSNNDGK LCLAEMARLL PDQENFLLKF
     QGVKMPRKEF NKIFELYDQD GNGYMDENEL DALLKDLCEK NQKVLDIKNI ATYKKTIMAL
     SDGGKLYRTE LALVLCADEN
//
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