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CALGL_BOTIN
ID   CALGL_BOTIN             Reviewed;         156 AA.
AC   Q8AY75;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Calglandulin;
OS   Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom gland;
RX   PubMed=12758151; DOI=10.1016/s1570-9639(03)00111-0;
RA   Junqueira-de-Azevedo I.L.M., Pertinhez T., Spisni A., Carreno F.R.,
RA   Farah C.S., Ho P.L.;
RT   "Cloning and expression of calglandulin, a new EF-hand protein from the
RT   venom glands of Bothrops insularis snake in E. coli.";
RL   Biochim. Biophys. Acta 1648:90-98(2003).
CC   -!- FUNCTION: May be involved in the cellular control mechanism of the
CC       secretion of toxins from the gland into the venom.
CC       {ECO:0000269|PubMed:12758151}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Not found in venom.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12758151}.
CC   -!- SIMILARITY: Belongs to the calmodulin family. Calglandulin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF545856; AAN37910.1; -; mRNA.
DR   AlphaFoldDB; Q8AY75; -.
DR   SMR; Q8AY75; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   2: Evidence at transcript level;
KW   Calcium; Cytoplasm; Metal-binding; Repeat.
FT   CHAIN           1..156
FT                   /note="Calglandulin"
FT                   /id="PRO_0000073549"
FT   DOMAIN          8..43
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          44..79
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          82..117
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          118..153
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         131
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         135
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   156 AA;  17716 MW;  7F152273172A4165 CRC64;
     MAATLTPEQI TEYKGIFEMF DEEGNGLVKT DDLESLMSLV GINPTKRDLA NMAKDVDKDK
     KGTFNCDGFL ALMGIYHEKS KNQDEELRAA FKVFDKEHKG YIEWDTLKYV LMNAGEPLNE
     QEAELMMKEA DKDGDGTIDY EEFVAMMTGE SFKLTQ
 
 
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