CATR_DUNSA
ID CATR_DUNSA Reviewed; 169 AA.
AC P54213;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Caltractin;
DE AltName: Full=Centrin;
OS Dunaliella salina (Green alga) (Protococcus salinus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX NCBI_TaxID=3046;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ko J.-H., Lee S.-H.;
RT "Nucleotide sequence of a cDNA encoding a caltractin-like protein from
RT Dunaliella salina.";
RL (er) Plant Gene Register PGR96-062(1996).
CC -!- FUNCTION: This calcium-binding protein is found in the basal body
CC complexes (the functional homolog of the centrosome in animal cell). In
CC mitotic cells it is specifically associated with the poles of the
CC mitotic spindles at the sites of the duplicated basal body complexes
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; U53812; AAB67855.1; -; mRNA.
DR PIR; T10724; T10724.
DR AlphaFoldDB; P54213; -.
DR SMR; P54213; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 2: Evidence at transcript level;
KW Calcium; Cell cycle; Cell division; Metal-binding; Mitosis; Repeat.
FT CHAIN 1..169
FT /note="Caltractin"
FT /id="PRO_0000073572"
FT DOMAIN 25..60
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 61..96
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..169
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 169 AA; 19397 MW; 84033DFED13F6F4D CRC64;
MSYRKTVVSA RRDQKKGRVG GLTEEQKQEI REAFDLFDTD GSGTIDAKEL KVAMRALGFE
PKKEEIKKMI ADIDKAGSGT IDFEEFLQMM TSKMGERDSR EEIIKAFKLF DDDNTGFITL
KNLKRVAKEL GENLTDEELQ EMTDEADRNG DGQIDEDEFY RIMKKTSLF