CATR_CHLRE
ID CATR_CHLRE Reviewed; 169 AA.
AC P05434;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Caltractin;
DE AltName: Full=20 kDa calcium-binding protein;
DE AltName: Full=Centrin;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2839516; DOI=10.1083/jcb.107.1.133;
RA Huang B., Mengersen A., Lee V.D.;
RT "Molecular cloning of cDNA for caltractin, a basal body-associated Ca2+-
RT binding protein: homology in its protein sequence with calmodulin and the
RT yeast CDC31 gene product.";
RL J. Cell Biol. 107:133-140(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1920403; DOI=10.1016/0022-2836(91)80213-e;
RA Lee V.D., Stapleton M., Huang B.;
RT "Genomic structure of Chlamydomonas caltractin. Evidence for intron
RT insertion suggests a probable genealogy for the EF-hand superfamily of
RT proteins.";
RL J. Mol. Biol. 221:175-191(1991).
RN [3]
RP PROTEIN SEQUENCE OF 70-77 AND 129-159.
RX PubMed=3292538; DOI=10.1083/jcb.107.1.121;
RA Huang B., Watterson D.M., Lee V.D., Schibler M.J.;
RT "Purification and characterization of a basal body-associated Ca2+-binding
RT protein.";
RL J. Cell Biol. 107:121-131(1988).
RN [4]
RP STRUCTURE BY NMR OF 95-169.
RX PubMed=12842464; DOI=10.1016/s0022-2836(03)00619-3;
RA Hu H., Chazin W.J.;
RT "Unique features in the C-terminal domain provide caltractin with target
RT specificity.";
RL J. Mol. Biol. 330:473-484(2003).
RN [5]
RP STRUCTURE BY NMR OF 1-94.
RX PubMed=16317001; DOI=10.1074/jbc.m509886200;
RA Sheehan J.H., Bunick C.G., Hu H., Fagan P.A., Meyn S.M., Chazin W.J.;
RT "Structure of the N-terminal calcium sensor domain of centrin reveals the
RT biochemical basis for domain-specific function.";
RL J. Biol. Chem. 281:2876-2881(2006).
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 -!- INTERACTION:
CC P05434; O12369; Xeno; NbExp=2; IntAct=EBI-983707, EBI-983753;
CC -!- MISCELLANEOUS: Binds four moles of calcium per mole of protein.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; X12634; CAA31163.1; -; mRNA.
DR EMBL; X57973; CAA41039.1; -; Genomic_DNA.
DR PIR; A28216; BCKM.
DR RefSeq; XP_001699499.1; XM_001699447.1.
DR PDB; 1OQP; NMR; -; A=95-169.
DR PDB; 2AMI; NMR; -; A=1-94.
DR PDB; 3QRX; X-ray; 2.20 A; A=1-169.
DR PDBsum; 1OQP; -.
DR PDBsum; 2AMI; -.
DR PDBsum; 3QRX; -.
DR AlphaFoldDB; P05434; -.
DR SMR; P05434; -.
DR IntAct; P05434; 1.
DR STRING; 3055.EDO98562; -.
DR PRIDE; P05434; -.
DR ProMEX; P05434; -.
DR EnsemblPlants; PNW76718; PNW76718; CHLRE_11g468450v5.
DR GeneID; 5725094; -.
DR Gramene; PNW76718; PNW76718; CHLRE_11g468450v5.
DR KEGG; cre:CHLRE_11g468450v5; -.
DR eggNOG; KOG0028; Eukaryota.
DR HOGENOM; CLU_061288_18_2_1; -.
DR OMA; YDEFEYM; -.
DR OrthoDB; 1382571at2759; -.
DR EvolutionaryTrace; P05434; -.
DR GO; GO:0036156; C:inner dynein arm; IDA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045504; F:dynein heavy chain binding; IPI:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR DisProt; DP01659; -.
DR IDEAL; IID50065; -.
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; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell cycle; Cell division;
KW Direct protein sequencing; Metal-binding; Mitosis; Repeat.
FT CHAIN 1..169
FT /note="Caltractin"
FT /id="PRO_0000073571"
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 9..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 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:3QRX"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3QRX"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3QRX"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3QRX"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3QRX"
FT HELIX 83..110
FT /evidence="ECO:0007829|PDB:3QRX"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3QRX"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:3QRX"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:3QRX"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3QRX"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:3QRX"
SQ SEQUENCE 169 AA; 19459 MW; 731D171794EAD983 CRC64;
MSYKAKTVVS ARRDQKKGRV GLTEEQKQEI REAFDLFDTD GSGTIDAKEL KVAMRALGFE
PKKEEIKKMI SEIDKDGSGT IDFEEFLTMM TAKMGERDSR EEILKAFRLF DDDNSGTITI
KDLRRVAKEL GENLTEEELQ EMIAEADRND DNEIDEDEFI RIMKKTSLF
