CATR2_PARTE
ID CATR2_PARTE Reviewed; 182 AA.
AC Q27179; Q3SEK1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Caltractin ICL1b;
DE AltName: Full=Centrin-2;
GN Name=Icl1b; ORFNames=GSPATT00033005001;
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Stock d4-2;
RA Klotz C.;
RT "Paramecium tetraurelia centrin-related protein genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2;
RX PubMed=17086204; DOI=10.1038/nature05230;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-182.
RC STRAIN=Stock d4-2;
RX PubMed=8665928; DOI=10.1111/j.1432-1033.1996.0121q.x;
RA Madeddu L., Klotz C., Le Caer J.-P., Beisson J.;
RT "Characterization of centrin genes in Paramecium.";
RL Eur. J. Biochem. 238:121-128(1996).
CC -!- FUNCTION: Plays a fundamental role in microtubule organizing center
CC structure and function. Component of the infraciliary lattice (ICL) and
CC the ciliary basal bodies.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=ICL, innermost
CC fibrous network of the cortical cytoskeleton.
CC -!- MISCELLANEOUS: Binds two moles of calcium per mole of protein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; CR932083; CAI38923.1; -; Genomic_DNA.
DR EMBL; CT868024; CAK63152.1; -; Genomic_DNA.
DR EMBL; U35397; AAC47158.1; -; Genomic_DNA.
DR EMBL; U76539; AAB18752.1; -; Genomic_DNA.
DR PIR; S71318; S71318.
DR RefSeq; XP_001430550.1; XM_001430513.1.
DR AlphaFoldDB; Q27179; -.
DR SMR; Q27179; -.
DR STRING; 5888.CAK63152; -.
DR EnsemblProtists; CAK63152; CAK63152; GSPATT00033005001.
DR GeneID; 5016334; -.
DR KEGG; ptm:GSPATT00033005001; -.
DR eggNOG; KOG0028; Eukaryota.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; Q27179; -.
DR OMA; ISCTEIK; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR029527; CETN1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23050:SF218; PTHR23050:SF218; 1.
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 3: Inferred from homology;
KW Calcium; Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..182
FT /note="Caltractin ICL1b"
FT /id="PRO_0000073568"
FT DOMAIN 38..73
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 74..109
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 111..146
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 147..182
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 2
FT /note="S -> A (in Ref. 3; AAC47158/AAB18752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20485 MW; B328B7FF08EF4B85 CRC64;
MSRRGQQPPP QQQQAPPQKN QAGKFNPAEF VKPGLTEEEV LEIKEAFDLF DTDGTQSIDP
KELKAAMTSL GFEAKNQTIY QMISDLDTDG SGQIDFAEFL KLMTARISER DSKADIQKVF
NLFDSERAGV ITLKDLRKVA KELGETMDDS ELQEMIDRAD SDGDAQVTFE DFYNIMTKKT
FA
