CATR_NAEGR
ID CATR_NAEGR Reviewed; 172 AA.
AC P53441;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Caltractin;
DE AltName: Full=Centrin;
GN Name=CTN;
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 30223 / NEG;
RX PubMed=8801035;
RX DOI=10.1002/(sici)1097-0169(1996)33:4<298::aid-cm6>3.0.co;2-5;
RA Levy Y.Y., Lai E.Y., Remillard S.P., Heintzelman M.B., Fulton C.;
RT "Centrin is a conserved protein that forms diverse associations with
RT centrioles and MTOCs in Naegleria and other organisms.";
RL Cell Motil. Cytoskeleton 33:298-323(1996).
CC -!- FUNCTION: Plays a fundamental role in microtubule-organizing center
CC structure and function.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Note=Centrosome of interphase and mitotic cells.
CC -!- MISCELLANEOUS: Binds two moles of calcium per mole of protein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U21725; AAA75032.1; -; mRNA.
DR AlphaFoldDB; P53441; -.
DR SMR; P53441; -.
DR STRING; 5762.XP_002671077.1; -.
DR PRIDE; P53441; -.
DR KEGG; ngr:NAEGRDRAFT_56351; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_56351; -.
DR eggNOG; KOG0028; Eukaryota.
DR OMA; YDEFEYM; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 2: Evidence at transcript level;
KW Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Metal-binding;
KW Mitosis; Repeat.
FT CHAIN 1..172
FT /note="Caltractin"
FT /id="PRO_0000073566"
FT DOMAIN 29..64
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 65..99
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 101..136
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 137..172
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 172 AA; 19608 MW; D410230AD74673C2 CRC64;
MQKYGSKKIG ATSATSSNKQ KVQIELTDEQ RQEIKEAFDL FDMDGSGKID AKELKVAMRA
LGFEPKKEEI KKMISGIDNG SGKIDFNDFL QLMTAKMSEK DSHAEIMKAF RLFDEDDSGF
ITFANLKRVA KDLGENMTDE ELREMIEEAD RSNQGQISKE DFLRIMKKTN LF
