CETN3_MOUSE
ID CETN3_MOUSE Reviewed; 167 AA.
AC O35648;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Centrin-3;
GN Name=Cetn3; Synonyms=Cen3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=9256449; DOI=10.1073/pnas.94.17.9141;
RA Middendorp S., Paoletti A., Schiebel E., Bornens M.;
RT "Identification of a new mammalian centrin gene, more closely related to
RT Saccharomyces cerevisiae CDC31 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9141-9146(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a fundamental role in microtubule-organizing center
CC structure and function.
CC -!- FUNCTION: As a component of the TREX-2 complex, involved in the export
CC of mRNAs to the cytoplasm through the nuclear pores.
CC {ECO:0000250|UniProtKB:O15182}.
CC -!- SUBUNIT: Monomer (By similarity). Component of the TREX-2 complex
CC (transcription and export complex 2), composed of at least ENY2, GANP,
CC PCID2, SEM1, and either centrin CETN2 or CETN3. {ECO:0000250,
CC ECO:0000250|UniProtKB:O15182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:O15182}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O15182}. Nucleus envelope
CC {ECO:0000250|UniProtKB:O15182}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:O15182}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O15182}. Note=Centrosome of interphase and
CC mitotic cells. Localizes to centriole distal lumen (By similarity).
CC Localization at the nuclear pore complex requires NUP153 and TPR (By
CC similarity). {ECO:0000250|UniProtKB:O15182}.
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; Y12474; CAA73078.1; -; mRNA.
DR EMBL; BC002162; AAH02162.1; -; mRNA.
DR EMBL; BC054097; AAH54097.1; -; mRNA.
DR CCDS; CCDS26663.1; -.
DR RefSeq; NP_031710.1; NM_007684.3.
DR AlphaFoldDB; O35648; -.
DR SMR; O35648; -.
DR STRING; 10090.ENSMUSP00000022009; -.
DR iPTMnet; O35648; -.
DR PhosphoSitePlus; O35648; -.
DR EPD; O35648; -.
DR PaxDb; O35648; -.
DR PeptideAtlas; O35648; -.
DR PRIDE; O35648; -.
DR ProteomicsDB; 280078; -.
DR Antibodypedia; 24818; 191 antibodies from 24 providers.
DR DNASU; 12626; -.
DR Ensembl; ENSMUST00000022009; ENSMUSP00000022009; ENSMUSG00000021537.
DR GeneID; 12626; -.
DR KEGG; mmu:12626; -.
DR UCSC; uc007rid.1; mouse.
DR CTD; 1070; -.
DR MGI; MGI:1097706; Cetn3.
DR VEuPathDB; HostDB:ENSMUSG00000021537; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000157995; -.
DR HOGENOM; CLU_061288_18_1_1; -.
DR InParanoid; O35648; -.
DR OMA; IDAHEMK; -.
DR OrthoDB; 1340191at2759; -.
DR PhylomeDB; O35648; -.
DR TreeFam; TF101141; -.
DR BioGRID-ORCS; 12626; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Cetn3; mouse.
DR PRO; PR:O35648; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O35648; protein.
DR Bgee; ENSMUSG00000021537; Expressed in cortical plate and 278 other tissues.
DR ExpressionAtlas; O35648; baseline and differential.
DR Genevisible; O35648; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0070390; C:transcription export complex 2; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 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 1: Evidence at protein level;
KW Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Metal-binding;
KW Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..167
FT /note="Centrin-3"
FT /id="PRO_0000073564"
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..167
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 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"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15182"
SQ SEQUENCE 167 AA; 19519 MW; 562FF752E56C2E9D CRC64;
MSLALRGELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDQAIDYHEL KVAMRALGFD
VKKADVLKIL KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL
RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI AIMTGDI
