ID   CETN3_HUMAN             Reviewed;         167 AA.
AC   O15182; Q53YD2; Q9BS23;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Centrin-3;
GN   Name=CETN3; Synonyms=CEN3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND VARIANT LEU-10.
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].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Testis;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [6]
RP   INTERACTION WITH TREX-2 COMPLEX, AND FUNCTION.
RX   PubMed=22307388; DOI=10.1093/nar/gks059;
RA   Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.;
RT   "Functional and structural characterization of the mammalian TREX-2 complex
RT   that links transcription with nuclear messenger RNA export.";
RL   Nucleic Acids Res. 40:4562-4573(2012).
RN   [7]
RP   FUNCTION, IDENTIFICATION IN THE TREX-2 COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=23591820; DOI=10.1242/jcs.118000;
RA   Umlauf D., Bonnet J., Waharte F., Fournier M., Stierle M., Fischer B.,
RA   Brino L., Devys D., Tora L.;
RT   "The human TREX-2 complex is stably associated with the nuclear pore
RT   basket.";
RL   J. Cell Sci. 126:2656-2667(2013).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=26337392; DOI=10.1091/mbc.e15-04-0235;
RA   Van de Mark D., Kong D., Loncarek J., Stearns T.;
RT   "MDM1 is a microtubule-binding protein that negatively regulates centriole
RT   duplication.";
RL   Mol. Biol. Cell 26:3788-3802(2015).
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:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}.
CC   -!- SUBUNIT: Monomer (By similarity). Component of the nuclear pore complex
CC       (NPC)-associated TREX-2 complex (transcription and export complex 2),
CC       composed of at least GANP, 2 copies of ENY2, PCID2, SEM1/DSS1, and
CC       either centrin CETN2 or centrin CETN3. The TREX-2 complex also
CC       associates with ALYREF/ALY and with the nucleoporin NUP153
CC       (PubMed:22307388, PubMed:23591820). {ECO:0000250,
CC       ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820}.
CC   -!- INTERACTION:
CC       O15182; O95994: AGR2; NbExp=3; IntAct=EBI-712959, EBI-712648;
CC       O15182; P17540: CKMT2; NbExp=3; IntAct=EBI-712959, EBI-712973;
CC       O15182; P13473-2: LAMP2; NbExp=3; IntAct=EBI-712959, EBI-21591415;
CC       O15182; O43679: LDB2; NbExp=3; IntAct=EBI-712959, EBI-2865580;
CC       O15182; Q8NA72: POC5; NbExp=8; IntAct=EBI-712959, EBI-2561090;
CC       O15182; Q8NA72-3: POC5; NbExp=8; IntAct=EBI-712959, EBI-11751537;
CC       O15182; Q15293: RCN1; NbExp=5; IntAct=EBI-712959, EBI-948278;
CC       O15182; O00141: SGK1; NbExp=3; IntAct=EBI-712959, EBI-1042854;
CC       O15182; Q2NKQ1-4: SGSM1; NbExp=6; IntAct=EBI-712959, EBI-10182463;
CC       O15182; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-712959, EBI-2623095;
CC       O15182; P19237: TNNI1; NbExp=3; IntAct=EBI-712959, EBI-746692;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:14654843,
CC       ECO:0000269|PubMed:9256449}. Nucleus, nucleolus
CC       {ECO:0000303|PubMed:22307388}. Nucleus envelope
CC       {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex
CC       {ECO:0000269|PubMed:23591820}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820,
CC       ECO:0000269|PubMed:26337392}. Note=Centrosome of interphase and mitotic
CC       cells (PubMed:9256449). Localizes to centriole distal lumen
CC       (PubMed:26337392). Localization at the nuclear pore complex requires
CC       NUP153 and TPR (PubMed:23591820). {ECO:0000269|PubMed:23591820,
CC       ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9256449}.
CC   -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR   EMBL; Y12473; CAA73077.1; -; mRNA.
DR   EMBL; BT006688; AAP35334.1; -; mRNA.
DR   EMBL; AC093510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005383; AAH05383.1; -; mRNA.
DR   EMBL; BC093793; AAH93793.1; -; mRNA.
DR   EMBL; BC112040; AAI12041.1; -; mRNA.
DR   CCDS; CCDS4066.1; -.
DR   RefSeq; NP_001284697.1; NM_001297768.1.
DR   RefSeq; NP_004356.2; NM_004365.3.
DR   AlphaFoldDB; O15182; -.
DR   SMR; O15182; -.
DR   BioGRID; 107497; 77.
DR   ComplexPortal; CPX-7281; TREX-2 transcription-export complex, CETN3 variant.
DR   IntAct; O15182; 40.
DR   MINT; O15182; -.
DR   STRING; 9606.ENSP00000428259; -.
DR   iPTMnet; O15182; -.
DR   MetOSite; O15182; -.
DR   PhosphoSitePlus; O15182; -.
DR   BioMuta; CETN3; -.
DR   EPD; O15182; -.
DR   jPOST; O15182; -.
DR   MassIVE; O15182; -.
DR   MaxQB; O15182; -.
DR   PeptideAtlas; O15182; -.
DR   ProteomicsDB; 48497; -.
DR   Pumba; O15182; -.
DR   Antibodypedia; 24818; 239 antibodies from 24 providers.
DR   DNASU; 1070; -.
DR   Ensembl; ENST00000283122.8; ENSP00000283122.3; ENSG00000153140.9.
DR   GeneID; 1070; -.
DR   KEGG; hsa:1070; -.
DR   MANE-Select; ENST00000283122.8; ENSP00000283122.3; NM_004365.4; NP_004356.2.
DR   UCSC; uc003kjo.4; human.
DR   AGR; HGNC:1868; -.
DR   CTD; 1070; -.
DR   DisGeNET; 1070; -.
DR   GeneCards; CETN3; -.
DR   HGNC; HGNC:1868; CETN3.
DR   HPA; ENSG00000153140; Tissue enhanced (testis).
DR   MIM; 602907; gene.
DR   neXtProt; NX_O15182; -.
DR   OpenTargets; ENSG00000153140; -.
DR   PharmGKB; PA26421; -.
DR   VEuPathDB; HostDB:ENSG00000153140; -.
DR   GeneTree; ENSGT00940000157995; -.
DR   InParanoid; O15182; -.
DR   OMA; DYHEFKV; -.
DR   OrthoDB; 67444at2759; -.
DR   PhylomeDB; O15182; -.
DR   TreeFam; TF101141; -.
DR   PathwayCommons; O15182; -.
DR   SignaLink; O15182; -.
DR   SIGNOR; O15182; -.
DR   BioGRID-ORCS; 1070; 27 hits in 1122 CRISPR screens.
DR   ChiTaRS; CETN3; human.
DR   GeneWiki; CETN3; -.
DR   GenomeRNAi; 1070; -.
DR   Pharos; O15182; Tbio.
DR   PRO; PR:O15182; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; O15182; Protein.
DR   Bgee; ENSG00000153140; Expressed in oocyte and 213 other cell types or tissues.
DR   ExpressionAtlas; O15182; baseline and differential.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
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; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR   GO; GO:0070390; C:transcription export complex 2; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:Ensembl.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007098; P:centrosome cycle; TAS:ProtInc.
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   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1.
DR   PANTHER; PTHR23050:SF325; CENTRIN-3; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   Genevisible; O15182; HS.
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_0000073563"
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         147
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         149
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         151
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         10
FT                   /note="V -> L (in dbSNP:rs4873)"
FT                   /evidence="ECO:0000269|PubMed:9256449"
FT                   /id="VAR_030846"
SQ   SEQUENCE   167 AA;  19550 MW;  EF67724B2D6C2680 CRC64;
     MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD
     VKKADVLKIL KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL
     RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI AIMTGDI
//