CETN2_MOUSE
ID CETN2_MOUSE Reviewed; 172 AA.
AC Q9R1K9; B1AUQ6; B1AUQ8; Q3UBB4; Q9CWM0;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Centrin-2;
DE AltName: Full=Caltractin isoform 1;
GN Name=Cetn2; Synonyms=Calt;
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 [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Ola;
RX PubMed=11250075; DOI=10.1016/s0378-1119(01)00342-0;
RA Hart P.E., Poynter G.M., Whitehead C.M., Orth J.D., Glantz J.N.,
RA Busby R.C., Barrett S.L., Salisbury J.L.;
RT "Characterization of the X-linked murine centrin Cetn2 gene.";
RL Gene 264:205-213(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=10854409; DOI=10.1101/gr.10.6.758;
RA Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M.,
RA Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D.,
RA Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G.,
RA Greystrong J.S., Clarke D., Kimberley C., Goerdes M., Blechschmidt K.,
RA Rump A., Hinzmann B., Mundy C.R., Miller W., Poustka A., Herman G.E.,
RA Rhodes M., Denny P., Rosenthal A., Brown S.D.M.;
RT "Comparative genome sequence analysis of the Bpa/Str region in mouse and
RT man.";
RL Genome Res. 10:758-775(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Corpora quadrigemina, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Spleen;
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. Required for centriole duplication and correct
CC spindle formation. Has a role in regulating cytokinesis and genome
CC stability via cooperation with CALM1 and CCP110 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Involved in global genome nucleotide excision repair (GG-NER)
CC by acting as component of the XPC complex. Cooperatively with Rad23b
CC appears to stabilize Xpc. In vitro, stimulates DNA binding of the
CC Xpc:Rad23b dimer (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The XPC complex is proposed to represent the first factor
CC bound at the sites of DNA damage and together with other core
CC recognition factors, Xpa, RPA and the TFIIH complex, is part of the
CC pre-incision (or initial recognition) complex. The XPC complex
CC recognizes a wide spectrum of damaged DNA characterized by distortions
CC of the DNA helix such as single-stranded loops, mismatched bubbles or
CC single-stranded overhangs. The orientation of XPC complex binding
CC appears to be crucial for inducing a productive NER. XPC complex is
CC proposed to recognize and to interact with unpaired bases on the
CC undamaged DNA strand which is followed by recruitment of the TFIIH
CC complex and subsequent scanning for lesions in the opposite strand in a
CC 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers
CC (CPDs) which are formed upon UV-induced DNA damage esacpe detection by
CC the XPC complex due to a low degree of structural perurbation. Instead
CC they are detected by the UV-DDB complex which in turn recruits and
CC cooperates with the XPC complex in the respective DNA repair (By
CC similarity). {ECO:0000250}.
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:P41208}.
CC -!- SUBUNIT: Monomer. Homooligomer. Interacts with CCP110, SFI1. Component
CC of the XPC complex composed of XPC, RAD23B and CETN2 (By similarity).
CC Component of the nuclear pore complex (NPC)-associated TREX-2 complex
CC (transcription and export complex 2), composed of at least GANP, 2
CC copies of ENY2, PCID2, SEM1/DSS1, and either centrin CETN2 or centrin
CC CETN3. The TREX-2 complex also associates with ALYREF/ALY and with the
CC nucleoporin NUP153 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P41208}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P41208}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:11250075}. Nucleus {ECO:0000250|UniProtKB:P41208}.
CC Nucleus envelope {ECO:0000250|UniProtKB:P41208}. Nucleus, nuclear pore
CC complex {ECO:0000250|UniProtKB:P41208}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues tested,
CC with strongest expression in brain, spleen, kidney, small intestine and
CC ovary. Also expressed in the NIH 3T3 fibroblast cell line and
CC peripheral blood lymphocytes. {ECO:0000269|PubMed:11250075}.
CC -!- MISCELLANEOUS: Binds two moles of calcium per mole of protein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM20357.1; Type=Erroneous gene model prediction; Evidence={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; AF080592; AAD46391.1; -; Genomic_DNA.
DR EMBL; AL021127; CAB88169.1; -; Genomic_DNA.
DR EMBL; AK004081; BAB23161.1; -; mRNA.
DR EMBL; AK010541; BAB27017.1; -; mRNA.
DR EMBL; AK140156; BAE24259.1; -; mRNA.
DR EMBL; AK151033; BAE30050.1; -; mRNA.
DR EMBL; AL671908; CAM20357.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL671908; CAM20359.1; -; Genomic_DNA.
DR EMBL; CH466624; EDL26558.1; -; Genomic_DNA.
DR EMBL; BC013545; AAH13545.1; -; mRNA.
DR CCDS; CCDS41003.1; -.
DR RefSeq; NP_062278.2; NM_019405.6.
DR AlphaFoldDB; Q9R1K9; -.
DR SMR; Q9R1K9; -.
DR BioGRID; 204930; 33.
DR IntAct; Q9R1K9; 32.
DR MINT; Q9R1K9; -.
DR STRING; 10090.ENSMUSP00000110198; -.
DR iPTMnet; Q9R1K9; -.
DR PhosphoSitePlus; Q9R1K9; -.
DR EPD; Q9R1K9; -.
DR jPOST; Q9R1K9; -.
DR MaxQB; Q9R1K9; -.
DR PaxDb; Q9R1K9; -.
DR PeptideAtlas; Q9R1K9; -.
DR PRIDE; Q9R1K9; -.
DR ProteomicsDB; 281199; -.
DR Antibodypedia; 30770; 199 antibodies from 28 providers.
DR DNASU; 26370; -.
DR Ensembl; ENSMUST00000114551; ENSMUSP00000110198; ENSMUSG00000031347.
DR GeneID; 26370; -.
DR KEGG; mmu:26370; -.
DR UCSC; uc009tkt.1; mouse.
DR CTD; 1069; -.
DR MGI; MGI:1347085; Cetn2.
DR VEuPathDB; HostDB:ENSMUSG00000031347; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000155935; -.
DR InParanoid; Q9R1K9; -.
DR OMA; YDEFEYM; -.
DR OrthoDB; 1382571at2759; -.
DR PhylomeDB; Q9R1K9; -.
DR TreeFam; TF101141; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 26370; 3 hits in 109 CRISPR screens.
DR ChiTaRS; Cetn2; mouse.
DR PRO; PR:Q9R1K9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R1K9; protein.
DR Bgee; ENSMUSG00000031347; Expressed in choroid plexus epithelium and 261 other tissues.
DR ExpressionAtlas; Q9R1K9; baseline and differential.
DR Genevisible; Q9R1K9; MM.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0070390; C:transcription export complex 2; ISS:UniProtKB.
DR GO; GO:0071942; C:XPC complex; 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:0032795; F:heterotrimeric G-protein binding; IDA:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; ISO:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEP:BHF-UCL.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR037629; Centrin_2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR23050:SF305; PTHR23050:SF305; 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 1: Evidence at protein level;
KW Acetylation; Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; Isopeptide bond; Metal-binding; Mitosis;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT CHAIN 2..172
FT /note="Centrin-2"
FT /id="PRO_0000073562"
FT DOMAIN 28..63
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 64..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..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..25
FT /note="Required for self-assembly"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41208"
FT CONFLICT 34
FT /note="R -> P (in Ref. 3; BAB27017)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="I -> N (in Ref. 3; BAB27017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19797 MW; 75311C8386861567 CRC64;
MASNFKKTTM ASSAQRKRMS PKPELTEDQK QEIREAFDLF DADGTGTIDI KELKVAMRAL
GFEPKKEEIK KMISEIDKEG TGKMNFSDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK
ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVNEQ EFLRIMKKTS LY
