CETN1_MOUSE
ID CETN1_MOUSE Reviewed; 172 AA.
AC P41209; Q3V119; Q9D9G9; Q9DAL6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Centrin-1 {ECO:0000305};
DE AltName: Full=Caltractin;
GN Name=Cetn1 {ECO:0000312|MGI:MGI:1347086}; 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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=8218402; DOI=10.1016/0167-4781(93)90048-i;
RA Ogawa K., Shimizu T.;
RT "cDNA sequence for mouse caltractin.";
RL Biochim. Biophys. Acta 1216:126-128(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=129/Ola; TISSUE=Testis;
RX PubMed=10486202; DOI=10.1006/geno.1999.5880;
RA Hart P.E., Glantz J.N., Orth J.D., Poynter G.M., Salisbury J.L.;
RT "Testis-specific murine centrin, Cetn1: genomic characterization and
RT evidence for retroposition of a gene encoding a centrosome protein.";
RL Genomics 60:111-120(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA].
RC TISSUE=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 [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [6]
RP INTERACTION WITH PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [7]
RP FUNCTION.
RX PubMed=27530713; DOI=10.1038/srep31666;
RA Oji A., Noda T., Fujihara Y., Miyata H., Kim Y.J., Muto M., Nozawa K.,
RA Matsumura T., Isotani A., Ikawa M.;
RT "CRISPR/Cas9 mediated genome editing in ES cells and its application for
RT chimeric analysis in mice.";
RL Sci. Rep. 6:31666-31666(2016).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30120214; DOI=10.1136/jmedgenet-2018-105364;
RA de Bruijn S.E., Verbakel S.K., de Vrieze E., Kremer H., Cremers F.P.M.,
RA Hoyng C.B., van den Born L.I., Roosing S.;
RT "Homozygous variants in KIAA1549, encoding a ciliary protein, are
RT associated with autosomal recessive retinitis pigmentosa.";
RL J. Med. Genet. 55:705-712(2018).
CC -!- FUNCTION: Plays a fundamental role in microtubule-organizing center
CC structure and function (By similarity). Plays a role in sperm cilia
CC formation (PubMed:27530713). {ECO:0000250|UniProtKB:Q12798,
CC ECO:0000269|PubMed:27530713}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with PIFO
CC (PubMed:20643351). {ECO:0000250, ECO:0000269|PubMed:20643351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Cell projection, cilium
CC {ECO:0000269|PubMed:30120214}. Note=Centrosome of interphase and
CC mitotic cells. In the retinal photoreceptor cells, localizes at the
CC connecting cilium, a thin bridge linking the cell body and the light-
CC sensing outer segment (PubMed:30120214). {ECO:0000269|PubMed:30120214}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Localizes to the caudal
CC portion of spermatozoa in seminiferous tubule and epididymis
CC (PubMed:10486202). Expressed in retina photoreceptor cells (at protein
CC level) (PubMed:30120214). {ECO:0000269|PubMed:10486202,
CC ECO:0000269|PubMed:30120214}.
CC -!- DEVELOPMENTAL STAGE: First expressed at 14 days postpartum (dpp).
CC Levels increase dramatically between 14 dpp and 17 dpp.
CC {ECO:0000269|PubMed:10486202}.
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; D16301; BAA03806.1; -; mRNA.
DR EMBL; AF080591; AAD46390.1; -; Genomic_DNA.
DR EMBL; AK005736; BAB24213.1; -; mRNA.
DR EMBL; AK005743; BAB24217.1; -; mRNA.
DR EMBL; AK005837; BAB24266.1; -; mRNA.
DR EMBL; AK006940; BAB24798.1; -; mRNA.
DR EMBL; AK015808; BAB29985.1; -; mRNA.
DR EMBL; AK076986; BAC36550.1; -; mRNA.
DR EMBL; AK132753; BAE21334.1; -; mRNA.
DR EMBL; BC048488; AAH48488.1; -; mRNA.
DR EMBL; BC061155; AAH61155.1; -; mRNA.
DR CCDS; CCDS37731.1; -.
DR PIR; S38531; S38531.
DR RefSeq; NP_031619.3; NM_007593.5.
DR PDB; 5D43; X-ray; 2.82 A; A/B=1-172.
DR PDBsum; 5D43; -.
DR AlphaFoldDB; P41209; -.
DR SMR; P41209; -.
DR STRING; 10090.ENSMUSP00000057392; -.
DR iPTMnet; P41209; -.
DR PhosphoSitePlus; P41209; -.
DR MaxQB; P41209; -.
DR PaxDb; P41209; -.
DR PeptideAtlas; P41209; -.
DR PRIDE; P41209; -.
DR ProteomicsDB; 280009; -.
DR Antibodypedia; 5901; 282 antibodies from 28 providers.
DR DNASU; 26369; -.
DR Ensembl; ENSMUST00000062769; ENSMUSP00000057392; ENSMUSG00000050996.
DR Ensembl; ENSMUST00000234003; ENSMUSP00000157153; ENSMUSG00000050996.
DR Ensembl; ENSMUST00000234590; ENSMUSP00000157126; ENSMUSG00000050996.
DR GeneID; 26369; -.
DR KEGG; mmu:26369; -.
DR UCSC; uc012aze.1; mouse.
DR CTD; 1068; -.
DR MGI; MGI:1347086; Cetn1.
DR VEuPathDB; HostDB:ENSMUSG00000050996; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000157209; -.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; P41209; -.
DR OMA; GIQKIFA; -.
DR OrthoDB; 1382571at2759; -.
DR PhylomeDB; P41209; -.
DR TreeFam; TF101141; -.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR BioGRID-ORCS; 26369; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cetn1; mouse.
DR PRO; PR:P41209; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P41209; protein.
DR Bgee; ENSMUSG00000050996; Expressed in spermatid and 23 other tissues.
DR Genevisible; P41209; MM.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005815; C:microtubule organizing center; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
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:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0007099; P:centriole replication; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR CDD; cd00051; EFh; 2.
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 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell cycle; Cell division; Cell projection;
KW Cytoplasm; Cytoskeleton; Metal-binding; Mitosis; Reference proteome;
KW Repeat.
FT CHAIN 1..172
FT /note="Centrin-1"
FT /id="PRO_0000073560"
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..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
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 CONFLICT 95
FT /note="Q -> R (in Ref. 3; BAB24213)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="M -> K (in Ref. 3; BAB24798)"
FT /evidence="ECO:0000305"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:5D43"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5D43"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:5D43"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:5D43"
FT HELIX 86..113
FT /evidence="ECO:0007829|PDB:5D43"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:5D43"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:5D43"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:5D43"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:5D43"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:5D43"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5D43"
SQ SEQUENCE 172 AA; 19696 MW; 45ABF106F58E4B60 CRC64;
MASTFRKSNV ASTSYKRKVG PKPELTEDQK QEVREAFDLF DSDGSGTIDV KELKVAMRAL
GFEPRKEEMK KMISEVDKEA TGKISFNDFL AVMTQKMAEK DTKEEILKAF RLFDDDETGK
ISFKNLKRVA NELGESLTDE ELQEMIDEAD RDGDGEVNEE EFLKIMKKTN LY
