CETN4_MOUSE
ID CETN4_MOUSE Reviewed; 168 AA.
AC Q8K4K1; E9PYP9; E9Q074; J3KMS3; Q3TLH1; Q5SUE1; Q8BIC4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Centrin-4;
DE AltName: Full=Centrin4 {ECO:0000303|PubMed:12802058};
GN Name=Cetn4 {ECO:0000312|EMBL:AAH60991.1,
GN ECO:0000312|Ensembl:ENSMUSP00000100020, ECO:0000312|MGI:MGI:2677454};
GN Synonyms=Cen4 {ECO:0000303|PubMed:15347651};
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] {ECO:0000305, ECO:0000312|EMBL:AAM75880.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CALCIUM-BINDING,
RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 3), TISSUE SPECIFICITY,
RP AND MISCELLANEOUS.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM75880.1};
RX PubMed=12802058; DOI=10.1091/mbc.e02-11-0709;
RA Gavet O., Alvarez C., Gaspar P., Bornens M.;
RT "Centrin4p, a novel mammalian centrin specifically expressed in ciliated
RT cells.";
RL Mol. Biol. Cell 14:1818-1834(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC41074.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Mammary gland {ECO:0000312|EMBL:BAE38821.1}, and
RC Urinary bladder {ECO:0000312|EMBL:BAC41074.1};
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 [3] {ECO:0000312|EMBL:AAH60991.1, ECO:0000312|Ensembl:ENSMUSP00000100020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000100020}, and
RC NOD {ECO:0000312|EMBL:CAI26236.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAH60991.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH60991.1};
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] {ECO:0000305}
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15347651; DOI=10.1074/jbc.m406770200;
RA Giessl A., Pulvermuller A., Trojan P., Park J.H., Choe H.W., Ernst O.P.,
RA Hofmann K.P., Wolfrum U.;
RT "Differential expression and interaction with the visual G-protein
RT transducin of centrin isoforms in mammalian photoreceptor cells.";
RL J. Biol. Chem. 279:51472-51481(2004).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-134 BY CK2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=18269917; DOI=10.1016/j.bbamcr.2008.01.006;
RA Trojan P., Rausch S., Giessl A., Klemm C., Krause E., Pulvermuller A.,
RA Wolfrum U.;
RT "Light-dependent CK2-mediated phosphorylation of centrins regulates complex
RT formation with visual G-protein.";
RL Biochim. Biophys. Acta 1783:1248-1260(2008).
RN [7]
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).
CC -!- FUNCTION: Ca(2+)-binding protein that may be involved in basal body
CC assembly or in a subsequent step of ciliogenesis.
CC {ECO:0000269|PubMed:12802058}.
CC -!- SUBUNIT: Interacts with G-protein beta-gamma dimers in a calcium-
CC dependent manner. {ECO:0000269|PubMed:15347651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:12802058,
CC ECO:0000269|PubMed:15347651, ECO:0000269|PubMed:18269917}. Cytoplasm
CC {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:15347651,
CC ECO:0000269|PubMed:18269917}. Note=Accumulates at procentrioles during
CC their elongation. Isoform 3 is not observed in the centriole.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:15489334};
CC IsoId=Q8K4K1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8K4K1-2; Sequence=VSP_044649;
CC Name=3 {ECO:0000269|PubMed:12802058, ECO:0000269|PubMed:16141072};
CC Synonyms=Splice4A {ECO:0000303|PubMed:12802058};
CC IsoId=Q8K4K1-3; Sequence=VSP_044650;
CC -!- TISSUE SPECIFICITY: In brain, specifically expressed in ciliated cells.
CC In retina, expression is localized to the connecting cilium and basal
CC body of photoreceptors (at protein level). Highly expressed in brain,
CC kidney, lung, retina and ovary, and weakly expressed in spleen. Not
CC detected in testis, colon, stomach, thymus, skeletal muscle, heart,
CC intestine or liver. {ECO:0000269|PubMed:12802058,
CC ECO:0000269|PubMed:15347651}.
CC -!- DOMAIN: The fourth EF-hand domain has been proven to bind calcium.
CC -!- PTM: Phosphorylated on Thr-134 by casein kinase II (CK2) in a light-
CC dependent manner. {ECO:0000269|PubMed:18269917}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; AF362367; AAM75880.1; -; mRNA.
DR EMBL; AK090064; BAC41074.1; -; mRNA.
DR EMBL; AK166515; BAE38821.1; -; mRNA.
DR EMBL; AC101743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645982; CAI26235.1; -; Genomic_DNA.
DR EMBL; AL645982; CAI26236.1; -; Genomic_DNA.
DR EMBL; AL691478; CAM14820.1; -; Genomic_DNA.
DR EMBL; AL691478; CAM14821.1; -; Genomic_DNA.
DR EMBL; BC060991; AAH60991.1; -; mRNA.
DR EMBL; BC087905; AAH87905.1; -; mRNA.
DR CCDS; CCDS17318.1; -. [Q8K4K1-1]
DR RefSeq; NP_665824.1; NM_145825.2. [Q8K4K1-1]
DR AlphaFoldDB; Q8K4K1; -.
DR SMR; Q8K4K1; -.
DR STRING; 10090.ENSMUSP00000100020; -.
DR iPTMnet; Q8K4K1; -.
DR EPD; Q8K4K1; -.
DR MaxQB; Q8K4K1; -.
DR PaxDb; Q8K4K1; -.
DR PRIDE; Q8K4K1; -.
DR ProteomicsDB; 281593; -. [Q8K4K1-1]
DR ProteomicsDB; 281594; -. [Q8K4K1-2]
DR ProteomicsDB; 281595; -. [Q8K4K1-3]
DR DNASU; 207175; -.
DR Ensembl; ENSMUST00000071400; ENSMUSP00000071349; ENSMUSG00000045031. [Q8K4K1-2]
DR Ensembl; ENSMUST00000075537; ENSMUSP00000074975; ENSMUSG00000045031. [Q8K4K1-3]
DR Ensembl; ENSMUST00000102955; ENSMUSP00000100020; ENSMUSG00000045031. [Q8K4K1-1]
DR GeneID; 207175; -.
DR KEGG; mmu:207175; -.
DR UCSC; uc008pam.1; mouse. [Q8K4K1-1]
DR CTD; 207175; -.
DR MGI; MGI:2677454; Cetn4.
DR VEuPathDB; HostDB:ENSMUSG00000045031; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000162309; -.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; Q8K4K1; -.
DR OMA; TIDIAMW; -.
DR OrthoDB; 1382571at2759; -.
DR PhylomeDB; Q8K4K1; -.
DR TreeFam; TF101141; -.
DR BioGRID-ORCS; 207175; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8K4K1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8K4K1; protein.
DR Bgee; ENSMUSG00000045031; Expressed in seminiferous tubule of testis and 208 other tissues.
DR ExpressionAtlas; Q8K4K1; baseline and differential.
DR Genevisible; Q8K4K1; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
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:0007099; P:centriole replication; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasm; Cytoskeleton; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..168
FT /note="Centrin-4"
FT /id="PRO_0000420789"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 97..132
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 133..168
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 134
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:18269917"
FT VAR_SEQ 51..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044649"
FT VAR_SEQ 94..139
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12802058,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_044650"
FT CONFLICT 22
FT /note="N -> S (in Ref. 2; BAE38821)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> G (in Ref. 2; BAC41074)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="R -> P (in Ref. 3; AC163025/AC101743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 19200 MW; 3A5AC9128E74AC2F CRC64;
MASSQRITLD QWKKKAAKVE LNDTQKQEIK EAFDLFDIDG SGTIDLKELK IAMRALGFEP
KKEEVKQLIA EIDKEGTGTI CFEDFFAIMS VKMSEKDEKE EILKAFKLFD DDATGSISLN
NIKRVAKELG ENLTEDELQE MLDEADRDGD GEINEEEFLK MMKKTSLY
