CETN1_HUMAN
ID CETN1_HUMAN Reviewed; 172 AA.
AC Q12798; B2R536;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Centrin-1 {ECO:0000305};
DE AltName: Full=Caltractin isoform 2;
GN Name=CETN1 {ECO:0000312|HGNC:HGNC:1866}; Synonyms=CEN1, CETN;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=8175926; DOI=10.1242/jcs.107.1.9;
RA Errabolu R., Sanders M.A., Salisbury J.L.;
RT "Cloning of a cDNA encoding human centrin, an EF-hand protein of
RT centrosomes and mitotic spindle poles.";
RL J. Cell Sci. 107:9-16(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 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).
CC -!- FUNCTION: Plays a fundamental role in microtubule-organizing center
CC structure and function (PubMed:8175926). Plays a role in sperm cilia
CC formation (By similarity). {ECO:0000250|UniProtKB:P41209,
CC ECO:0000269|PubMed:8175926}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with PIFO
CC (PubMed:20643351). {ECO:0000250, ECO:0000269|PubMed:20643351}.
CC -!- INTERACTION:
CC Q12798; Q8NA72: POC5; NbExp=6; IntAct=EBI-2512818, EBI-2561090;
CC Q12798; Q8NA72-3: POC5; NbExp=4; IntAct=EBI-2512818, EBI-11751537;
CC Q12798; Q2NKQ1-4: SGSM1; NbExp=7; IntAct=EBI-2512818, EBI-10182463;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:8175926}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:P41209}. Note=Centrosome of interphase
CC and 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 (By similarity). {ECO:0000250|UniProtKB:P41209,
CC ECO:0000269|PubMed:8175926}.
CC -!- MISCELLANEOUS: Binds two moles of calcium per mole of protein.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; U03270; AAC27343.1; -; mRNA.
DR EMBL; AK312047; BAG34983.1; -; mRNA.
DR EMBL; CH471113; EAX01727.1; -; Genomic_DNA.
DR EMBL; BC029515; AAH29515.1; -; mRNA.
DR CCDS; CCDS11820.1; -.
DR PIR; I38424; I38424.
DR RefSeq; NP_004057.1; NM_004066.2.
DR AlphaFoldDB; Q12798; -.
DR SMR; Q12798; -.
DR BioGRID; 107495; 61.
DR IntAct; Q12798; 43.
DR MINT; Q12798; -.
DR STRING; 9606.ENSP00000319052; -.
DR iPTMnet; Q12798; -.
DR PhosphoSitePlus; Q12798; -.
DR BioMuta; CETN1; -.
DR DMDM; 2493440; -.
DR jPOST; Q12798; -.
DR MassIVE; Q12798; -.
DR MaxQB; Q12798; -.
DR PaxDb; Q12798; -.
DR PeptideAtlas; Q12798; -.
DR PRIDE; Q12798; -.
DR ProteomicsDB; 58948; -.
DR Antibodypedia; 5901; 282 antibodies from 28 providers.
DR DNASU; 1068; -.
DR Ensembl; ENST00000327228.5; ENSP00000319052.3; ENSG00000177143.5.
DR GeneID; 1068; -.
DR KEGG; hsa:1068; -.
DR MANE-Select; ENST00000327228.5; ENSP00000319052.3; NM_004066.3; NP_004057.1.
DR UCSC; uc002kko.2; human.
DR CTD; 1068; -.
DR DisGeNET; 1068; -.
DR GeneCards; CETN1; -.
DR HGNC; HGNC:1866; CETN1.
DR HPA; ENSG00000177143; Tissue enriched (testis).
DR MIM; 603187; gene.
DR neXtProt; NX_Q12798; -.
DR OpenTargets; ENSG00000177143; -.
DR PharmGKB; PA26419; -.
DR VEuPathDB; HostDB:ENSG00000177143; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000157209; -.
DR HOGENOM; CLU_061288_18_2_1; -.
DR InParanoid; Q12798; -.
DR OMA; GIQKIFA; -.
DR OrthoDB; 1382571at2759; -.
DR PhylomeDB; Q12798; -.
DR TreeFam; TF101141; -.
DR PathwayCommons; Q12798; -.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR SignaLink; Q12798; -.
DR SIGNOR; Q12798; -.
DR BioGRID-ORCS; 1068; 6 hits in 1066 CRISPR screens.
DR GeneWiki; CETN1; -.
DR GenomeRNAi; 1068; -.
DR Pharos; Q12798; Tbio.
DR PRO; PR:Q12798; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q12798; protein.
DR Bgee; ENSG00000177143; Expressed in left testis and 45 other tissues.
DR ExpressionAtlas; Q12798; baseline and differential.
DR Genevisible; Q12798; HS.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; 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:0032795; F:heterotrimeric G-protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
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 Calcium; Cell cycle; Cell division; Cell projection; Cytoplasm;
KW Cytoskeleton; Metal-binding; Mitosis; Reference proteome; Repeat.
FT CHAIN 1..172
FT /note="Centrin-1"
FT /id="PRO_0000073559"
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 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"
SQ SEQUENCE 172 AA; 19570 MW; 9ED8193F26F18881 CRC64;
MASGFKKPSA ASTGQKRKVA PKPELTEDQK QEVREAFDLF DVDGSGTIDA KELKVAMRAL
GFEPRKEEMK KMISEVDREG TGKISFNDFL AVMTQKMSEK DTKEEILKAF RLFDDDETGK
ISFKNLKRVA NELGENLTDE ELQEMIDEAD RDGDGEVNEE EFLRIMKKTS LY
