CENPT_CHICK
ID CENPT_CHICK Reviewed; 639 AA.
AC F1NPG5;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Centromere protein T;
DE Short=CENP-T;
GN Name=CENPT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=White Leghorn Hisex;
RX PubMed=12445392; DOI=10.1016/s0960-9822(02)01296-4;
RA Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E.,
RA Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J.;
RT "A comprehensive collection of chicken cDNAs.";
RL Curr. Biol. 12:1965-1969(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3]
RP FUNCTION, INTERACTION WITH CENPW, AND SUBCELLULAR LOCATION.
RX PubMed=19070575; DOI=10.1016/j.cell.2008.10.019;
RA Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y.,
RA McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T.;
RT "CCAN makes multiple contacts with centromeric DNA to provide distinct
RT pathways to the outer kinetochore.";
RL Cell 135:1039-1052(2008).
RN [4]
RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH CENPW.
RX PubMed=21464230; DOI=10.1083/jcb.201012050;
RA Suzuki A., Hori T., Nishino T., Usukura J., Miyagi A., Morikawa K.,
RA Fukagawa T.;
RT "Spindle microtubules generate tension-dependent changes in the
RT distribution of inner kinetochore proteins.";
RL J. Cell Biol. 193:125-140(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 54-162, FUNCTION, INTERACTION
RP WITH CENPS; CENPW AND CEPNX, AND SUBCELLULAR LOCATION.
RX PubMed=22304917; DOI=10.1016/j.cell.2011.11.061;
RA Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T.,
RA Morikawa K., Cheeseman I.M., Fukagawa T.;
RT "CENP-T-W-S-X forms a unique centromeric chromatin structure with a
RT histone-like fold.";
RL Cell 148:487-501(2012).
CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC complex that plays a central role in assembly of kinetochore proteins,
CC mitotic progression and chromosome segregation (By similarity). The
CC CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex
CC and may be involved in incorporation of newly synthesized CENPA into
CC centromeres (By similarity). Part of a nucleosome-associated complex
CC that binds specifically to histone H3-containing nucleosomes at the
CC centromere, as opposed to nucleosomes containing CENPA. Component of
CC the heterotetrameric CENP-T-W-S-X complex that binds and supercoils
CC DNA, and plays an important role in kinetochore assembly. CENPT has a
CC fundamental role in kinetochore assembly and function. It is one of the
CC inner kinetochore proteins, with most further proteins binding
CC downstream. Required for normal chromosome organization and normal
CC progress through mitosis. {ECO:0000250, ECO:0000269|PubMed:19070575,
CC ECO:0000269|PubMed:22304917}.
CC -!- SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK,
CC CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is
CC probably recruited on centromeres by the CENPA-NAC complex, at least
CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (By
CC similarity). Identified in a centromeric complex containing histones
CC H2A, H2B, H3 and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN,
CC HJURP, SUPT16H, SSRP1 and RSF1 (By similarity). Interacts (via N-
CC terminus) with the NDC80 complex (By similarity). Heterodimer with
CC CENPW; this dimer coassembles with CENPS-CENPX heterodimers at
CC centromeres to form the tetrameric CENP-T-W-S-X complex
CC (PubMed:19070575, PubMed:21464230, PubMed:22304917).
CC {ECO:0000250|UniProtKB:Q96BT3, ECO:0000269|PubMed:19070575,
CC ECO:0000269|PubMed:21464230, ECO:0000269|PubMed:22304917}.
CC -!- INTERACTION:
CC F1NPG5; E1BSW7: CENPS; NbExp=3; IntAct=EBI-2132248, EBI-5487792;
CC F1NPG5; P0DJH6: CENPW; NbExp=4; IntAct=EBI-2132248, EBI-2132287;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19070575}.
CC Chromosome, centromere {ECO:0000269|PubMed:19070575}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:19070575}.
CC Note=Constitutively localizes to centromeres throughout the cell cycle,
CC and to kinetochores during mitosis. Localizes to the inner kinetochore,
CC and may connect it to the outer kinetochore via its N-terminus.
CC {ECO:0000250|UniProtKB:Q96BT3}.
CC -!- DOMAIN: The largest part of the sequence forms an elongated and
CC flexible stalk structure that is connected to a C-terminal globular
CC domain with a histone-type fold. {ECO:0000269|PubMed:21464230}.
CC -!- MISCELLANEOUS: Association with CENPA-containing complexes may be
CC indirect and due to the proximity of centromeric nucleosomes containing
CC histone H3 with those containing CENPA.
CC -!- SIMILARITY: Belongs to the CENP-T/CNN1 family. {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; AJ452155; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU128959; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU260128; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU381659; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU382952; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU433983; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD734856; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AADN02051672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001263242.1; NM_001276313.1.
DR PDB; 3B0C; X-ray; 2.20 A; T=531-639.
DR PDB; 3B0D; X-ray; 2.20 A; B/T=531-639.
DR PDB; 3VH5; X-ray; 2.40 A; T=531-637.
DR PDB; 3VH6; X-ray; 3.35 A; T=531-637.
DR PDB; 3VZA; X-ray; 1.90 A; E/F=63-98.
DR PDBsum; 3B0C; -.
DR PDBsum; 3B0D; -.
DR PDBsum; 3VH5; -.
DR PDBsum; 3VH6; -.
DR PDBsum; 3VZA; -.
DR AlphaFoldDB; F1NPG5; -.
DR SMR; F1NPG5; -.
DR BioGRID; 677267; 1.
DR IntAct; F1NPG5; 6.
DR MINT; F1NPG5; -.
DR STRING; 9031.ENSGALP00000042737; -.
DR iPTMnet; F1NPG5; -.
DR PaxDb; F1NPG5; -.
DR Ensembl; ENSGALT00000043964; ENSGALP00000042737; ENSGALG00000028900.
DR GeneID; 415654; -.
DR KEGG; gga:415654; -.
DR CTD; 80152; -.
DR VEuPathDB; HostDB:geneid_415654; -.
DR eggNOG; ENOG502RZH1; Eukaryota.
DR GeneTree; ENSGT00390000003044; -.
DR HOGENOM; CLU_040180_0_0_1; -.
DR InParanoid; F1NPG5; -.
DR OrthoDB; 360139at2759; -.
DR PRO; PR:F1NPG5; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000028900; Expressed in testis and 14 other tissues.
DR ExpressionAtlas; F1NPG5; baseline and differential.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR028255; CENP-T.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR032373; CENP-T_N.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR46904; PTHR46904; 1.
DR Pfam; PF15511; CENP-T_C; 1.
DR Pfam; PF16171; CENP-T_N; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA-binding; Kinetochore; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..639
FT /note="Centromere protein T"
FT /id="PRO_0000417383"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..500
FT /note="Flexible stalk domain"
FT REGION 266..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..518
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:3VZA"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:3VZA"
FT HELIX 538..549
FT /evidence="ECO:0007829|PDB:3B0D"
FT HELIX 555..582
FT /evidence="ECO:0007829|PDB:3B0D"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:3B0D"
FT HELIX 590..599
FT /evidence="ECO:0007829|PDB:3B0D"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:3B0C"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:3B0D"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:3B0D"
FT HELIX 619..625
FT /evidence="ECO:0007829|PDB:3B0D"
SQ SEQUENCE 639 AA; 70670 MW; 9D314920A56ADC11 CRC64;
MDGRVGLRAS RRAAPTPRVA VRSSPRHRAR VREQEPVVSA MSGSGLGKEN KAGSSTPLRH
RPNAFSELDN ATPRVMLRKI IQNQPQVSPL ALQTVQLEET EDARPEPPSQ RTSSTVELQL
PDLVPEDASV TTFRMTRKRK KLSISEFERA ADKRLPQNQA HSTLDSTLVR SLRMSVGSVM
APDTVEKRGL LRRPQNHKAI DIAAFEGGVE QNMLQIKAQD YLVDLQTSSM TGTTTIRTDA
EVVLNNTELF VEPQLGEQNL LAVEPQLSDS KTSAQRSNTS YPAHEKARLE GLVSRVSTDE
RRTLRFSEKD LITDHEHVDG ITQKTPAKQG EEEQDHSQQN DPMEQFSESE EMAGTTEHHA
DAEYSEHSEK KLSRKAVSQL TAAQDAGVEM EMTPSEGGVA EGTEHQDSPK AELQMAGSPG
GHSPASYSLE KPGAKPLKEA VEQTGEIERG TITGVLDAAE EEATDDESDK EDHESEEISM
KTPMFVHAAA YRPQPVLSPP HPVKSASPEL PPQPVRAKPV PKSSGAAQRK TREPEIASSL
IKQIFSHYVK TPVTRDAYKI VEKCSERYFK QISSDLEAYS QHAGRKTVEM ADVELLMRRQ
GLVTDKMPLH VLVERHLPLE YRKLLIPIAV SGNKVIPCK
