CENPT_MACFA
ID CENPT_MACFA Reviewed; 561 AA.
AC Q4R5U8; Q4R7F5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Centromere protein T;
DE Short=CENP-T;
GN Name=CENPT; ORFNames=QtsA-15444, QtsA-20687;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. The CENPA-NAC complex
CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved
CC in incorporation of newly synthesized CENPA into centromeres. Part of a
CC nucleosome-associated complex that binds specifically to histone H3-
CC containing nucleosomes at the centromere, as opposed to nucleosomes
CC containing CENPA. Component of the heterotetrameric CENP-T-W-S-X
CC complex that binds and supercoils DNA, and plays an important role in
CC kinetochore assembly. CENPT has a fundamental role in kinetochore
CC assembly and function. It is one of the inner kinetochore proteins,
CC with most further proteins binding downstream. Required for normal
CC chromosome organization and normal progress through mitosis.
CC {ECO:0000250|UniProtKB:Q96BT3}.
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.
CC Identified in a centromeric complex containing histones H2A, H2B, H3
CC and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H,
CC SSRP1 and RSF1. Interacts (via N-terminus) with the NDC80 complex.
CC Heterodimer with CENPW; this dimer coassembles with CENPS-CENPX
CC heterodimers at centromeres to form the tetrameric CENP-T-W-S-X
CC complex. {ECO:0000250|UniProtKB:Q96BT3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BT3}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q96BT3}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q96BT3}.
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:0000250}.
CC -!- PTM: Dynamically phosphorylated during the cell cycle. Phosphorylated
CC during G2 phase, metaphase and anaphase, but not during telophase or G1
CC phase. {ECO:0000250|UniProtKB:Q96BT3}.
CC -!- SIMILARITY: Belongs to the CENP-T/CNN1 family. {ECO:0000305}.
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DR EMBL; AB168863; BAE00967.1; -; mRNA.
DR EMBL; AB169445; BAE01527.1; -; mRNA.
DR RefSeq; NP_001271777.1; NM_001284848.1.
DR AlphaFoldDB; Q4R5U8; -.
DR SMR; Q4R5U8; -.
DR STRING; 9541.XP_005592347.1; -.
DR GeneID; 101926328; -.
DR CTD; 80152; -.
DR eggNOG; ENOG502RZH1; Eukaryota.
DR OrthoDB; 360139at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
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:0051276; P:chromosome organization; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; DNA-binding;
KW Kinetochore; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..561
FT /note="Centromere protein T"
FT /id="PRO_0000249515"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..421
FT /note="Flexible stalk domain"
FT /evidence="ECO:0000250"
FT REGION 114..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q561R1"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q561R1"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT CONFLICT 115
FT /note="P -> L (in Ref. 1; BAE00967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 60497 MW; 32B68BA923E6A83E CRC64;
MADHNPDGDP TPRTLLRRVL DTADPRTPRR PRSARAGAQR ALLETASSRR LSGQTKTIAK
GRSRGARSIG RSAHVQARGH LEEQTPRTLL KNILLTAPES SILMPESVVK PVPAPQVVQP
SRRESSRGSL ELQLPELEPS TTLAPGLLAP GRRKQRLRLS MFQQGVDQGL PLSQEPQGNA
DASSLTSSLN LTFATPLQPQ SVQRPGLARR PPARRAVDVG AFLRDLRDTS LAPPNIVLED
TQPFSQPTVG SPNVYHSLPC TPHTGAEDAE QAAGRRTQSS GPGLQNNSPG KPAQFLAGEA
EEVDAFALGF LSTSSGVSGE DEVEPLHNGV EEAEKKMKEE GVSVSEMEAT GAQGPSRAEE
PEGHTQVTEA EGSQGTAEAE GPGASSGDED ASSRAASPEL ASSTPESLQA RRHHQFPEPA
PPPGAAVLSS EPAEPLLVRC PPRSRTTGPR PRQDPHKAGL SHYVKLFSFF AKMPMERKAL
EMVEKCLDKY FQHLCDDLEV FAAHAGRKTV KPEDLELLMR RQGLVTDQVS LHVLVERHLP
LEYRQLLIPC AYSGNSVFPA Q
