INCE_XENTR
ID INCE_XENTR Reviewed; 898 AA.
AC Q0IHP2; Q28GE7; Q5XHA5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Inner centromere protein;
GN Name=incenp; ORFNames=TEgg071h21.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Spleen, and Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-570.
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC complex that acts as a key regulator of mitosis. The CPC complex has
CC essential functions at the centromere in ensuring correct chromosome
CC alignment and segregation and is required for chromatin-induced
CC microtubule stabilization and spindle assembly. Acts as a scaffold
CC regulating CPC localization and activity. The C-terminus associates
CC with aurkb/aurora-B, the N-terminus associated with cdca8/borealin
CC and/or cdca9/dasra-A tethers the CPC to the inner centromere, and the
CC microtubule binding activity within the central SAH domain directs
CC aurkb/aurora-B toward substrates near microtubules. Activates aurkb.
CC {ECO:0000250|UniProtKB:O13024, ECO:0000250|UniProtKB:P53352}.
CC -!- SUBUNIT: Component of the CPC at least composed of survivin/birc5,
CC incenp, cdca8/borealin and/or cdca9/dasra-A, and aurkb/aurora-B.
CC Interacts (via C-terminus) with aurkb (via N-terminus and kinase
CC domain). Interacts (via N-terminus) with birc5.1, birc5.2, cdca8 and
CC cdca9. Interacts with mtus1 (By similarity).
CC {ECO:0000250|UniProtKB:O13024, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQS7}.
CC Chromosome {ECO:0000250|UniProtKB:O13024}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O13024}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:O13024}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NQS7}.
CC Note=Localizes on chromosome arms and inner centromeres from prophase
CC through metaphase and then transferring to the spindle midzone and
CC midbody from anaphase through cytokinesis. Colocalizes to the
CC equatorial cell cortex at anaphase. Colocalizes with AURKB at mitotic
CC chromosomes. {ECO:0000250|UniProtKB:O13024}.
CC -!- DOMAIN: The IN box mediates interaction with aurkb/aurora-B.
CC {ECO:0000250|UniProtKB:O13024}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds. It can refold after extension
CC suggesting an in vivo force-dependent function. The isolated SAH domain
CC is monomeric. {ECO:0000250|UniProtKB:P53352}.
CC -!- SIMILARITY: Belongs to the INCENP family. {ECO:0000305}.
CC -!- CAUTION: Originally predicted to contain a coiled coil domain but shown
CC to contain a stable SAH domain instead. {ECO:0000250|UniProtKB:P53352}.
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DR EMBL; BC084167; AAH84167.1; ALT_TERM; mRNA.
DR EMBL; BC123050; AAI23051.1; -; mRNA.
DR EMBL; CR761418; CAJ82292.1; -; mRNA.
DR RefSeq; NP_001121150.1; NM_001127678.1.
DR AlphaFoldDB; Q0IHP2; -.
DR SMR; Q0IHP2; -.
DR STRING; 8364.ENSXETP00000014718; -.
DR PaxDb; Q0IHP2; -.
DR DNASU; 496453; -.
DR GeneID; 496453; -.
DR KEGG; xtr:496453; -.
DR CTD; 3619; -.
DR Xenbase; XB-GENE-990398; incenp.
DR eggNOG; KOG4456; Eukaryota.
DR HOGENOM; CLU_015997_0_0_1; -.
DR InParanoid; Q0IHP2; -.
DR OrthoDB; 671886at2759; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000006735; Expressed in 2-cell stage embryo and 11 other tissues.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:1990385; C:meiotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0051257; P:meiotic spindle midzone assembly; IBA:GO_Central.
DR GO; GO:0051310; P:metaphase plate congression; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:InterPro.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR InterPro; IPR039130; INCENP.
DR InterPro; IPR022006; INCENP_N.
DR InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
DR PANTHER; PTHR13142; PTHR13142; 1.
DR Pfam; PF03941; INCENP_ARK-bind; 1.
DR Pfam; PF12178; INCENP_N; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..898
FT /note="Inner centromere protein"
FT /id="PRO_0000278831"
FT REGION 50..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..730
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:P53352"
FT REGION 525..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..881
FT /note="IN box"
FT /evidence="ECO:0000305"
FT COMPBIAS 68..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 133
FT /note="M -> I (in Ref. 1; AAH84167)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="K -> KTE (in Ref. 2; CAJ82292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 104130 MW; 6981A1F0DCE9EA09 CRC64;
MNDAECLSHL LQVCARKTEE FVRTLDSKHM VWLLEIEEEA RKMFSSDFNA EPELMPKTPS
QKRRRKKRTS IVPDENRDPS GRRISRRRSS ANWSNSVRRL SIRNQNKTNE DSMQEEPAQP
KRMTRARAQA SIMCPSVVEM ALPESPSQLY QKNVQVTISE QDRRSAEQKL VGSATEESEM
KTDVLPVPKI AKDTISEIVN TVVPPPVPET PAVPVTPENK SRAAAKLKIA GSSTPIEAAE
MVDLTCESPR PANELANEQP LNLTNQSVTP TGSKSDRRSV RRSLVVVKPS SRRSSLASQF
SLASKRESMT REAVRKSIRQ SIAKKKAAME TSSASSQRSC QSSIEIIDDE ITIKIRPETA
PSESVSEEAH TIESPRRSLR SRTFKKIAIS NLPDSEEPQR RVTRQMVAMD AEPTPETTDD
AQNIRRKSYK RAVDELSDDE RPSEGERSPP RKKTPSPPCP PSKIVKPPPH MKSFLHTVQK
NQLLMMTPGS IGKNIMMKSF IKRNTPLKMD PKEKERQRLD ALRKKEEAEL QRKQKIEEGK
KRKQEELKLR REERLRKVLQ ARERVEQLEE EKKKKIEQKF AQIDEKSEKV REDRMAEEKA
KKKITAKKQE EVECRRRQEE EARKLKAKQM EEEERRHQDL LQKKREEEEL ERQKKIAEAK
RLAEQRQAEQ ERERQREQQL LAEKERLRAE RERIEREKAL QLQRELERAA QEKEQQRREA
EERKKREQQE RLEQERLERL HKEQEAKRLQ EEQQRKAKEQ AAAASAPVMN VTVDMQNSPA
CESYEMTPKS YKAPSVKVNE ENYGMDLNSD DSTDDESQPR KPIPAWASGN LLAQAIRQQY
YKPMDVDRMY GTIDSPKLEE LFYKSKPRYY KRTSSAVWHS PPLSSNRHHL AVGYGLKY
