INCE_CHICK
ID INCE_CHICK Reviewed; 877 AA.
AC P53352;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Inner centromere protein;
GN Name=INCENP;
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 [MRNA] (ISOFORMS INCENP I AND INCENP II), AND
RP SUBCELLULAR LOCATION.
RX PubMed=8408220; DOI=10.1083/jcb.123.2.373;
RA Mackay A.M., Eckley D.M., Chue C., Earnshaw W.C.;
RT "Molecular analysis of the INCENPs (inner centromere proteins): separate
RT domains are required for association with microtubules during interphase
RT and with the central spindle during anaphase.";
RL J. Cell Biol. 123:373-385(1993).
RN [2]
RP INTERACTION WITH CBX5.
RX PubMed=9864353; DOI=10.1083/jcb.143.7.1763;
RA Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.;
RT "INCENP centromere and spindle targeting: identification of essential
RT conserved motifs and involvement of heterochromatin protein HP1.";
RL J. Cell Biol. 143:1763-1774(1998).
RN [3]
RP FUNCTION, INTERACTION WITH AURKB, AND MUTAGENESIS OF TRP-804 AND PHE-840.
RX PubMed=19951914; DOI=10.1083/jcb.200906053;
RA Xu Z., Ogawa H., Vagnarelli P., Bergmann J.H., Hudson D.F., Ruchaud S.,
RA Fukagawa T., Earnshaw W.C., Samejima K.;
RT "INCENP-aurora B interactions modulate kinase activity and chromosome
RT passenger complex localization.";
RL J. Cell Biol. 187:637-653(2009).
RN [4]
RP SAH DOMAIN, SUBUNIT, AND FUNCTION.
RX PubMed=26175154; DOI=10.1074/jbc.m115.645317;
RA Samejima K., Platani M., Wolny M., Ogawa H., Vargiu G., Knight P.J.,
RA Peckham M., Earnshaw W.C.;
RT "The inner centromere protein (INCENP) coil is a single alpha-helix (SAH)
RT domain that binds directly to microtubules and is important for chromosome
RT passenger complex (CPC) localization and function in mitosis.";
RL J. Biol. Chem. 290:21460-21472(2015).
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, the N-terminus associated with BIRC5/survivin and
CC CDCA8/borealin tethers the CPC to the inner centromere, and the
CC microtubule binding activity within the central SAH domain directs
CC AURKB toward substrates near microtubules. The flexibility of the SAH
CC domain is proposed to allow AURKB to follow substrates on dynamic
CC microtubules while ensuring CPC docking to static chromatin. Activates
CC AURKB. {ECO:0000250|UniProtKB:O13024, ECO:0000250|UniProtKB:Q9NQS7,
CC ECO:0000305|PubMed:26175154}.
CC -!- SUBUNIT: Component of the chromosomal passenger complex (CPC) composed
CC of at least BIRC5/survivin, CDCA8/borealin, INCENP and AURKB; in the
CC complex binds directly to AURKB via the IN box, and forms a triple-
CC helix bundle-based subcomplex with BIRC5 and CDCA8 via its N-terminus.
CC The initially reported homodimerization is questioned as the SAH domain
CC is shown to be monomeric. Interacts with CBX5.
CC {ECO:0000250|UniProtKB:O13024, ECO:0000250|UniProtKB:Q9NQS7,
CC ECO:0000269|PubMed:19951914, ECO:0000269|PubMed:9864353,
CC ECO:0000305|PubMed:26175154}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8408220}. Chromosome,
CC centromere {ECO:0000269|PubMed:8408220}. Chromosome
CC {ECO:0000269|PubMed:8408220}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:8408220}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NQS7}.
CC Note=Is restricted to the nucleus in interphase, remains tightly bound
CC to the chromosomes until early metaphase, and during late metaphase
CC gets concentrated in linear arrays that transect the metaphase plate
CC between the chromosomes (PubMed:8408220). As anaphase begins to move to
CC the spindle midzone where it is intimately associated with the bundled
CC microtubules (PubMed:8408220). Later in anaphase gets closely
CC associated with the cell cortex, and by telophase is concentrated at
CC each side of the midbody in the intercellular bridge, with which it is
CC discarded after (PubMed:8408220). {ECO:0000269|PubMed:8408220}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=INCENP II;
CC IsoId=P53352-1; Sequence=Displayed;
CC Name=INCENP I;
CC IsoId=P53352-2; Sequence=VSP_004292;
CC -!- DOMAIN: The IN box mediates interaction with AURKB and AURKC.
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:0000305|PubMed:26175154}.
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:0000305|PubMed:26175154}.
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DR EMBL; Z25419; CAA80906.1; -; mRNA.
DR EMBL; Z25420; CAA80907.1; -; mRNA.
DR PIR; I50590; I50590.
DR PIR; I50591; I50591.
DR RefSeq; NP_990661.1; NM_205330.1.
DR AlphaFoldDB; P53352; -.
DR BioGRID; 676530; 1.
DR STRING; 9031.ENSGALP00000012175; -.
DR PaxDb; P53352; -.
DR PRIDE; P53352; -.
DR GeneID; 396270; -.
DR KEGG; gga:396270; -.
DR CTD; 3619; -.
DR VEuPathDB; HostDB:geneid_396270; -.
DR eggNOG; KOG4456; Eukaryota.
DR InParanoid; P53352; -.
DR PhylomeDB; P53352; -.
DR PRO; PR:P53352; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; 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:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
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; ISS:UniProtKB.
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 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 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule;
KW Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..877
FT /note="Inner centromere protein"
FT /id="PRO_0000084199"
FT REGION 47..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..270
FT /note="Interaction with CBX5"
FT /evidence="ECO:0000269|PubMed:9864353"
FT REGION 178..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..715
FT /note="SAH"
FT /evidence="ECO:0000305|PubMed:26175154"
FT REGION 572..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..823
FT /note="IN box"
FT /evidence="ECO:0000305"
FT MOTIF 155..159
FT /note="PXVXL/I motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NQS7"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 716..753
FT /note="Missing (in isoform INCENP I)"
FT /evidence="ECO:0000303|PubMed:8408220"
FT /id="VSP_004292"
FT VARIANT 257
FT /note="A -> T"
FT VARIANT 471
FT /note="E -> Q"
FT MUTAGEN 804
FT /note="W->G: Disrupts interaction with AURKB."
FT /evidence="ECO:0000269|PubMed:19951914"
FT MUTAGEN 840
FT /note="F->A: Interacts with AURKB but fails to fully
FT activate AURKB."
FT /evidence="ECO:0000269|PubMed:19951914"
SQ SEQUENCE 877 AA; 100941 MW; AFA703149F555352 CRC64;
MAVATGLARL PVVCNQRLAE LLRQVDDVDL LWLEEIHEEA ARMFGSHYSD QPELMPKTPS
QKNRKRRKRP SALRGESLEL GRRRLSRRRT NNLKAVSSKR DSQRLQNKED TEGLGTEAQE
LSSQTVSRRL TRSQVAAPAD RSEVLPEHLR ERVVPVVEIS VCDRISAEFQ FQKCASERAE
NHSASLPPSS DDKSPKESSA AESQPLPAAS ELIVPHTPEA KGAGKNKSAF KKTANVADTT
VVLSEKELGL EEVDDSAQVQ KHNERDDKEP SQRTTDSPET PTGSRLSRRS VRRSLMGKPS
TIRRTSLAEK YSLARKREST IRKSIARTVI KRKAPQKLSV SSSSVNGSGS EEVPEDEETV
VNAGPPPVPQ TPPKLDFQGL RMSLRSQTVN RNEQQQETSN NECDLSKSEK TQEPPQSARR
KTSYKRAVDQ RYDTQQAEDG GLSPLRKKTP SPPCPASKVV RPFKTFLHTV EKNQLLMTPS
SVGRNGVIKS FIKYNTPLQH DPKEKERQKL QALRKKEEAE QLRKQKVEEE KKRRQEEAKL
RREERLRKVL QARERAEQLE EERKRRIEQK LALFDEKTEK AREERLAEEK IKKRAAAKKM
EEAEARRRQD EEARKQKALQ QEEEERRHKE LMQKKKEEEQ ERARKIAEQR QAEQEREKQL
AAEREQERKK EQERKKEEER IQAEKQREQQ EKAARLQKEV LAAKEQLQKE MEKKEKEEQL
LAEMKRQEQE QKKLPEEQKA KDVAQTQHLE NKENSPACNS YQMTPQYHKD PKPPKINPNN
YGMDLNSDDS TDDESQPRKP IPAWASGNQL SQAVIRQYYN PPNVDALFGT IVSPKLEDIF
YKSKPRYFKR TSSAVWNSPP FPGAKSVLGL PYSLKKY
