NDC80_CHICK
ID NDC80_CHICK Reviewed; 640 AA.
AC Q76I89; Q5ZLT8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Kinetochore protein NDC80 homolog;
DE AltName: Full=Kinetochore protein Hec1;
DE AltName: Full=Kinetochore-associated protein 2;
GN Name=NDC80; Synonyms=HEC1, KNTC2; ORFNames=RCJMB04_4o15;
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], FUNCTION, INTERACTION WITH CDCA1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12829748; DOI=10.1242/jcs.00645;
RA Hori T., Haraguchi T., Hiraoka Y., Kimura H., Fukagawa T.;
RT "Dynamic behavior of Nuf2-Hec1 complex that localizes to the centrosome and
RT centromere and is essential for mitotic progression in vertebrate cells.";
RL J. Cell Sci. 116:3347-3362(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [3]
RP INTERACTION WITH CENPH, AND SUBCELLULAR LOCATION.
RX PubMed=15713649; DOI=10.1128/mcb.25.5.1958-1970.2005;
RA Mikami Y., Hori T., Kimura H., Fukagawa T.;
RT "The functional region of CENP-H interacts with the Nuf2 complex that
RT localizes to centromere during mitosis.";
RL Mol. Cell. Biol. 25:1958-1970(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15870271; DOI=10.1128/mcb.25.10.3967-3981.2005;
RA Regnier V., Vagnarelli P., Fukagawa T., Zerjal T., Burns E., Trouche D.,
RA Earnshaw W., Brown W.;
RT "CENP-A is required for accurate chromosome segregation and sustained
RT kinetochore association of BubR1.";
RL Mol. Cell. Biol. 25:3967-3981(2005).
RN [5]
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Acts as a component of the essential kinetochore-associated
CC NDC80 complex, which is required for chromosome segregation and spindle
CC checkpoint activity (PubMed:12829748). Required for kinetochore
CC integrity and the organization of stable microtubule binding sites in
CC the outer plate of the kinetochore. The NDC80 complex synergistically
CC enhances the affinity of the SKA1 complex for microtubules and may
CC allow the NDC80 complex to track depolymerizing microtubules. May play
CC a role in chromosome congression and may be essential for the end-on
CC attachment of the kinetochores to spindle microtubules (By similarity).
CC {ECO:0000250|UniProtKB:O14777, ECO:0000269|PubMed:12829748}.
CC -!- SUBUNIT: Component of the NDC80 complex, which is composed of at least
CC NDC80/HEC1 and CDCA1. Interacts with CENPH.
CC {ECO:0000269|PubMed:12829748, ECO:0000269|PubMed:15713649}.
CC -!- INTERACTION:
CC Q76I89; Q90ZF9: CENPH; NbExp=5; IntAct=EBI-1003779, EBI-1003677;
CC Q76I89; Q76I90: NUF2; NbExp=3; IntAct=EBI-1003779, EBI-1003866;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14777}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O14777}.
CC Note=Localizes to kinetochores from late prophase to anaphase.
CC Localizes specifically to the outer plate of the kinetochore.
CC {ECO:0000250|UniProtKB:O14777}.
CC -!- SIMILARITY: Belongs to the NDC80/HEC1 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; AB098622; BAC81642.1; -; mRNA.
DR EMBL; AJ719646; CAG31305.1; -; mRNA.
DR RefSeq; NP_989808.2; NM_204477.2.
DR RefSeq; XP_015133419.1; XM_015277933.1.
DR AlphaFoldDB; Q76I89; -.
DR SMR; Q76I89; -.
DR BioGRID; 675431; 2.
DR IntAct; Q76I89; 2.
DR STRING; 9031.ENSGALP00000023851; -.
DR PaxDb; Q76I89; -.
DR PRIDE; Q76I89; -.
DR Ensembl; ENSGALT00000023897; ENSGALP00000023851; ENSGALG00000014801.
DR GeneID; 395134; -.
DR KEGG; gga:395134; -.
DR CTD; 10403; -.
DR VEuPathDB; HostDB:geneid_395134; -.
DR eggNOG; KOG0995; Eukaryota.
DR GeneTree; ENSGT00390000018386; -.
DR HOGENOM; CLU_012583_2_0_1; -.
DR InParanoid; Q76I89; -.
DR OMA; IRFKVHV; -.
DR OrthoDB; 925552at2759; -.
DR PhylomeDB; Q76I89; -.
DR TreeFam; TF101177; -.
DR Reactome; R-GGA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR Reactome; R-GGA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-GGA-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q76I89; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000014801; Expressed in ovary and 9 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0031262; C:Ndc80 complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000940; C:outer kinetochore; IEA:Ensembl.
DR GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0140483; F:kinetochore adaptor activity; ISS:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051298; P:centrosome duplication; IEA:Ensembl.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:Ensembl.
DR GO; GO:0008315; P:G2/MI transition of meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0051383; P:kinetochore organization; IEA:Ensembl.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IEA:Ensembl.
DR Gene3D; 1.10.418.30; -; 1.
DR InterPro; IPR040967; DUF5595.
DR InterPro; IPR005550; Kinetochore_Ndc80.
DR InterPro; IPR038273; Ndc80_sf.
DR PANTHER; PTHR10643; PTHR10643; 1.
DR Pfam; PF18077; DUF5595; 1.
DR Pfam; PF03801; Ndc80_HEC; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW Kinetochore; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..640
FT /note="Kinetochore protein NDC80 homolog"
FT /id="PRO_0000249553"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..427
FT /evidence="ECO:0000255"
FT COILED 464..573
FT /evidence="ECO:0000255"
FT CONFLICT 93
FT /note="A -> T (in Ref. 2; CAG31305)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="D -> N (in Ref. 2; CAG31305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 73741 MW; FACFED7A0857F71B CRC64;
MRRSSTTSGS SGRQSTMVLR VQDSNKMGLQ TPQTKDRGTF GKLSMSKTTS ATSERKVSFF
GKRASGAGGS RNSQYGMFGT EKIKDPRPLH DKAFIQQCIK QLCEFLVENG YAHNVTIKSL
QSPSVKDFIK IFTFIYGFLC PSYELPDSKF EEEIPRVFKE LGYPFPLSKS SMYTVGAPHT
WPQIVAALIW LTDCFKLYAA MRENPSSFDD GQNWGGETDD GIVHNKLFMD YVVKCYEHFM
KGGDTYEELD AEVQSKLKDL FNVDEFKIEG LAAENKRLHE EIARLEKERE SEPDRLVSLR
KLRSSFQADV QKYQAYLANL ESHTTILDQK MKSVNEEVET TEMEVEAMKQ ENARLQHIFD
NQKYSVADIE RINHERNELQ QTINKLTKEL EAEEHQLWNE ELKYARNKEA IETQLAEYHK
LARKLKLIPI SAENSKGHDF EIHFNPEAGP NCLVKYRTQI KAPLMEIVNQ TEEEIRKATQ
RKMSLEDTLE QVNAMVAEKK SSVKTLKEEA EKLDDLYHQK LKEAEEEEQK CANELELLEK
HKQLLESGVN EGLSEATNEL HDIQRQYQIV MQTTTEESRK AGDNLNRLLE VITTHVVSIE
KYLDEQNSKI DRDYEEFMSE DLLSTLTGIL DSYKKKAESI