NUF2_CAEEL
ID NUF2_CAEEL Reviewed; 490 AA.
AC Q21952;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Kinetochore protein Nuf2 homolog;
DE Short=CeNuf2;
DE AltName: Full=Kinetochore protein him-10;
DE AltName: Full=Protein high incidence of males 10;
GN Name=him-10; ORFNames=R12B2.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-109.
RX PubMed=11402066; DOI=10.1083/jcb.153.6.1227;
RA Howe M., McDonald K.L., Albertson D.G., Meyer B.J.;
RT "HIM-10 is required for kinetochore structure and function on
RT Caenorhabditis elegans holocentric chromosomes.";
RL J. Cell Biol. 153:1227-1238(2001).
RN [3]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX
RP WITH NDC-80 AND KNL-1, AND SUBCELLULAR LOCATION.
RX PubMed=14522947; DOI=10.1101/gad.1126303;
RA Desai A., Rybina S., Mueller-Reichert T., Shevchenko A., Shevchenko A.,
RA Hyman A., Oegema K.;
RT "KNL-1 directs assembly of the microtubule-binding interface of the
RT kinetochore in C. elegans.";
RL Genes Dev. 17:2421-2435(2003).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15371539; DOI=10.1091/mbc.e04-06-0486;
RA Stear J.H., Roth M.B.;
RT "The Caenorhabditis elegans kinetochore reorganizes at prometaphase and in
RT response to checkpoint stimuli.";
RL Mol. Biol. Cell 15:5187-5196(2004).
RN [5]
RP FUNCTION.
RX PubMed=23085020; DOI=10.1016/j.devcel.2012.09.012;
RA Schmidt J.C., Arthanari H., Boeszoermenyi A., Dashkevich N.M.,
RA Wilson-Kubalek E.M., Monnier N., Markus M., Oberer M., Milligan R.A.,
RA Bathe M., Wagner G., Grishchuk E.L., Cheeseman I.M.;
RT "The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and
RT binds to curved protofilaments.";
RL Dev. Cell 23:968-980(2012).
CC -!- FUNCTION: Acts as a component of the essential kinetochore-associated
CC NDC80 complex, which is required for chromosome segregation in mitosis
CC and meiosis and spindle checkpoint activity (PubMed:11402066,
CC PubMed:14522947, PubMed:15371539). The ndc-80 complex synergistically
CC enhances the affinity of the ska-1 complex for microtubules and may
CC allow the ndc-80 complex to track depolymerizing microtubules
CC (PubMed:23085020). {ECO:0000269|PubMed:11402066,
CC ECO:0000269|PubMed:14522947, ECO:0000269|PubMed:15371539,
CC ECO:0000269|PubMed:23085020}.
CC -!- SUBUNIT: Component of the NDC80 complex, which is composed of at least
CC ndc-80 and him-10. The NDC80 complex interacts with knl-1.
CC {ECO:0000269|PubMed:14522947}.
CC -!- INTERACTION:
CC Q21952; Q17635: ndc-80; NbExp=6; IntAct=EBI-326288, EBI-314429;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Localizes to kinetochores.
CC -!- SIMILARITY: Belongs to the NUF2 family. {ECO:0000305}.
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DR EMBL; FO081686; CCD73315.1; -; Genomic_DNA.
DR PIR; T16722; T16722.
DR RefSeq; NP_498253.1; NM_065852.5.
DR AlphaFoldDB; Q21952; -.
DR SMR; Q21952; -.
DR BioGRID; 41037; 20.
DR ComplexPortal; CPX-806; Ndc80 complex.
DR DIP; DIP-25404N; -.
DR IntAct; Q21952; 9.
DR STRING; 6239.R12B2.4; -.
DR EPD; Q21952; -.
DR PaxDb; Q21952; -.
DR PeptideAtlas; Q21952; -.
DR PRIDE; Q21952; -.
DR EnsemblMetazoa; R12B2.4.1; R12B2.4.1; WBGene00001869.
DR GeneID; 175813; -.
DR KEGG; cel:CELE_R12B2.4; -.
DR UCSC; R12B2.4; c. elegans.
DR CTD; 175813; -.
DR WormBase; R12B2.4; CE01367; WBGene00001869; him-10.
DR eggNOG; ENOG502SZZC; Eukaryota.
DR HOGENOM; CLU_028990_0_0_1; -.
DR InParanoid; Q21952; -.
DR OMA; QCDTERQ; -.
DR OrthoDB; 1156184at2759; -.
DR PhylomeDB; Q21952; -.
DR SignaLink; Q21952; -.
DR PRO; PR:Q21952; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001869; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR GO; GO:0005874; C:microtubule; IDA:ComplexPortal.
DR GO; GO:0031262; C:Ndc80 complex; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; ISS:WormBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051383; P:kinetochore organization; IMP:WormBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:WormBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 1.10.418.60; -; 1.
DR InterPro; IPR005549; Kinetochore_Nuf2_N.
DR InterPro; IPR038275; Nuf2_N_sf.
DR Pfam; PF03800; Nuf2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..490
FT /note="Kinetochore protein Nuf2 homolog"
FT /id="PRO_0000249820"
FT REGION 346..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 146..280
FT /evidence="ECO:0000255"
FT COILED 310..407
FT /evidence="ECO:0000255"
FT MUTAGEN 109
FT /note="P->S: In e1511; reduces the fidelity of mitotic
FT chromosome segregation at 25 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:11402066"
SQ SEQUENCE 490 AA; 56722 MW; 7247744354F3E211 CRC64;
MSNVVLIVYD PRMISKYLGQ KLHMGLVADD IIKPTAEIAQ QIFANFVRLV LNVSESSLTT
LPLSANCDYD PELHKKSIPI IILFQCMKAF IKDNSGNKLD LTMCDLVTPA KHEHRFRKLT
SFLVDFLKLH ELATPAFNEI SEEFSDRKFE MEKIREELLE AEKKKNDLLA KQSIRKRHEH
ELINEQSNAK AELKNVVNEY TETRQINEEL DKQKEEAILH IQALEKEMLT GKKTIEHLNE
EVLTSPEQLK QEMEERKRHI EELRDCLESS KKGLQAKLEA REICINSEKN VPVIIEKIHQ
WTEVREVIID LIDVESENLR KLKEMEEQLD FMMKEMETAQ KRLVEQSETH EQLRIEHTQK
SEERQRRIEE ITEQIANLKT SQPDVSQEIA KKKQELLALK NAHSETISQI TNSCQDAVAK
FAKLNAMFKE TQKVAFEKNT AAAREMERLK SSLTGRLLSD YTFGSSTIDA GENTENCDPQ
PNDSSFSVFK
