SPC25_DROME
ID SPC25_DROME Reviewed; 222 AA.
AC Q9V3V7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Kinetochore protein Spc25 {ECO:0000303|PubMed:17895365, ECO:0000312|EMBL:AAF54875.1};
DE AltName: Full=Chromosome alignment defect 2 {ECO:0000303|PubMed:17412918};
DE AltName: Full=Mitotic chaos {ECO:0000303|PubMed:17895365};
GN Name=Spc25 {ECO:0000312|FlyBase:FBgn0087021};
GN Synonyms=Cal2 {ECO:0000303|PubMed:17412918},
GN mitch {ECO:0000303|PubMed:17895365}; ORFNames=CG7242;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF37563.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17895365; DOI=10.1242/jcs.012112;
RA Williams B., Leung G., Maiato H., Wong A., Li Z., Williams E.V.,
RA Kirkpatrick C., Aquadro C.F., Rieder C.L., Goldberg M.L.;
RT "Mitch a rapidly evolving component of the Ndc80 kinetochore complex
RT required for correct chromosome segregation in Drosophila.";
RL J. Cell Sci. 120:3522-3533(2007).
RN [2] {ECO:0000312|EMBL:AAF54875.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF54875.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAK93305.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93305.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NDC80 AND NUF2, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17333235; DOI=10.1007/s00412-007-0103-y;
RA Schittenhelm R.B., Heeger S., Althoff F., Walter A., Heidmann S.,
RA Mechtler K., Lehner C.F.;
RT "Spatial organization of a ubiquitous eukaryotic kinetochore protein
RT network in Drosophila chromosomes.";
RL Chromosoma 116:385-402(2007).
RN [6] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=17412918; DOI=10.1126/science.1141314;
RA Goshima G., Wollman R., Goodwin S.S., Zhang N., Scholey J.M., Vale R.D.,
RA Stuurman N.;
RT "Genes required for mitotic spindle assembly in Drosophila S2 cells.";
RL Science 316:417-421(2007).
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 during meiosis and mitosis (PubMed:17895365,
CC PubMed:17333235). Required for kinetochore integrity and the
CC organization of stable microtubule binding sites in the outer plate of
CC the kinetochore (PubMed:17895365, PubMed:17333235). Participates in SAC
CC signaling that responds specifically to disruptions in spindle
CC microtubule dynamics (PubMed:17333235). The NDC80 complex
CC synergistically enhances the affinity of the SKA1 complex for
CC microtubules and may allow the NDC80 complex to track depolymerizing
CC microtubules (By similarity). {ECO:0000250|UniProtKB:Q9HBM1,
CC ECO:0000269|PubMed:17333235, ECO:0000269|PubMed:17895365}.
CC -!- SUBUNIT: Component of the Ndc80 complex, which is composed of Ndc80,
CC Nuf2 and Spc25. {ECO:0000269|PubMed:17333235}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17333235,
CC ECO:0000269|PubMed:17895365}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:17333235, ECO:0000269|PubMed:17895365}.
CC Note=Independent of microtubules (MTs) and several other known
CC kinetochore components. Ndc80 complex has polar orientation along the
CC spindle axis. {ECO:0000269|PubMed:17333235,
CC ECO:0000269|PubMed:17895365}.
CC -!- DISRUPTION PHENOTYPE: Die as late third-instar larvae. Mitotic
CC neuroblasts in larval brains exhibit high levels of aneuploidy:
CC chromosome alignment is compromised during spindle formation, many
CC chromosomes display persistent mono-orientation which leads to
CC aneuploidy during anaphase. Chromosome behavior is also disrupted
CC during both meiotic divisions in spermatocytes: the entire chromosome
CC complement often moves to only one spindle pole.
CC {ECO:0000269|PubMed:17333235, ECO:0000269|PubMed:17895365}.
CC -!- SIMILARITY: Belongs to the SPC25 family. {ECO:0000255}.
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; AF219224; AAF37563.1; -; mRNA.
DR EMBL; AE014297; AAF54875.1; -; Genomic_DNA.
DR EMBL; AY051881; AAK93305.1; -; mRNA.
DR RefSeq; NP_650239.1; NM_141982.3.
DR AlphaFoldDB; Q9V3V7; -.
DR SMR; Q9V3V7; -.
DR BioGRID; 66674; 18.
DR STRING; 7227.FBpp0082158; -.
DR PaxDb; Q9V3V7; -.
DR PRIDE; Q9V3V7; -.
DR DNASU; 41585; -.
DR EnsemblMetazoa; FBtr0082690; FBpp0082158; FBgn0087021.
DR GeneID; 41585; -.
DR KEGG; dme:Dmel_CG7242; -.
DR UCSC; CG7242-RA; d. melanogaster.
DR CTD; 57405; -.
DR FlyBase; FBgn0087021; Spc25.
DR VEuPathDB; VectorBase:FBgn0087021; -.
DR eggNOG; ENOG502RVT8; Eukaryota.
DR HOGENOM; CLU_1246541_0_0_1; -.
DR InParanoid; Q9V3V7; -.
DR OMA; SNELMEC; -.
DR OrthoDB; 1350883at2759; -.
DR PhylomeDB; Q9V3V7; -.
DR BioGRID-ORCS; 41585; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41585; -.
DR PRO; PR:Q9V3V7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0087021; Expressed in secondary oocyte and 14 other tissues.
DR Genevisible; Q9V3V7; DM.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0031262; C:Ndc80 complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR GO; GO:0051311; P:meiotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:FlyBase.
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..222
FT /note="Kinetochore protein Spc25"
FT /id="PRO_0000392420"
FT COILED 51..86
FT /evidence="ECO:0000255"
SQ SEQUENCE 222 AA; 25742 MW; 55C832D4CC75DDC0 CRC64;
MAIIMTESSY ERRVKALYEK QIHMEALEAK FIKKVFKFNS NLLDVKEAAS RHQRKVGKLQ
KVLMERREEL DKRVSFIEEL DRELEATKLH NLAMKDWFKQ QKMLAKQRKN EIMESIHTLS
KTTRTYINQE ALPARVKGVT VLRGDKRDQL IPFDLKATDV EGLDSLCQHL ESLNVDVAQW
QQLISLAMDM AMESRAPTTP PKEADNCKSI IEIDLTSPMS HT
