ID   KNTC1_MOUSE             Reviewed;        2207 AA.
AC   Q8C3Y4; Q6A0B3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Kinetochore-associated protein 1;
GN   Name=Kntc1; Synonyms=Kiaa0166;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 839-843 AND 1650-1657, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1484-2207.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC       cells from prematurely exiting mitosis. Required for the assembly of
CC       the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its
CC       function related to the spindle assembly machinery is proposed to
CC       depend on its association in the mitotic RZZ complex (By similarity).
CC       {ECO:0000250|UniProtKB:P50748}.
CC   -!- SUBUNIT: Interacts with ZW10. This interaction is required for stable
CC       association with the kinetochore. Component of the RZZ complex composed
CC       of KNTC1/ROD, ZW10 and ZWILCH (By similarity).
CC       {ECO:0000250|UniProtKB:P50748}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50748}. Nucleus
CC       {ECO:0000250|UniProtKB:P50748}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:P50748}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:P50748}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK172905; BAD32183.1; ALT_INIT; mRNA.
DR   EMBL; AK084529; BAC39211.1; -; mRNA.
DR   CCDS; CCDS39274.1; -.
DR   RefSeq; NP_001035886.1; NM_001042421.1.
DR   AlphaFoldDB; Q8C3Y4; -.
DR   BioGRID; 228995; 6.
DR   IntAct; Q8C3Y4; 3.
DR   MINT; Q8C3Y4; -.
DR   STRING; 10090.ENSMUSP00000031366; -.
DR   iPTMnet; Q8C3Y4; -.
DR   PhosphoSitePlus; Q8C3Y4; -.
DR   EPD; Q8C3Y4; -.
DR   MaxQB; Q8C3Y4; -.
DR   PaxDb; Q8C3Y4; -.
DR   PeptideAtlas; Q8C3Y4; -.
DR   PRIDE; Q8C3Y4; -.
DR   ProteomicsDB; 263673; -.
DR   Antibodypedia; 9885; 125 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000031366; ENSMUSP00000031366; ENSMUSG00000029414.
DR   GeneID; 208628; -.
DR   KEGG; mmu:208628; -.
DR   UCSC; uc008zoo.1; mouse.
DR   CTD; 9735; -.
DR   MGI; MGI:2673709; Kntc1.
DR   VEuPathDB; HostDB:ENSMUSG00000029414; -.
DR   eggNOG; KOG4256; Eukaryota.
DR   GeneTree; ENSGT00390000007883; -.
DR   HOGENOM; CLU_231522_0_0_1; -.
DR   InParanoid; Q8C3Y4; -.
DR   OMA; QIEMAYE; -.
DR   OrthoDB; 122381at2759; -.
DR   PhylomeDB; Q8C3Y4; -.
DR   TreeFam; TF101176; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 208628; 17 hits in 74 CRISPR screens.
DR   ChiTaRS; Kntc1; mouse.
DR   PRO; PR:Q8C3Y4; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8C3Y4; protein.
DR   Bgee; ENSMUSG00000029414; Expressed in manus and 154 other tissues.
DR   ExpressionAtlas; Q8C3Y4; baseline and differential.
DR   Genevisible; Q8C3Y4; MM.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005828; C:kinetochore microtubule; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:1990423; C:RZZ complex; ISO:MGI.
DR   GO; GO:0000922; C:spindle pole; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISO:MGI.
DR   GO; GO:1903394; P:protein localization to kinetochore involved in kinetochore assembly; IBA:GO_Central.
DR   InterPro; IPR019527; RZZ-complex_KNTC1/ROD_C.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF10493; Rod_C; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Kinetochore; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..2207
FT                   /note="Kinetochore-associated protein 1"
FT                   /id="PRO_0000084313"
FT   REGION          1024..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        2187
FT                   /note="G -> E (in Ref. 3; BAC39211)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2207 AA;  250358 MW;  CE217F32714D83D0 CRC64;
     MWNNIELLTS DDTGSGCLSV GSRKENVTAL YQADLLGKIS SEKTSLSPKI QAFSLSHGFI
     IVADQSVILL DSICRSLQLF LIFDTDVDVV GLCQEGKFLF VGERSGNFHL IYVTSKQTLF
     TKAFVEKALD ESQRTYRNLI IEKDGSNEGT YYMLLLTNNG FFYITNLQLS QIEQAIENTD
     LDSAKKLQGQ FKCSFISTEN YHSCLSLVAS QSGTFASKTS VIIGGTGSCA FSKWEPDSTK
     KEMSLKNFVG TDIIKGAKSF QLIDNLLFVL DTDNVLSLWD AYTLTPVWNW PSLPVEQFVL
     TTEADSPSSV TWQGITNLKL VTLTATAKEK MRSLIIYSLP SMETLYSLEV SSVSSLVQTG
     ISTDTIYLLE GIHKNDPNLC EDSVSDLVLR YLTEVLPENR LSRLLHKHRF AEAESFAIQF
     GLDVELVYKV KSNDMLEKLA LISSDKSEQS KWQQLVDEAK ENLCKIQDDD FVVNFCLKAQ
     WVTYETTQEM LSYAKTRLMK KEDRALPASS DAFMEVLKAH AKLTTFYGAF GPEKFSGSSW
     IEFLNNEDDL RDVFLQLSEG NFACAQYLWL RHRADFESKF DVKMLENLLN SISTQFPLEN
     LCSWFKNEVI PFVRRIVPEG QNILAKWLEQ ASRNLELTDK ANWPENGLQL AEVFFTAEKT
     DRFGFASSWH WISLDYQNTE EVRQLRTLVS KLRELIILHR KYNCKLALSD FEKENATTVV
     FRMFDRVSAP ELIPSVLEKS VRVYIREQNL QEEELLLLYI EDLLKRCSSK SMTLFDTAWE
     AKAMAVIRCL SDTDLIFDAV LKIMYKAVVP WSAAVEQLVK QHLEMDHPKV KLLQESYKLM
     EMKKLLRGYG IREVNLLNKE IMRVIRYILK QDIPSSLEDA LKVAQGYRLS DDEIYSLRII
     DLIDREQGGD CLLLLKSLPA AEAEKTAERV IIWARLALQE EPDGSEEDKA WRISVAKTSV
     DILKILCDIR KDNLQKKDES EEFLKRFQMV ASLQENFEVF LPFEDYSNTA LVAGLREQYI
     KAQEAAQAEH KHRGPPGPTP ARGTHLSIKS KLHRQALALQ VSEQELEAEL TLRALKDGKV
     VAALSKCRDL LKHYCNADTG RLLFVVCQKL CQMLADDVPM VAPGGLSLPS EIHDLACHAV
     TICSPDYLLD VLELSKYTLT AVELCRQCQM DDCGMLMKAA LGTHKDPYEE WSFSDFFSED
     GIVLESQVVL PVIYELISSV MPPAESKRHP LDSISLPYCS TSEGENRILP LVSSISALLR
     SLQECSQWEL ALRFVVGSFG TCLQHSMSNV MSISLSKQLL GKNTLANSRH IIMELKEKSI
     TFIRENATTL LHKVFNCRVV DLDLALAYCT LLPQKDVFDN LWKFIDKAWQ NYDKILALSL
     VGSQLANLYQ DIETGLWFHE LSIDAKWGIR LGKLGISFQP AFRQNFLTKK DLIKALVNNI
     DMDTSLILEY CSTFQLDSDA ALRLFIETLL RNTSSQSQGD AAPESTKHQH SKLLAKATEL
     VPLLKNTKDL VISLSEILYK LDPYDYEMID VVLKVLEQAN EKITSVNINQ ALNLLRHLKS
     YRRISPPVDH EYQYALEHMI TLPPAAHTRL PFHLILFGTA QNFWKILSSE LSEESLPTLL
     LIAKLMKFSL DTLYVSTAKH LFEKNLKPKL LKSAQARSST LMSKEVDKLM QTLESYLLSI
     VNPEWAVAIA ISLTQEVPEG PFKMSSLKFC LYLAERWLQN IPPQDETCEK AKALQKKLCL
     QVRLSGTEAV LIAHKLNDQE YLRVIGKPAH LIVSLYEHPS ISERLCTTSG KDYPDIHTAA
     KEIAEVNEVN LEKIWDMLLE KWLCPSTVPS EKASEFFELE EDEVLHRVVY LLQARPVDYC
     SRMLFVFATS ATSTLGMRQL TFAHKARALQ CLLYLADKET IESLFKKPIK EMKSYLKCIT
     FLASFETLNI PITYELFCNS PKEGMIKGLW KNHSHEPMAV RLVAELCLEY KIYDLQLWNG
     LLQKLLGFNM IPYLRKVLSC ISSIHSLWQV PYFSKAWQRV IQIPLLSASC PLRPSQLADC
     CDSLVAILEC PVSDDLDMMG VAKQYVQLDL PAFALTCLTL MPHSEKRHQQ IKNFLNSCDA
     RIILQQIEEH MNTGQLAGFS HQIGSLVLNH VVNKKEFGIL AKTKYFQLLK CHVINTGNVT
     ELVNYLANDF SVDEASALIN EYSKHCGKPV PADAAPCEIL QTFLGGS