KNTC1_CAEEL
ID KNTC1_CAEEL Reviewed; 2049 AA.
AC Q20849;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Kinetochore-associated protein rod-1 {ECO:0000305};
DE AltName: Full=Rough deal homolog {ECO:0000312|WormBase:F55G1.4};
GN Name=rod-1 {ECO:0000312|WormBase:F55G1.4};
GN ORFNames=F55G1.4 {ECO:0000312|WormBase:F55G1.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11590237; DOI=10.1242/jcs.114.17.3103;
RA Scaeerou F., Starr D.A., Piano F., Papoulas O., Karess R.E., Goldberg M.L.;
RT "The ZW10 and Rough Deal checkpoint proteins function together in a large,
RT evolutionarily conserved complex targeted to the kinetochore.";
RL J. Cell Sci. 114:3103-3114(2001).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN RZZ COMPLEX, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18765790; DOI=10.1101/gad.1687508;
RA Gassmann R., Essex A., Hu J.-S., Maddox P.S., Motegi F., Sugimoto A.,
RA O'Rourke S.M., Bowerman B., McLeod I., Yates J.R. III, Oegema K.,
RA Cheeseman I.M., Desai A.;
RT "A new mechanism controlling kinetochore-microtubule interactions revealed
RT by comparison of two dynein-targeting components: SPDL-1 and the
RT Rod/Zwilch/Zw10 complex.";
RL Genes Dev. 22:2385-2399(2008).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19109417; DOI=10.1091/mbc.e08-10-1047;
RA Essex A., Dammermann A., Lewellyn L., Oegema K., Desai A.;
RT "Systematic analysis in Caenorhabditis elegans reveals that the spindle
RT checkpoint is composed of two largely independent branches.";
RL Mol. Biol. Cell 20:1252-1267(2009).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH NDC-80.
RX PubMed=24231804; DOI=10.1126/science.1246232;
RA Cheerambathur D.K., Gassmann R., Cook B., Oegema K., Desai A.;
RT "Crosstalk between microtubule attachment complexes ensures accurate
RT chromosome segregation.";
RL Science 342:1239-1242(2013).
CC -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC cells from prematurely exiting mitosis (PubMed:11590237,
CC PubMed:18765790). Required for chromosome segregation, the assembly of
CC the dynein-dynactin and mdf-1-mdf-2 complexes onto kinetochores and
CC spindle pole separation (PubMed:18765790, PubMed:19109417). Plays a
CC role in nuclear envelope breakdown (PubMed:19109417). Its function
CC related to the spindle assembly machinery and kinetochore-microtubule
CC attachments likely depends on its association in the mitotic RZZ
CC complex (PubMed:18765790, PubMed:24231804). The RZZ complex recruits
CC the spindly-like protein spdl-1 to kinetochores (PubMed:18765790,
CC PubMed:24231804). To prevent irregular chromosome segregation, the
CC complex also inhibits the attachment of the kinetochore-associated
CC NDC80 complex to microtubules (PubMed:24231804). The recruitment of
CC spdl-1 to kinetochores relieves this inhibition (PubMed:24231804).
CC Required for embryonic development (PubMed:11590237, PubMed:18765790,
CC PubMed:19109417). {ECO:0000269|PubMed:11590237,
CC ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:19109417,
CC ECO:0000269|PubMed:24231804}.
CC -!- SUBUNIT: Component of the RZZ complex composed of rod-1, czw-1 and zwl-
CC 1 (PubMed:18765790). Interacts (via N-terminus) with NDC80 complex
CC component ndc-80 (PubMed:24231804). {ECO:0000269|PubMed:18765790,
CC ECO:0000269|PubMed:24231804}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000305|PubMed:18765790}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P50748}. Note=Localizes to the kinetochore
CC during nuclear envelope breakdown and remains there until the
CC metaphase-anaphase transition. Localization of the RZZ complex to
CC kinetochores is dependent upon knl-1. {ECO:0000305|PubMed:18765790}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality (PubMed:11590237, PubMed:18765790, PubMed:19109417). RNAi-
CC mediated knockdown results in defects in mitosis which include the
CC formation of chromatin bridges in between sister chromatids during
CC anaphase (PubMed:11590237). There is also defective chromosome
CC segregation, premature spindle pole separation and incorrectly attached
CC kinetochores (PubMed:18765790). In addition, localization of the
CC spindly-like protein spdl-1 and the other Rzz complex components czw-1
CC and zwl-1 to the kinetochore is abolished (PubMed:18765790).
CC {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:18765790,
CC ECO:0000269|PubMed:19109417}.
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DR EMBL; BX284604; CCD69392.1; -; Genomic_DNA.
DR PIR; T29227; T29227.
DR RefSeq; NP_501200.1; NM_068799.5.
DR AlphaFoldDB; Q20849; -.
DR ComplexPortal; CPX-810; Rzz complex.
DR STRING; 6239.F55G1.4; -.
DR EPD; Q20849; -.
DR PaxDb; Q20849; -.
DR PeptideAtlas; Q20849; -.
DR EnsemblMetazoa; F55G1.4.1; F55G1.4.1; WBGene00018900.
DR GeneID; 177520; -.
DR KEGG; cel:CELE_F55G1.4; -.
DR UCSC; F55G1.4; c. elegans.
DR CTD; 177520; -.
DR WormBase; F55G1.4; CE07281; WBGene00018900; rod-1.
DR eggNOG; KOG4256; Eukaryota.
DR GeneTree; ENSGT00390000007883; -.
DR HOGENOM; CLU_232474_0_0_1; -.
DR InParanoid; Q20849; -.
DR OMA; EYAKFAM; -.
DR OrthoDB; 30020at2759; -.
DR PRO; PR:Q20849; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00018900; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005828; C:kinetochore microtubule; IBA:GO_Central.
DR GO; GO:1990423; C:RZZ complex; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0090268; P:activation of mitotic cell cycle spindle assembly checkpoint; IGI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IGI:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:1905561; P:positive regulation of kinetochore assembly; IGI:UniProtKB.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IGI:UniProtKB.
DR GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IMP:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IMP:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IDA:ComplexPortal.
DR GO; GO:1903394; P:protein localization to kinetochore involved in kinetochore assembly; IMP:UniProtKB.
DR GO; GO:1902423; P:regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:WormBase.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Kinetochore; Mitosis; Reference proteome.
FT CHAIN 1..2049
FT /note="Kinetochore-associated protein rod-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438726"
SQ SEQUENCE 2049 AA; 233823 MW; 0262B439B5D9F3AF CRC64;
MGRLGEAKAV DLEAETSTVG LYDVCTVGRI LPLLNEMSID KKSPAWKLKP KSNERFLVLA
SCSDLAVFSL GEKSDYSFNT GLGGAITDFE ILGSSSFFVG VIEHRRIVIL SLDKQEIYLN
EPAPHEIDFV VCHTTSSVCQ LIFGSRSDNW HTITLPGDVA ASKETNRFEN WHRDQIQEFF
HQAMGKTVSK SVDMSKVAGD ITLISNGPLQ TFASIDQQRG IHWCGLVESE FEVIGMEKQF
LQVRDGGRFS LHLDTDGWIH VFDSLVSSFC HEFDMKMSPD DKILDFVIID KNEVEVPKMF
AILVLPRDGD STKMMIYDRL NKDNCFALDS STSTTLFAYG GSDRVLIAVE ELENSLADEQ
DGSQIVVRQV SQSRPEMRFE SLLKNNRFEE AEKFAMAFML DVQKVYKGHV HYLMDSCDES
DESFETLMTK MGQIQDHNMV AETYFTLVGM SRRCDRIRTY LTHAKKRRIT DLDILKMIEA
LCYTWGTYRI IAGPEENEPS RPQVNETIWD LFVEALHDAN PWIEIYNEFI SDAQFTQARV
IFSRHGKSIT DYMCDDEENT ISRLETLFRM FIDAISSDIS KWSNVIEHVT TDILPACVMI
TEELIPCLES LITSLISLLE YRDSTNWPEN AIKAASSYDT MTKILSNNGN TPATQCILVM
YGSKLGSSAG NKPSSMSRIK KIYYDLIELK RLKDVYECSI SFSVFQNMSS EQICHKILQN
ALANPNMTHA KIEKFVKPFM AERHLDQEQT IVNYIQMMSG AAVTNANLFG WEKQCVQLCA
SLMDETRRCC SIISIASTAK IPWPAELNEA VEKILASRTL LRSEIEQMHL VCKRTELYKM
LSSYGFSRQD IELLTTPDSN MDIILTIRCM LAHREKASRF VDVIKLVDLL KAMQGSSQPR
TLRIEYVQSF AIIHMMSHQD VTISIINYID SLGDRERVKT ISLVFSFIEC VANAPATGDN
VLEREKILGV GEELMSHYTC RDNNFNDPER RLKDELVLLR EVQKTETKAV LLSELKDEDW
QRRFLERLIE SNSSMSLNLG RCSYMGISPE HLIEMILTKA TVENDMDTIV DSITNYVEFI
NSLTDSSREM LEPIVQILSW ITFRLPKLLP NETEMARADY IAFVVKRIGR VVRETLRRFS
FDVISDDLDY LLQLEAFYHL GEHIIKQSLR GQENENEKQE MFRSDDDTFL PTDSSNPFSN
QSSLRIFEFK RPLGTFDFSN DPALFEGVQG VLALAMVAPS VARPYDSEIS PDDANEFRSS
WEQLNMFLAM HSQDLLDISA RVFAGSLKCW AGEYLQGIVE MEQPILSVVE RMLQQKKFDF
WHAVTLLGGI PLERLDRAII DLQKRQGVRS STKATIQYLQ LAFVMSLLAR NMEKVPTIVS
AYEQKYLVKK LAEEGIRVSI TQDFVDKVLQ QAIDLRQPLS PLRLHDYVKK YVEKLIRNSK
ISVGEYMVRY ATLLIRKASV AGRHTDREIR KEEIEKYIEA ARIALRIAEE EDASCICNYL
HCLLYVVCPY NYEVIQFIVT SYGKYATETV EIEFNKNLKS IMAFLWAYQR TNHISNEESI
WFTKRESVLM KDEKEFEKTG RMLDPFGHSL RVVYEDDGSN MSDSYNSDLA LSSDAMVYER
NSVIISDLPS LAEQYLPFHA FLLRKKEEID EIVMGIVKAE LSIFNVPIWQ TFLREVSWLS
SRFSRSQLLS SAIFAHANKY AKFGKSLPDG ERNVIYELLN SASQRHVVVS TIALLFKRII
LSDVKIELLQ MGVNISERWT SDLTGEEQQE MEEQSARLKD GIAKFSTELE LKKNGLYNEK
TADNIENVSE LCSLIYNEMV QWDDSRDVLK KCQVVDKIAK ANGLDLTALH EQLVFSWVED
TQTIISINHV DMNESIGGTS FLDHKDETDD QNDLRIPLFD GILDKVVVLC QRIDKKRLLT
RLGSILMRGG RKATGGYTAV VRATCIILRS FTDTEVSELL SGADMFALCS TLENQLYERL
FEKAEVKGDC KTDKMQLIKS LLQCPSRTHP MTALIACLII DHEFKDPKRD ISLGWDVGCV
PVSANSSNS
