KNL1_CAEBR
ID KNL1_CAEBR Reviewed; 957 AA.
AC A8WL28;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Kinetochore null protein 1 {ECO:0000250|UniProtKB:P34278};
GN Name=knl-1 {ECO:0000312|EMBL:CAP21173.1}; ORFNames=CBG24615;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP21173.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP21173.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Proposed to be part of the KMN network incorporating the
CC MIS12 complex and NDC80 complex that is required for establishing the
CC kinetochore-microtubule interface that aids in chromosome segregation
CC during meiotic and mitotic cell division. Appears to function
CC downstream of hcp-3 (CENP-A) and hcp-4 (CENP-C) in the kinetochore
CC assembly hierarchy. Has a role in the correct localization of spdl-1
CC and the RZZ complex that is composed of rod-1, czw-1 and zwl-1.
CC Required for the recruitment of spindle-assembly checkpoint components
CC bub-1 and mdf-1/2 to unattached kinetochores (By similarity).
CC {ECO:0000250|UniProtKB:P34278}.
CC -!- SUBUNIT: Interacts with hcp-3 and hcp-4 to form a complex. Interacts
CC with hcp-4, him-10, kbp-3, kbp-4, kbp-5, knl-3, and ndc-80. Interacts
CC with kbp-1, kbp-2 and mis-12; which make up the MIS12 complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:P34278}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P34278}. Note=Also found on the surface of
CC chromosomes. Subcellular localization dependent on expression of hcp-3,
CC hcp-4 and knl-3. During anaphase of meiosis I, localized also to
CC spindle-associated rod-shaped structures which depends on zwl-1 (By
CC similarity). {ECO:0000250|UniProtKB:P34278}.
CC -!- DOMAIN: The N-terminus contains a number of repeats which contribute
CC additively to bub-1 recruitment to unattached kinetochores. The repeats
CC are not required for localization to kinetochores (By similarity).
CC {ECO:0000250|UniProtKB:P34278}.
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DR EMBL; HE601354; CAP21173.1; -; Genomic_DNA.
DR RefSeq; XP_002641315.1; XM_002641269.1.
DR AlphaFoldDB; A8WL28; -.
DR SMR; A8WL28; -.
DR STRING; 6238.CBG24615; -.
DR EnsemblMetazoa; CBG24615.1; CBG24615.1; WBGene00042685.
DR GeneID; 8583307; -.
DR KEGG; cbr:CBG_24615; -.
DR CTD; 8583307; -.
DR WormBase; CBG24615; CBP12964; WBGene00042685; Cbr-knl-1.
DR eggNOG; ENOG502TGNI; Eukaryota.
DR HOGENOM; CLU_296876_0_0_1; -.
DR InParanoid; A8WL28; -.
DR OMA; NDTMAVF; -.
DR OrthoDB; 1487822at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Cytoplasm; Kinetochore; Meiosis; Mitosis; Reference proteome;
KW Repeat.
FT CHAIN 1..957
FT /note="Kinetochore null protein 1"
FT /id="PRO_0000383651"
FT REPEAT 87..90
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 109..112
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 206..209
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 251..254
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 282..285
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 326..329
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 367..370
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 390..393
FT /note="8"
FT /evidence="ECO:0000305"
FT REGION 87..393
FT /note="8 X 4 AA repeats of M-[D/E]-[I/L/M]-[S/T]"
FT /evidence="ECO:0000305"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 830..950
FT /evidence="ECO:0000255"
SQ SEQUENCE 957 AA; 105839 MW; 07DFD18A9115C0A8 CRC64;
MDNQRKKRNS ILKVRQETNL MDVLEDTTVA TSSGATNRRV SFHQLKQVKN YDRAGGQIID
ATPIKEKAYD TMSSDGNSTS HTTRLDMDIT GLNSTPVTPK TQTPFNGSMD MSVENYDETA
RLFDITRDKT ICVYEKTVET TTTKVVERVV RVPEGSSGAN NDTLALFNMT DRAEVDMSVD
GGSEGALKVD DTISVFNQTN VEPVDMDITV QKPLDDTMGV FRSPAIPTSS RIQKTSASTM
DSQNMSMSMD MDITSNEMMA AFKSPKIMSS VLVAAVKDSD DMDLTGLVNT AAEDVADDTM
AVFRTPTRAQ TTIQKTSGEI PESVDMEMTG IGNSDAPDDT MAVFRTPTRA QQTVQKTSGE
IPESVDMEMT LLALLQPVSD VKDNFDDVAM DITQQTLVGV SDDTMAVFKN PAAEKKTPGK
PLFDESMEIE STIVCPDNVT FSETAQPENP AYHSSMLMSM ASEVSEDVVV QKTSESLQQS
SMRMSTTITE DVTASKNPES STISEVQKIP EVVQKTSNGV EDIQNASETP EDVSMEITSE
VVEGERGTMY QMSTMDVDSL QKTSLASPKI QMTSFTDTSE KMGGVSETSL IQTMMIEASE
SMECSEAPED VTASPEGLTM APEDVTVASN VSGIVSVSSI SRRRRSQLQE SLHRESPRRM
ALEKNLSMMS QMGGASEALA EFRQNKLKNQ TTLLNDSVNT TIGANTSESI GRDIFKMNTS
IRSPAHRSST APSPMVSKTL PESPKFHVTP FDAAIVNVIY LTPEDAETQE PIPEAFEFEK
VLSAEESNVH KEIDTANWSI SGAIKSNLDA EVMNIARGQA EMKFLELRGK FAKESNVEIA
QKIQELESQN LELAGKIRDS QNLRVLQKQI EELQKPQFSL EEAERIENEY HETKVELLRA
QAASIRRQHE LLMTIREERR RLIHEIEEKD ELLARLEEED RKKKEEMVER VRGVMRA
