KNL2_CAEEL
ID KNL2_CAEEL Reviewed; 877 AA.
AC O44548;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Kinetochore null protein 2 {ECO:0000305};
GN Name=knl-2 {ECO:0000312|WormBase:K06A5.4};
GN ORFNames=K06A5.4 {ECO:0000312|WormBase:K06A5.4};
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, INTERACTION WITH HCP-3, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17339379; DOI=10.1083/jcb.200701065;
RA Maddox P.S., Hyndman F., Monen J., Oegema K., Desai A.;
RT "Functional genomics identifies a Myb domain-containing protein family
RT required for assembly of CENP-A chromatin.";
RL J. Cell Biol. 176:757-763(2007).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26904949; DOI=10.1016/j.celrep.2016.01.065;
RA Lee B.C., Lin Z., Yuen K.W.;
RT "RbAp46/48(LIN-53) is required for holocentromere assembly in
RT Caenorhabditis elegans.";
RL Cell Rep. 14:1819-1828(2016).
RN [4] {ECO:0000305}
RP STRUCTURE BY NMR OF 617-678.
RA Osborne M.J., Borden L.B.;
RT "NMR solution structure of a MYB-like DNA binding domain of KNL-2 from C.
RT elegans.";
RL Submitted (APR-2014) to the PDB data bank.
CC -!- FUNCTION: Required for the recruitment of hcp-3, hcp-4, knl-1, bub-1
CC and lin-53 to kinetochores, kinetochore assembly, chromosome
CC condensation and chromosome segregation in meiosis and mitosis.
CC {ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:26904949}.
CC -!- SUBUNIT: Interacts with hcp-3. {ECO:0000269|PubMed:17339379}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17339379}.
CC Chromosome, centromere {ECO:0000269|PubMed:17339379}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:17339379}. Note=Requires
CC hcp-3 for chromatin localization. {ECO:0000269|PubMed:17339379}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis (at protein
CC level). {ECO:0000269|PubMed:17339379}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in absence of
CC hcp-3, hcp-4, knl-1, bub-1 and lin-53 at kinetochores (PubMed:17339379,
CC PubMed:26904949). Also causes defects in chromosome condensation and
CC aberrant meiotic and mitotic chromosome segregation (PubMed:17339379).
CC {ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:26904949}.
CC -!- SIMILARITY: Belongs to the KNL2 family.
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DR EMBL; BX284601; CCD68114.1; -; Genomic_DNA.
DR RefSeq; NP_491858.1; NM_059457.5.
DR PDB; 2M3A; NMR; -; A=617-678.
DR PDBsum; 2M3A; -.
DR AlphaFoldDB; O44548; -.
DR SMR; O44548; -.
DR IntAct; O44548; 6.
DR STRING; 6239.K06A5.4; -.
DR EPD; O44548; -.
DR PaxDb; O44548; -.
DR PeptideAtlas; O44548; -.
DR EnsemblMetazoa; K06A5.4.1; K06A5.4.1; WBGene00019432.
DR UCSC; K06A5.4; c. elegans.
DR WormBase; K06A5.4; CE26645; WBGene00019432; knl-2.
DR eggNOG; ENOG502TD1S; Eukaryota.
DR GeneTree; ENSGT00390000007395; -.
DR HOGENOM; CLU_361400_0_0_1; -.
DR InParanoid; O44548; -.
DR OMA; AITRLKW; -.
DR OrthoDB; 1328188at2759; -.
DR PRO; PR:O44548; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019432; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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.
DR Gene3D; 1.10.10.1900; -; 1.
DR InterPro; IPR044895; Knl-2_Myb-like_DNA-bd_sf.
DR InterPro; IPR039110; KNL2-like.
DR InterPro; IPR015216; SANTA.
DR PANTHER; PTHR16124; PTHR16124; 1.
DR Pfam; PF09133; SANTA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Kinetochore; Meiosis; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..877
FT /note="Kinetochore null protein 2"
FT /id="PRO_0000439236"
FT DOMAIN 20..107
FT /note="SANTA"
FT DOMAIN 617..678
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 122..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..211
FT /evidence="ECO:0000255"
FT COILED 491..549
FT /evidence="ECO:0000255"
FT COMPBIAS 154..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..877
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 625..638
FT /evidence="ECO:0007829|PDB:2M3A"
FT HELIX 644..654
FT /evidence="ECO:0007829|PDB:2M3A"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:2M3A"
FT HELIX 662..672
FT /evidence="ECO:0007829|PDB:2M3A"
SQ SEQUENCE 877 AA; 101203 MW; 836AC7FEB5AB6A5D CRC64;
MGDTEIVPLR VQNVLDSEII RLNLWSMKFN ATSFKLEGFV RNEEGTMMQK VCSEFICRRF
TSTLLFDVSG RFFDLVGQID REYQQKMGMP SRIIDEFSNG IPENWADLIY SCMSANQRSA
LRPIQQAPKE PIRTRTEPIV TLADETELTG GCQKNSENEK ERNRREREEQ QTKERERRLE
EEKQRRDAEA EAERRRKEEE ELEEANYTLR APKSQNGEPI TPIRFTRGHD NGGAKKVFIF
EQTPVRKQGP IASSTPQQKQ RLADGANNQI PPTQKSQDSV QAVQPPPPRP AARNAQFASD
ADLFAVPKAP PSKSVRNLAA SNVDIFADVD SVLDTFHFES TPGRVRKPGR RNVSSPSPEP
RHRSSSRDGY EQSRYSQRYE HDNSRWSRHN ATYRRHEDES RMSRKRSIVR DDFEYSRRHD
DGARRRDYYD ADIQGDSKRY RGRDASSSSG RSVRFEEEHR RHGDEYRDPR GPRDYNDYGR
RRNHANSRSG EDEEKLNAIV RREKELRNRL QKSQKASSSS YRHRSNSSDA EESLNEWDIE
NQELLDNSMM FGDGIPKRSN ARKDKFVKKQ ATRSKPANST KSPAQARKKK RASLEDNRDL
NDSIACNRPR RSCVTPVAKK ITWRKQDLDR LKRVIALKKP SASDADWTEV LRLLAKEGVV
EPEVVRQIAI TRLKWVEPEQ NEEVLKQVEE VEQKRRRGAV ARVKENVKMH EELREGGNHR
AEDLQSGVES MEDYQPEDVA ADQSLLALRT PIVTKKRGGT RASIMPKPVE DSPMSRGNNS
TFNSPRLEQT KAKDIETNFK YVQHLSMMQA RPSSRLKKSS SMNNSTYRGN KNTSISLEKG
TQKALKIINR GTTIHEDDEN EDNDDDDDMR EEDTSIY
