CENPC_ARATH
ID CENPC_ARATH Reviewed; 705 AA.
AC Q66LG9; Q68BI6; Q68BI7; Q9M9D0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Centromere protein C {ECO:0000303|PubMed:15329494};
DE Short=AtCENP-C {ECO:0000303|PubMed:15329494};
DE Short=CENP-C {ECO:0000303|PubMed:15329494};
DE Short=CENP-C homolog {ECO:0000303|PubMed:15329494};
GN Name=CENPC {ECO:0000303|PubMed:15329494};
GN OrderedLocusNames=At1g15660 {ECO:0000312|Araport:AT1G15660};
GN ORFNames=T16N11.16 {ECO:0000312|EMBL:AAF71990.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Flower bud, and Green siliques;
RX PubMed=15329494; DOI=10.1266/ggs.79.139;
RA Ogura Y., Shibata F., Sato H., Murata M.;
RT "Characterization of a CENP-C homolog in Arabidopsis thaliana.";
RL Genes Genet. Syst. 79:139-144(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RX PubMed=15345035; DOI=10.1186/jbiol11;
RA Talbert P.B., Bryson T.D., Henikoff S.;
RT "Adaptive evolution of centromere proteins in plants and animals.";
RL J. Biol. 3:18.1-18.17(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15161939; DOI=10.1242/jcs.01144;
RA Shibata F., Murata M.;
RT "Differential localization of the centromere-specific proteins in the major
RT centromeric satellite of Arabidopsis thaliana.";
RL J. Cell Sci. 117:2963-2970(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=26124146; DOI=10.1073/pnas.1506351112;
RA Batzenschlager M., Lermontova I., Schubert V., Fuchs J., Berr A.,
RA Koini M.A., Houlne G., Herzog E., Rutten T., Alioua A., Fransz P.,
RA Schmit A.C., Chaboute M.E.;
RT "Arabidopsis MZT1 homologs GIP1 and GIP2 are essential for centromere
RT architecture.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:8656-8660(2015).
CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC complex that plays a central role in assembly of kinetochore proteins,
CC mitotic progression and chromosome segregation.
CC {ECO:0000250|UniProtKB:Q03188}.
CC -!- SUBUNIT: Oligomer. Component of the CENPA-NAC complex.
CC {ECO:0000250|UniProtKB:Q03188}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:15329494}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:15161939}. Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00768, ECO:0000269|PubMed:15329494,
CC ECO:0000269|PubMed:26124146}. Note=Present at the centromeric regions,
CC especially in the kinetochore domain, throughout the cell cycle.
CC {ECO:0000269|PubMed:15161939, ECO:0000269|PubMed:15329494}.
CC -!- DOMAIN: The MIF2 homology domain II targets centromeres and binds the
CC alpha satellite DNA in vivo. {ECO:0000250|UniProtKB:Q03188}.
CC -!- SIMILARITY: Belongs to the CENP-C/MIF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71990.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AB128986; BAD42453.1; -; mRNA.
DR EMBL; AB128987; BAD42454.1; -; mRNA.
DR EMBL; AY693798; AAU04629.1; -; mRNA.
DR EMBL; AC013453; AAF71990.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29346.1; -; Genomic_DNA.
DR PIR; F86290; F86290.
DR RefSeq; NP_173018.2; NM_101434.4.
DR AlphaFoldDB; Q66LG9; -.
DR STRING; 3702.AT1G15660.1; -.
DR PaxDb; Q66LG9; -.
DR PRIDE; Q66LG9; -.
DR ProteomicsDB; 220607; -.
DR EnsemblPlants; AT1G15660.1; AT1G15660.1; AT1G15660.
DR GeneID; 838135; -.
DR Gramene; AT1G15660.1; AT1G15660.1; AT1G15660.
DR KEGG; ath:AT1G15660; -.
DR Araport; AT1G15660; -.
DR TAIR; locus:2196578; AT1G15660.
DR eggNOG; ENOG502QR44; Eukaryota.
DR HOGENOM; CLU_015138_0_0_1; -.
DR InParanoid; Q66LG9; -.
DR OMA; TSCPNEM; -.
DR OrthoDB; 1286357at2759; -.
DR PhylomeDB; Q66LG9; -.
DR PRO; PR:Q66LG9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q66LG9; baseline and differential.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:TAIR.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019237; F:centromeric DNA binding; IBA:GO_Central.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051382; P:kinetochore assembly; IBA:GO_Central.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IBA:GO_Central.
DR InterPro; IPR028386; CENP-C/Mif2/cnp3.
DR PANTHER; PTHR16684; PTHR16684; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Kinetochore; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..705
FT /note="Centromere protein C"
FT /id="PRO_0000440649"
FT REGION 146..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..658
FT /note="MIF2 homology domain II"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT MOTIF 86..93
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 159..166
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 556..563
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 592..599
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 311..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 78935 MW; EBAE8DE80C507638 CRC64;
MADVSRSSSL YTEEDPLQAY SGLSLFPRTL KSLSNPLPPS YQSEDLQQTH TLLQSMPFEI
QSEHQEQAKA ILEDVDVDVQ LNPIPNKRER RPGLDRKRKS FSLHLTTSQP PPVAPSFDPS
KYPRSEDFFA AYDKFELANR EWQKQTGSSV IDIQENPPSR RPRRPGIPGR KRRPFKESFT
DSYFTDVINL EASEKEIPIA SEQSLESATA AHVTTVDREV DDSTVDTDKD LNNVLKDLLA
CSREELEGDG AIKLLEERLQ IKSFNIEKFS IPEFQDVRKM NLKASGSNPP NRKSLSDIQN
ILKGTNRVAV RKNSHSPSPQ TIKHFSSPNP PVDQFSFPDI HNLLPGDQQP SEVNVQPIAK
DIPNTSPTNV GTVDVASPFN DSVVKRSGED DSHIHSGIHR SHLSRDGNPD ICVMDSISNR
SSAMLQKNVD MRTKGKEVDV PMSESGANRN TGDRENDAEI NEETDNLERL AECASKEVTR
PFTVEEDSIP YQQGASSKSP NRAPEQYNTM GGSLEHAEHN QGLHEEENVN TGSASGLQVE
NAPEVHKYSH KQTNKRRKRG SSDSNVKKRS KTVHGETGGD KQMKTLPHES RAKKQTKGKS
NEREEKKPKK TLTHEGKLFS CRKSLAAAGT KIEGGVRRST RIKSRPLEYW RGERFLYGRI
HESLTTVIGI KYASPGEGKR DSRASKVKSF VSDEYKKLVD FAALH
