CENPC_SCHPO
ID CENPC_SCHPO Reviewed; 643 AA.
AC Q9USR9; Q9USY5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Inner kinetochore subunit cnp3;
DE AltName: Full=CENP-C homolog;
DE AltName: Full=Centromere protein 3;
DE AltName: Full=Constitutive centromere-associated network protein cnp3;
GN Name=cnp3; ORFNames=SPBC1861.01c, SPBC56F2.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=15791413; DOI=10.1007/s10577-005-7062-z;
RA Holland S., Ioannou D., Haines S., Brown W.R.;
RT "Comparison of Dam tagging and chromatin immunoprecipitation as tools for
RT the identification of the binding sites for S. pombe CENP-C.";
RL Chromosome Res. 13:73-83(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Component of the kinetochore, a multiprotein complex that
CC assembles on centromeric DNA and attaches chromosomes to spindle
CC microtubules, mediating chromosome segregation and sister chromatid
CC segregation during meiosis and mitosis. Component of the inner
CC kinetochore constitutive centromere-associated network (CCAN), which
CC serves as a structural platform for outer kinetochore assembly.
CC {ECO:0000269|PubMed:15791413}.
CC -!- SUBUNIT: Component of the inner kinetochore constitutive centromere-
CC associated network (CCAN) (also known as central kinetochore Sim4
CC complex in fission yeast), which is composed of at least cnl2, cnp3,
CC cnp20, fta1, fta2, fta3, fta4, fta6, fta7, mal2, mhf1, mhf2, mis6,
CC mis15, mis17, sim4 and wip1. {ECO:0000250|UniProtKB:P35201}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the CENP-C/MIF2 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB54977.1; -; Genomic_DNA.
DR PIR; T39740; T39740.
DR PIR; T40544; T40544.
DR RefSeq; XP_001713151.1; XM_001713099.2.
DR PDB; 6O2D; X-ray; 2.52 A; A/B=489-643.
DR PDBsum; 6O2D; -.
DR AlphaFoldDB; Q9USR9; -.
DR SMR; Q9USR9; -.
DR BioGRID; 276178; 10.
DR IntAct; Q9USR9; 1.
DR STRING; 4896.SPBC1861.01c.1; -.
DR iPTMnet; Q9USR9; -.
DR MaxQB; Q9USR9; -.
DR PaxDb; Q9USR9; -.
DR PRIDE; Q9USR9; -.
DR EnsemblFungi; SPBC1861.01c.1; SPBC1861.01c.1:pep; SPBC1861.01c.
DR PomBase; SPBC1861.01c; cnp3.
DR VEuPathDB; FungiDB:SPBC1861.01c; -.
DR eggNOG; ENOG502S47H; Eukaryota.
DR HOGENOM; CLU_477476_0_0_1; -.
DR InParanoid; Q9USR9; -.
DR OMA; KMHMVFY; -.
DR PRO; PR:Q9USR9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:PomBase.
DR GO; GO:0140483; F:kinetochore adaptor activity; IPI:PomBase.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:PomBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR GO; GO:0051382; P:kinetochore assembly; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IMP:PomBase.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR028386; CENP-C/Mif2/cnp3.
DR InterPro; IPR025974; Mif2/CENP-C_cupin.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR16684; PTHR16684; 1.
DR Pfam; PF11699; CENP-C_C; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..643
FT /note="Inner kinetochore subunit cnp3"
FT /id="PRO_0000116879"
FT DNA_BIND 333..345
FT /note="A.T hook"
FT REGION 55..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 517..525
FT /evidence="ECO:0007829|PDB:6O2D"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 540..547
FT /evidence="ECO:0007829|PDB:6O2D"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 551..558
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 572..587
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 590..595
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:6O2D"
FT STRAND 618..626
FT /evidence="ECO:0007829|PDB:6O2D"
FT HELIX 628..633
FT /evidence="ECO:0007829|PDB:6O2D"
SQ SEQUENCE 643 AA; 72052 MW; 44DAD8EE46C54A4F CRC64;
MTMNETSAIP ARQRENQFFE IGVVGRKTGF TVPRDVKKGD DGFEDMDAYF LSDGSIHLDE
DNGDIEQDMP PVTRLQPTSP MAVNAASDEA SHASSSDSSD KNPDIPSSPL LMNSRALRAS
RGSSGPLIVP IDHSAFQAED EGTADKTKVD GNKLSIQPRK ANRIVDFSRI KASPDRKKFE
PRRSTELPSK IPSSTPKDDN VQESPAFPDE NITALQKNVA NFTSIKDSGG RDNLYIQTIS
KPRRSYVQNN KSEQTIKPSK QNKQKEEKKT ISQGNKPNSR DEDSELSIDV PLSMLNRSLA
NNSQKNKKRT PNKPLQESSI NSVKEGESNP VVKRKRGRPR KNKLEIGNSV QTSEATQVKG
AKKPAIRNAK KMSNEKDDSL NSQSDSASGE FIKTIARNNL QEIKQVERED TLVGVRRSKR
TRIAPLAFWK NERVVYELHR DENRIPALPE VKQIIRVDDP SPSIRQGRKK RHAKRSGVEI
KSNLEAKSND VEEYDAFYKD EINCEVLSWN EQNPKASEER VVGYSLPSVN LQQISNQQLK
FASLFKEEPS FAAGVVEMPA GAEKPVKPSK HNIMSFCILQ GKIEVTVNAT TFRMKKDGVF
IVPRGNYYSI KNIGKEAVRL YYTHATDTLE NKRRGIGDFP NER
