CID_DROME
ID CID_DROME Reviewed; 225 AA.
AC Q9V6Q2; Q7YUD4; Q7YUD5; Q8MQP5; Q9NG62;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Histone H3-like centromeric protein cid;
DE AltName: Full=CENP-A homolog;
DE AltName: Full=Centromere identifier protein;
GN Name=cid {ECO:0000312|FlyBase:FBgn0040477};
GN Synonyms=CENP-A {ECO:0000303|PubMed:24703848,
GN ECO:0000312|FlyBase:FBgn0040477};
GN ORFNames=CG13329 {ECO:0000312|FlyBase:FBgn0040477};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=10639145; DOI=10.1073/pnas.97.2.716;
RA Henikoff S., Ahmad K., Platero J.S., van Steensel B.;
RT "Heterochromatic deposition of centromeric histone H3-like proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:716-721(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Antigua, In, Melbourne, Oregon-R, and Tai 255.1;
RX PubMed=12815450; DOI=10.1038/sj.hdy.6800275;
RA Sainz A., Wilder J.A., Wolf M., Hollocher H.;
RT "Drosophila melanogaster and D. simulans rescue strains produce fit
RT offspring, despite divergent centromere-specific histone alleles.";
RL Heredity 91:28-35(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION.
RX PubMed=11483958; DOI=10.1038/35087045;
RA Blower M.D., Karpen G.H.;
RT "The role of Drosophila CID in kinetochore formation, cell-cycle
RT progression and heterochromatin interactions.";
RL Nat. Cell Biol. 3:730-739(2001).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15475964; DOI=10.1038/nsmb845;
RA Sullivan B.A., Karpen G.H.;
RT "Centromeric chromatin exhibits a histone modification pattern that is
RT distinct from both euchromatin and heterochromatin.";
RL Nat. Struct. Mol. Biol. 11:1076-1083(2004).
RN [8]
RP INTERACTION WITH CAP-G.
RX PubMed=15592865; DOI=10.1007/s00412-004-0322-4;
RA Jaeger H., Rauch M., Heidmann S.;
RT "The Drosophila melanogaster condensin subunit Cap-G interacts with the
RT centromere-specific histone H3 variant CID.";
RL Chromosoma 113:350-361(2005).
RN [9]
RP FUNCTION.
RX PubMed=16839185; DOI=10.1371/journal.pgen.0020110;
RA Blower M.D., Daigle T., Kaufman T., Karpen G.H.;
RT "Drosophila CENP-A mutations cause a BubR1-dependent early mitotic delay
RT without normal localization of kinetochore components.";
RL PLoS Genet. 2:1025-1032(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-75; THR-76 AND
RP SER-77, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21080953; DOI=10.1186/1471-2156-11-104;
RA Meyer R.E., Delaage M., Rosset R., Capri M., Ait-Ahmed O.;
RT "A single mutation results in diploid gamete formation and parthenogenesis
RT in a Drosophila yemanuclein-alpha meiosis I defective mutant.";
RL BMC Genet. 11:104-104(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHRAC-14.
RX PubMed=24703848; DOI=10.1016/j.celrep.2014.03.008;
RA Mathew V., Pauleau A.L., Steffen N., Bergner A., Becker P.B., Erhardt S.;
RT "The histone-fold protein CHRAC14 influences chromatin composition in
RT response to DNA damage.";
RL Cell Rep. 7:321-330(2014).
CC -!- FUNCTION: Histone H3-like variant which exclusively replaces
CC conventional H3 in the nucleosome core of centromeric chromatin at the
CC inner plate of the kinetochore (PubMed:11483958, PubMed:16839185).
CC Required for recruitment and assembly of kinetochore proteins, mitotic
CC progression and chromosome segregation (PubMed:24703848,
CC PubMed:11483958, PubMed:16839185). May serve as an epigenetic mark that
CC propagates centromere identity through replication and cell division
CC (PubMed:11483958, PubMed:16839185). {ECO:0000269|PubMed:11483958,
CC ECO:0000269|PubMed:16839185, ECO:0000269|PubMed:24703848}.
CC -!- SUBUNIT: Forms a nucleosome-like histone octamer containing two
CC molecules each of H2A, H2B, cid and H4 assembled in one cid-H4
CC heterotetramer and two H2A-H2B heterodimers (By similarity). The cid-H4
CC heterotetramer is more compact and structurally more rigid than
CC corresponding H3-H4 heterotetramers (By similarity). Interacts with the
CC condensin subunit Cap-G (PubMed:15592865). Interacts with Chrac-14
CC (PubMed:24703848). {ECO:0000250|UniProtKB:P49450,
CC ECO:0000269|PubMed:15592865, ECO:0000269|PubMed:24703848}.
CC -!- INTERACTION:
CC Q9V6Q2; Q24572: Caf1-55; NbExp=6; IntAct=EBI-129287, EBI-75924;
CC Q9V6Q2; P84051: His2A:CG33865; NbExp=2; IntAct=EBI-129287, EBI-182580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24703848}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21080953}.
CC Note=Localizes exclusively in the kinetochore domain of centromeres.
CC Co-expressed with yemalpha. {ECO:0000269|PubMed:21080953}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM75058.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF259371; AAF72652.1; -; Genomic_DNA.
DR EMBL; AY126929; AAM80987.1; -; Genomic_DNA.
DR EMBL; AY126930; AAM80988.1; -; Genomic_DNA.
DR EMBL; AY126931; AAM80989.1; -; Genomic_DNA.
DR EMBL; AY126932; AAM80990.1; -; Genomic_DNA.
DR EMBL; AY126933; AAM80991.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58371.2; -; Genomic_DNA.
DR EMBL; AY128465; AAM75058.1; ALT_FRAME; mRNA.
DR RefSeq; NP_523730.2; NM_079006.4.
DR PDB; 6XWS; X-ray; 4.36 A; A=1-225.
DR PDB; 6XWT; X-ray; 3.47 A; A/C=1-225.
DR PDBsum; 6XWS; -.
DR PDBsum; 6XWT; -.
DR AlphaFoldDB; Q9V6Q2; -.
DR SMR; Q9V6Q2; -.
DR BioGRID; 62254; 28.
DR DIP; DIP-29506N; -.
DR IntAct; Q9V6Q2; 6.
DR MINT; Q9V6Q2; -.
DR STRING; 7227.FBpp0086787; -.
DR iPTMnet; Q9V6Q2; -.
DR PaxDb; Q9V6Q2; -.
DR DNASU; 36495; -.
DR EnsemblMetazoa; FBtr0087667; FBpp0086787; FBgn0040477.
DR GeneID; 36495; -.
DR KEGG; dme:Dmel_CG13329; -.
DR CTD; 36495; -.
DR FlyBase; FBgn0040477; cid.
DR VEuPathDB; VectorBase:FBgn0040477; -.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_091477_0_0_1; -.
DR InParanoid; Q9V6Q2; -.
DR OMA; DSYMLTK; -.
DR OrthoDB; 1398997at2759; -.
DR PhylomeDB; Q9V6Q2; -.
DR BioGRID-ORCS; 36495; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36495; -.
DR PRO; PR:Q9V6Q2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0040477; Expressed in secondary oocyte and 6 other tissues.
DR ExpressionAtlas; Q9V6Q2; baseline and differential.
DR Genevisible; Q9V6Q2; DM.
DR GO; GO:0043505; C:CENP-A containing nucleosome; IDA:FlyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0000939; C:inner kinetochore; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0000786; C:nucleosome; IPI:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IGI:FlyBase.
DR GO; GO:0051382; P:kinetochore assembly; IMP:FlyBase.
DR GO; GO:0051383; P:kinetochore organization; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromosome; DNA-binding; Kinetochore;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..225
FT /note="Histone H3-like centromeric protein cid"
FT /id="PRO_0000249474"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..225
FT /note="H3-like"
FT COMPBIAS 40..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 113..114
FT /note="AA -> TS (in strain: Tai 255.1)"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:6XWT"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6XWT"
FT HELIX 174..201
FT /evidence="ECO:0007829|PDB:6XWT"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:6XWT"
SQ SEQUENCE 225 AA; 25968 MW; E125327C4EDD12D2 CRC64;
MPRHSRAKRA PRPSANNSKS PNDDDTAFRS PEPEDGTDYG LEFTTSQLTL QDNNRRSSTL
RRDAGRRQPA ARDSSTSGEE EDQENRYPTT RSPQTRRMTV QQESKTRAAG PVAAQNQTRR
RKAANPMSRA KRMDREIRRL QHHPGTLIPK LPFSRLVREF IVKYSDDEPL RVTEGALLAM
QESCEMYLTQ RLADSYMLTK HRNRVTLEVR DMALMAYICD RGRQF
