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CENPA_XENLA
ID   CENPA_XENLA             Reviewed;         150 AA.
AC   Q569M3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Histone H3-like centromeric protein A;
DE   AltName: Full=Centromere protein A;
DE            Short=CENP-A;
GN   Name=cenpa;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX   PubMed=15673610; DOI=10.1091/mbc.e04-09-0788;
RA   Edwards N.S., Murray A.W.;
RT   "Identification of Xenopus CENP-A and an associated centromeric DNA
RT   repeat.";
RL   Mol. Biol. Cell 16:1800-1810(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15964249; DOI=10.1016/j.dnarep.2005.02.007;
RA   Zeitlin S.G., Patel S., Kavli B., Slupphaug G.;
RT   "Xenopus CENP-A assembly into chromatin requires base excision repair
RT   proteins.";
RL   DNA Repair 4:760-772(2005).
CC   -!- FUNCTION: Histone H3-like nucleosomal protein that is specifically
CC       found in centromeric nucleosomes. Replaces conventional H3 in the
CC       nucleosome core of centromeric chromatin at the inner plate of the
CC       kinetochore. The presence of CENPA subtly modifies the nucleosome
CC       structure and the way DNA is wrapped around the nucleosome and gives
CC       rise to protruding DNA ends that are less well-ordered and rigid
CC       compared to nucleosomes containing histone H3. May serve as an
CC       epigenetic mark that propagates centromere identity through replication
CC       and cell division. Required for recruitment and assembly of kinetochore
CC       proteins, and as a consequence required for progress through mitosis,
CC       chromosome segregation and cytokinesis. {ECO:0000250|UniProtKB:P49450}.
CC   -!- SUBUNIT: Component of centromeric nucleosomes, where DNA is wrapped
CC       around a histone octamer core. The octamer contains two molecules each
CC       of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer and
CC       two H2A-H2B heterodimers. CENPA modulates the DNA-binding
CC       characteristics of nucleosomes so that protruding DNA ends have higher
CC       flexibility than in nucleosomes containing conventional histone H3.
CC       {ECO:0000250|UniProtKB:P49450}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15964249}.
CC       Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P49450}.
CC       Chromosome, centromere {ECO:0000269|PubMed:15673610,
CC       ECO:0000269|PubMed:15964249}. Note=Localizes exclusively in the
CC       kinetochore domain of centromeres. Occupies a compact domain at the
CC       inner kinetochore plate stretching across 2 thirds of the length of the
CC       constriction but encompassing only one third of the constriction width
CC       and height. {ECO:0000250|UniProtKB:P49450}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q569M3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q569M3-2; Sequence=VSP_020431;
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; BC092389; AAH92389.1; -; mRNA.
DR   RefSeq; NP_001090007.1; NM_001096538.1. [Q569M3-1]
DR   AlphaFoldDB; Q569M3; -.
DR   SMR; Q569M3; -.
DR   BioGRID; 592860; 1.
DR   IntAct; Q569M3; 1.
DR   MaxQB; Q569M3; -.
DR   DNASU; 735079; -.
DR   GeneID; 735079; -.
DR   KEGG; xla:735079; -.
DR   CTD; 735079; -.
DR   Xenbase; XB-GENE-865062; cenpa.L.
DR   OMA; REICITF; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 735079; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Centromere; Chromosome; DNA-binding; Kinetochore;
KW   Nucleosome core; Nucleus; Reference proteome.
FT   CHAIN           1..150
FT                   /note="Histone H3-like centromeric protein A"
FT                   /id="PRO_0000249470"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..150
FT                   /note="H3-like"
FT   COMPBIAS        34..51
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         145..149
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15673610"
FT                   /id="VSP_020431"
SQ   SEQUENCE   150 AA;  17343 MW;  79A70E6115B68D33 CRC64;
     MRPGSTPPSR RKSRPPRRVS PPLPTTSRTS PRRPHAQQQR RASRASPKKR FRPGTRALME
     IRKYQKSTEL LIRKAPFSRL VREVCMTYAC GMNYNWQSMA LMALQEASEA FLVRLFEDSY
     LCSLHAKRVT LYVQDIQLAR RIRGVNEGLG
 
 
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