CENPX_CHICK
ID CENPX_CHICK Reviewed; 80 AA.
AC P0DJH7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Centromere protein X;
DE Short=CENP-X;
GN Name=CENPX; Synonyms=STRA13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=White Leghorn Hisex;
RX PubMed=12445392; DOI=10.1016/s0960-9822(02)01296-4;
RA Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E.,
RA Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J.;
RT "A comprehensive collection of chicken cDNAs.";
RL Curr. Biol. 12:1965-1969(2002).
RN [2]
RP FUNCTION, INTERACTION WITH CENPS, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19620631; DOI=10.1083/jcb.200903100;
RA Amano M., Suzuki A., Hori T., Backer C., Okawa K., Cheeseman I.M.,
RA Fukagawa T.;
RT "The CENP-S complex is essential for the stable assembly of outer
RT kinetochore structure.";
RL J. Cell Biol. 186:173-182(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), FUNCTION, INTERACTION WITH CENPS;
RP CENPT AND CEPNW, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-9; ARG-27 AND
RP LYS-62.
RX PubMed=22304917; DOI=10.1016/j.cell.2011.11.061;
RA Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T.,
RA Morikawa K., Cheeseman I.M., Fukagawa T.;
RT "CENP-T-W-S-X forms a unique centromeric chromatin structure with a
RT histone-like fold.";
RL Cell 148:487-501(2012).
CC -!- FUNCTION: DNA-binding component of the Fanconi anemia (FA) core
CC complex. Required for the normal activation of the FA pathway, leading
CC to monoubiquitination of the FANCI-FANCD2 complex in response to DNA
CC damage, cellular resistance to DNA cross-linking drugs, and prevention
CC of chromosomal breakage. In complex with CENPS (MHF heterodimer),
CC crucial cofactor for FANCM in both binding and ATP-dependent remodeling
CC of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not
CC other FANC proteins), rapidly recruited to blocked forks and promotes
CC gene conversion at blocked replication forks (By similarity). In
CC complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer),
CC involved in the formation of a functional kinetochore outer plate,
CC which is essential for kinetochore-microtubule attachment and faithful
CC mitotic progression (PubMed:19620631, PubMed:22304917). As a component
CC of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a
CC nucleosome-like structure. DNA-binding function is fulfilled in the
CC presence of CENPS, with the following preference for DNA substates:
CC Holliday junction > double-stranded > splay arm > single-stranded. Does
CC not bind DNA on its own (By similarity). {ECO:0000250|UniProtKB:A8MT69,
CC ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:22304917}.
CC -!- SUBUNIT: Heterodimer with CENPX, sometimes called MHF; this interaction
CC stabilizes both partners (PubMed:19620631, PubMed:22304917). MHF
CC heterodimers can assemble to form tetrameric structures
CC (PubMed:22304917). MHF also coassemble with CENPT-CENPW heterodimers at
CC centromeres to form the tetrameric CENP-T-W-S-X complex
CC (PubMed:22304917). Forms a discrete complex with FANCM and CENPX,
CC called FANCM-MHF; this interaction, probably mediated by direct binding
CC between CENPS and FANCM, leads to synergistic activation of double-
CC stranded DNA binding and strongly stimulates FANCM-mediated DNA
CC remodeling. Recruited by FANCM to the Fanconi anemia (FA) core complex,
CC which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF,
CC FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates
CC with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA
CC topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32.
CC The super complex between FA and BLM is called BRAFT (By similarity).
CC {ECO:0000250|UniProtKB:A8MT69, ECO:0000269|PubMed:19620631,
CC ECO:0000269|PubMed:22304917}.
CC -!- INTERACTION:
CC P0DJH7; E1BSW7: CENPS; NbExp=4; IntAct=EBI-5590609, EBI-5487792;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19620631}.
CC Chromosome, centromere {ECO:0000269|PubMed:19620631}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:19620631}. Note=Assembly of
CC CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres
CC occurs through a dynamic exchange mechanism. Although exchange is
CC continuous in the cell cycle, de novo assembly starts principally
CC during mid-late S phase and is complete by G2. CENPX being less stably
CC bound at the kinetochore than CENPS. {ECO:0000250|UniProtKB:A8MT69}.
CC -!- SIMILARITY: Belongs to the CENP-X/MHF2 family. {ECO:0000305}.
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DR EMBL; CN236791; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 3B0B; X-ray; 2.15 A; C/D=2-80.
DR PDB; 3VH5; X-ray; 2.40 A; D=2-80.
DR PDB; 3VH6; X-ray; 3.35 A; D=2-80.
DR PDB; 7DA0; X-ray; 1.25 A; C=2-80.
DR PDB; 7DA1; X-ray; 2.01 A; C/D=2-80.
DR PDB; 7DA2; X-ray; 2.79 A; B/D=2-80.
DR PDBsum; 3B0B; -.
DR PDBsum; 3VH5; -.
DR PDBsum; 3VH6; -.
DR PDBsum; 7DA0; -.
DR PDBsum; 7DA1; -.
DR PDBsum; 7DA2; -.
DR AlphaFoldDB; P0DJH7; -.
DR SMR; P0DJH7; -.
DR IntAct; P0DJH7; 1.
DR PaxDb; P0DJH7; -.
DR VEuPathDB; HostDB:geneid_101751277; -.
DR InParanoid; P0DJH7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0071821; C:FANCM-MHF complex; IBA:GO_Central.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR InterPro; IPR018552; CENP-X.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR28680; PTHR28680; 1.
DR Pfam; PF09415; CENP-X; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA damage; DNA repair; DNA-binding; Kinetochore; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..80
FT /note="Centromere protein X"
FT /id="PRO_0000417385"
FT MUTAGEN 9
FT /note="R->A: Abolishes sequence-specific DNA binding; when
FT associated with A-27 and A-62."
FT /evidence="ECO:0000269|PubMed:22304917"
FT MUTAGEN 27
FT /note="R->A: Abolishes sequence-specific DNA binding; when
FT associated with A-9 and A-62."
FT /evidence="ECO:0000269|PubMed:22304917"
FT MUTAGEN 62
FT /note="K->A: Abolishes sequence-specific DNA binding; when
FT associated with A-9 and A-27."
FT /evidence="ECO:0000269|PubMed:22304917"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:7DA0"
FT HELIX 30..57
FT /evidence="ECO:0007829|PDB:7DA0"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7DA0"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:7DA0"
SQ SEQUENCE 80 AA; 9257 MW; 91AAB8A5C2D5BBCF CRC64;
MEEREGGFRK ETVERLLRLH FRDGRTRVNG DALLLMAELL KVFVREAAAR AARQAQAEDL
EKVDIEHVEK VLPQLLLDFV
