CENPW_CHICK
ID CENPW_CHICK Reviewed; 76 AA.
AC P0DJH6;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Centromere protein W;
DE Short=CENP-W;
GN Name=CENPW;
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 CENPT, MUTAGENESIS OF ARG-7; ARG-11; LYS-12;
RP ARG-22 AND ARG-75, AND SUBCELLULAR LOCATION.
RX PubMed=19070575; DOI=10.1016/j.cell.2008.10.019;
RA Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y.,
RA McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T.;
RT "CCAN makes multiple contacts with centromeric DNA to provide distinct
RT pathways to the outer kinetochore.";
RL Cell 135:1039-1052(2008).
RN [3]
RP INTERACTION WITH CENPT.
RX PubMed=21464230; DOI=10.1083/jcb.201012050;
RA Suzuki A., Hori T., Nishino T., Usukura J., Miyagi A., Morikawa K.,
RA Fukagawa T.;
RT "Spindle microtubules generate tension-dependent changes in the
RT distribution of inner kinetochore proteins.";
RL J. Cell Biol. 193:125-140(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), FUNCTION, INTERACTION WITH CENPS;
RP CENPW AND CEPNX, AND MUTAGENESIS OF ARG-7; ARG-11; LYS-12; ARG-22; LYS-54
RP AND LYS-56.
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: 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 (By similarity). The
CC CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex
CC and may be involved in incorporation of newly synthesized CENPA into
CC centromeres (By similarity). Part of a nucleosome-associated complex
CC that binds specifically to histone H3-containing nucleosomes at the
CC centromere, as opposed to nucleosomes containing CENPA. Component of
CC the heterotetrameric CENP-T-W-S-X complex that binds and supercoils
CC DNA, and plays an important role in kinetochore assembly. CENPW has a
CC fundamental role in kinetochore assembly and function. It is one of the
CC inner kinetochore proteins, with most further proteins binding
CC downstream. Required for normal chromosome organization and normal
CC progress through mitosis. {ECO:0000250, ECO:0000269|PubMed:19070575,
CC ECO:0000269|PubMed:22304917}.
CC -!- SUBUNIT: Heterodimer with CENPT; this dimer coassembles with CENPS-
CC CENPX heterodimers at centromeres to form the tetrameric CENP-T-W-S-X
CC complex, which is a subcomplex of the large constitutive centromere-
CC associated network (CCAN, also known as the interphase centromere
CC complex or ICEN) (PubMed:19070575, PubMed:21464230, PubMed:22304917).
CC Interacts with NPM1 (By similarity). {ECO:0000250|UniProtKB:Q5EE01,
CC ECO:0000269|PubMed:19070575, ECO:0000269|PubMed:21464230,
CC ECO:0000269|PubMed:22304917}.
CC -!- INTERACTION:
CC P0DJH6; F1NPG5: CENPT; NbExp=4; IntAct=EBI-2132287, EBI-2132248;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19070575}.
CC Chromosome, centromere {ECO:0000269|PubMed:19070575}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:19070575}.
CC Note=Constitutively localizes to centromeres throughout the cell cycle,
CC and to kinetochores during mitosis (PubMed:19070575). Localizes to the
CC inner kinetochore. {ECO:0000269|PubMed:19070575}.
CC -!- MISCELLANEOUS: Association with CENPA-containing complexes may be
CC indirect and due to the proximity of centromeric nucleosomes containing
CC histone H3 with those containing CENPA.
CC -!- SIMILARITY: Belongs to the CENP-W/WIP1 family. {ECO:0000305}.
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DR EMBL; BU413473; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001264662.1; NM_001277733.1.
DR PDB; 3B0C; X-ray; 2.20 A; W=2-76.
DR PDB; 3B0D; X-ray; 2.20 A; C/W=2-76.
DR PDB; 3VH5; X-ray; 2.40 A; W=2-76.
DR PDB; 3VH6; X-ray; 3.35 A; W=2-76.
DR PDBsum; 3B0C; -.
DR PDBsum; 3B0D; -.
DR PDBsum; 3VH5; -.
DR PDBsum; 3VH6; -.
DR AlphaFoldDB; P0DJH6; -.
DR SMR; P0DJH6; -.
DR BioGRID; 682498; 1.
DR IntAct; P0DJH6; 3.
DR STRING; 9031.ENSGALP00000042097; -.
DR Ensembl; ENSGALT00000045695; ENSGALP00000042097; ENSGALG00000027454.
DR GeneID; 421716; -.
DR KEGG; gga:421716; -.
DR CTD; 387103; -.
DR VEuPathDB; HostDB:geneid_421716; -.
DR GeneTree; ENSGT00390000010369; -.
DR HOGENOM; CLU_178644_1_0_1; -.
DR InParanoid; P0DJH6; -.
DR OMA; IIKKDHV; -.
DR OrthoDB; 1578618at2759; -.
DR PRO; PR:P0DJH6; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000027454; Expressed in testis and 12 other tissues.
DR ExpressionAtlas; P0DJH6; baseline and differential.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051382; P:kinetochore assembly; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR028847; CENP-W.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF15510; CENP-W; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA-binding; Kinetochore; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..76
FT /note="Centromere protein W"
FT /id="PRO_0000417384"
FT MUTAGEN 7
FT /note="R->A: Lethal mitotic defects; when associated with
FT A-22 and A-75. Lethal mitotic defects; when associated with
FT A-11; A-12; A-22; A-54 and A-56. Lethal mitotic defects;
FT when associated with A-11; A-12; A-22 and A-75."
FT /evidence="ECO:0000269|PubMed:19070575,
FT ECO:0000269|PubMed:22304917"
FT MUTAGEN 11
FT /note="R->A: Lethal mitotic defects; when associated with
FT A-7; A-12; A-22; A-54 and A-56. Lethal mitotic defects;
FT when associated with A-7; A-12; A-22 and A-75."
FT /evidence="ECO:0000269|PubMed:19070575,
FT ECO:0000269|PubMed:22304917"
FT MUTAGEN 12
FT /note="K->A: Lethal mitotic defects; when associated with
FT A-7; A-11; A-22; A-54 and A-56. Lethal mitotic defects;
FT when associated with A-7; A-11; A-22 and A-75."
FT /evidence="ECO:0000269|PubMed:19070575,
FT ECO:0000269|PubMed:22304917"
FT MUTAGEN 22
FT /note="R->A: Lethal mitotic defects; when associated with
FT A-7 and A-75. Lethal mitotic defects; when associated with
FT A-7; A-11; A-12; A-54 and A-56. Lethal mitotic defects;
FT when associated with A-7; A-11; A-12 and A-75."
FT /evidence="ECO:0000269|PubMed:19070575,
FT ECO:0000269|PubMed:22304917"
FT MUTAGEN 54
FT /note="K->A: Lethal mitotic defects; when associated with
FT A-7; A-11; A-12; A-22; and A-56."
FT /evidence="ECO:0000269|PubMed:22304917"
FT MUTAGEN 56
FT /note="K->A: Lethal mitotic defects; when associated with
FT A-7; A-11; A-12; A-22 and A-54."
FT /evidence="ECO:0000269|PubMed:22304917"
FT MUTAGEN 75
FT /note="R->A: Lethal mitotic defects; when associated with
FT A-7 and A-22. Lethal mitotic defects; when associated with
FT A-7; A-11; A-12 and A-22."
FT /evidence="ECO:0000269|PubMed:19070575"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:3B0D"
FT HELIX 27..52
FT /evidence="ECO:0007829|PDB:3B0D"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3B0D"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:3B0D"
SQ SEQUENCE 76 AA; 8743 MW; B34E201BEBDE72F7 CRC64;
MRRTVPRGTL RKIIKKHKPH LRLAANTDLL VHLSFLLFLH RLAEEARTNA FENKSKIIKP
EHTIAAAKVI LKKSRG
