ZW10_PONAB
ID ZW10_PONAB Reviewed; 779 AA.
AC Q5RFM4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Centromere/kinetochore protein zw10 homolog;
GN Name=ZW10;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC cells from prematurely exiting mitosis. Required for the assembly of
CC the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Involved
CC in regulation of membrane traffic between the Golgi and the endoplasmic
CC reticulum (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NBAS and KNTC1/ROD; the interactions are
CC mutually exclusive and indicative for its association in two different
CC vesicle tethering complexes (By similarity). Component of the RZZ
CC complex composed of KNTC1/ROD, ZW10 and ZWILCH (By similarity).
CC Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L;
CC NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the
CC assembly has been described as syntaxin 18 complex) (By similarity).
CC Interacts directly with RINT1/TIP20L bound to BNIP1/SEC20L (By
CC similarity). Interacts with C19orf25 and ZWINT (By similarity).
CC Interacts with ZFYVE1 (By similarity). Interacts with RAB18 and this
CC interaction is enhanced in the presence of ZFYVE1 (By similarity).
CC {ECO:0000250|UniProtKB:O43264}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43264}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43264};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O43264}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:O43264}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. Lipid droplet
CC {ECO:0000250|UniProtKB:O43264}. Note=Dynamic pattern of localization
CC during the cell cycle. In most cells at interphase, present diffusely
CC in the cytoplasm. In prometaphase, associated with the kinetochore. At
CC metaphase, detected both at the kinetochores and, most prominently, at
CC the spindle, particularly at the spindle poles. In very early anaphase,
CC detected on segregating kinetochores. In late anaphase and telophase,
CC accumulates at the spindle midzone. {ECO:0000250|UniProtKB:O43264}.
CC -!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
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DR EMBL; CR857131; CAH89433.1; -; mRNA.
DR RefSeq; NP_001124608.1; NM_001131136.2.
DR AlphaFoldDB; Q5RFM4; -.
DR SMR; Q5RFM4; -.
DR STRING; 9601.ENSPPYP00000004454; -.
DR GeneID; 100171445; -.
DR KEGG; pon:100171445; -.
DR CTD; 9183; -.
DR eggNOG; KOG2163; Eukaryota.
DR InParanoid; Q5RFM4; -.
DR OrthoDB; 422807at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.357.150; -; 1.
DR InterPro; IPR009361; RZZ-complex_Zw10.
DR InterPro; IPR046362; Zw10/DSL1_C_sf.
DR Pfam; PF06248; Zw10; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW ER-Golgi transport; Kinetochore; Lipid droplet; Membrane; Mitosis;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT CHAIN 2..779
FT /note="Centromere/kinetochore protein zw10 homolog"
FT /id="PRO_0000249883"
FT REGION 2..317
FT /note="Interaction with RINT1"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT REGION 2..81
FT /note="Interaction with ZWINT"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT COILED 14..130
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
FT MOD_RES 777
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43264"
SQ SEQUENCE 779 AA; 88901 MW; EA9584A170F539F0 CRC64;
MASFVTEVLA HSGRLEKEDL GARISRLTRR VEEIKGEVCN MISKKYSEFL PSMQSAQGLI
TQVDKLSEDI DLLKSRIESE VRRDLHVSTG EFTDLKQQLE RDSIVLSLLK QLQEFSTAIE
EYNCALTEKK YVTGAQRLEE AQKCLKLLKS RKCFDLKILK FLSMELTIQK QNILYHLGEE
WQKLIVWKFS PSKDTSSLES YLQTELHLYT EQSHKEEKTP MPPISSVLLA FSVLGELHSK
LKSFGQMLLK YILRPLASCP SLHAVIESQP NIVIIRFESI MTNLEYPSPS EVFTKIRLVL
EVLQKQLLDL PLDTDLENEK TSTVPLAEML GDMIWEDLSE YLIKNCLVYS IPTNSSKLQQ
YEEIIQSTEE FENALKEMRF LKGDTTDLLK YARNINSHFA NKKCQDVIVA ARNLMTSEIH
NTVKIIPDSK INVPELPTPD EDNKLEVQKV SNTQYNEVMN LEPENTLDQH SFSLPTCRIS
ESVKKLMELA YQTLLEATTS SDQCAVQLFY SVRNIFHLFH DVVPTYHKEN LQKLPQLAAI
HHNNCMYIAH HLLTLGHQFR LRLAPILCDG TATFVDLVPG FRRLGTECFL AQMRAQKGEL
LERLSSARNF SNMDDEENYS AASKAVRQVL HQLKRLGIVW QDVLPVNIYC KAMGTLLNTA
ISEVIGKITA LEDISTEDGD RLYSLCKTVM DEGPQVFAPL SEESKNKKYQ EEVPVYVPKW
MPFKELMMML QASLQEIGDR WADGKGPLAA AFSSSEVKAL IRALFQNTER RAAALAKIK
