KI20A_BOVIN
ID KI20A_BOVIN Reviewed; 888 AA.
AC Q29RT6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Kinesin-like protein KIF20A;
GN Name=KIF20A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitotic kinesin required for chromosome passenger complex
CC (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved
CC in recruitment of PLK1 to the central spindle. Interacts with guanosine
CC triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor
CC required for the retrograde RAB6 regulated transport of Golgi membranes
CC and associated vesicles along microtubules. Has a microtubule plus end-
CC directed motility.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:O95235}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O95235}.
CC Note=Localizes to the spindle midzone during anaphase and telophase.
CC {ECO:0000250|UniProtKB:O95235}.
CC -!- PTM: Phosphorylated by PLK1 at Ser-527 during mitosis, creating a
CC docking site for PLK1 and recruiting PLK1 at central spindle.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC114026; AAI14027.1; -; mRNA.
DR RefSeq; NP_001039753.1; NM_001046288.2.
DR AlphaFoldDB; Q29RT6; -.
DR SMR; Q29RT6; -.
DR STRING; 9913.ENSBTAP00000011539; -.
DR PaxDb; Q29RT6; -.
DR PRIDE; Q29RT6; -.
DR Ensembl; ENSBTAT00000011539; ENSBTAP00000011539; ENSBTAG00000008758.
DR GeneID; 527854; -.
DR KEGG; bta:527854; -.
DR CTD; 10112; -.
DR VEuPathDB; HostDB:ENSBTAG00000008758; -.
DR VGNC; VGNC:30594; KIF20A.
DR eggNOG; KOG0247; Eukaryota.
DR GeneTree; ENSGT00940000156931; -.
DR HOGENOM; CLU_001485_2_5_1; -.
DR InParanoid; Q29RT6; -.
DR OMA; DVREECW; -.
DR OrthoDB; 314538at2759; -.
DR TreeFam; TF105232; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000008758; Expressed in oocyte and 95 other tissues.
DR ExpressionAtlas; Q29RT6; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0061952; P:midbody abscission; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027326; KIF20A.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF352; PTHR24115:SF352; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT CHAIN 2..888
FT /note="Kinesin-like protein KIF20A"
FT /id="PRO_0000244376"
FT DOMAIN 63..506
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 761..888
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 823..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..587
FT /evidence="ECO:0000255"
FT COILED 630..760
FT /evidence="ECO:0000255"
FT COMPBIAS 823..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 527
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 855
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95235"
SQ SEQUENCE 888 AA; 100044 MW; FD2A2D7083DD4662 CRC64;
MSQGILSPPA GLLSDEEVVV SPMFESTAAD LGSVIRKDLL SDCSVISTSL EDKQVPSEDG
TEKVKVYLRV RPLLPSELER QEDQGCVCIE NMETLALQAP KDSFAQKSNE RGIGQATHRF
TFSQIFGPEV GQASFFNLTV KEMVKDVLKG QNWLIYTYGV TNSGKTYTIQ GTIKDGGILP
RSLALIFNSL QGQLHPTPNL KPLFSNEVMW LDSKQIRQEE LKKLALLNGG LQEEELSTSL
KKSVYIDSRM GTSTSFDSGI AGLSSSSQFP SSSQLDEMSH RWAQPDTVPV SVPADLRFSI
WISFFEIYNE LLYDLLEPPS QQRKRQTLRL CEDQNGNPYV KDLNWIHVQD AEEAWKLLKV
GRKNQSFAST HLNQNSSRSH SIFSIRILHL QGEGDIIPKI SELSLCDLAG SERCKDQKSG
ERLKEAGNIN TSLHTLGRCI AALRQNQQNR SKQNLVPFRD SKLTRVFQGF FTGRGRSCMI
VNVNPCASTY DETLHVAKFS AIASQLVHAP PVQLGFPSIH SFLKEHSLRA SPSLETGAKT
DPGLGDDIEN EVDISTYGKE ELLQVVEAMK ALLLKERQEK LRLEVQLRDE ICNEMVEQMQ
QREQWCSEHL DTQKELLEEL YEDKLTILKE SLTSFYQEEL QERDEKIKEL EALLQEARQQ
QVAHQPSGSE LSLRRSQRLT SVSTQQFHEI KAKLEQCKAE LNSTTEELQK YQKMLEPPPS
AKPFIVDVDK KLEEGQKNIR LLRTELQKLG ESLQSAERAC CHNTGAGKLR QALATCDDIL
IKQDQTLAEL QNNMTLVKLD LRKKAACIAE QYHTVLKLQG QASTKKRLGA NQENQQPNQQ
PPGKKPFLRN LLPRTPTCQS STDCSPYARI LRSRRSPLLK SGPFGKKY
