KIF22_BOVIN
ID KIF22_BOVIN Reviewed; 662 AA.
AC A6QPL4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Kinesin-like protein KIF22;
GN Name=KIF22;
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=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Kinesin family member that is involved in spindle formation
CC and the movements of chromosomes during mitosis and meiosis. Binds to
CC microtubules and to DNA. Plays a role in congression of laterally
CC attached chromosomes in NDC80-depleted cells.
CC {ECO:0000250|UniProtKB:Q14807, ECO:0000250|UniProtKB:Q9I869}.
CC -!- SUBUNIT: Interacts with FAM83D and SIAH1.
CC {ECO:0000250|UniProtKB:Q14807}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14807}.
CC Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q14807}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI49377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC149376; AAI49377.1; ALT_INIT; mRNA.
DR RefSeq; NP_001095338.2; NM_001101868.2.
DR AlphaFoldDB; A6QPL4; -.
DR SMR; A6QPL4; -.
DR STRING; 9913.ENSBTAP00000018167; -.
DR iPTMnet; A6QPL4; -.
DR PaxDb; A6QPL4; -.
DR PRIDE; A6QPL4; -.
DR GeneID; 506294; -.
DR KEGG; bta:506294; -.
DR CTD; 3835; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_27_1_1; -.
DR InParanoid; A6QPL4; -.
DR OrthoDB; 787964at2759; -.
DR TreeFam; TF105233; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR026986; KIF22.
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 InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF801; PTHR24115:SF801; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47781; SSF47781; 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 ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW Isopeptide bond; Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..662
FT /note="Kinesin-like protein KIF22"
FT /id="PRO_0000347236"
FT DOMAIN 38..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 389..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..498
FT /evidence="ECO:0000255"
FT COMPBIAS 389..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT CROSSLNK 460
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
SQ SEQUENCE 662 AA; 73202 MW; EBB260C12AFBAD38 CRC64;
MDAGLPARRR REMAAAISGA GRCRLSKVGA GRRPPPARVR VAVRLRPFVD GTAGENDTPC
VRGLDSCSLE IANWRNHQET LKYQFDAFYG ERSSQQDIYA GSVQPILRHL LEGQNASVLA
YGPTGAGKTH TMLGSPEQPG VIPRALMDLL QLTREEGAEG RPWALSVTMS YLEIYQEKVL
DLLEPSSGDL VIREDCRGNI LIPGLTQKPI TSFADFERHF LPASRNRTVG ATRLNQRSSR
SHAVLLVKVD QRERLAPFRQ REGKLYLIDL AGSEDNRRTG NKGLRLKESG AINTSLFVLG
KVVDALNQGL PRVPYRDSKL TRLLQDSLGG SAHSILIANI APERRFYLDT VSALNFAARS
KEVINRPFTN ESLQLPVLAP VKLSQKELLG PSEAKRARGP EEEETESPEL PIAPASASQK
LSPLQKLSSM DPAMLERLLS LDRLLGSQGS QGTPLLSTPK RERMVLMKTV EEKDLEIERL
KMKQKELEAK VLAQEAADPK EKENYSTTML RPLARRTVTV AKPLKKAVVM PLQLIQEQAA
SPNAKIHILK KKGRKRKLES LDASQPEKAE DGWELQISPE LLAHGRQKIL DLLNEGSARD
LRSLQRIGQK KAQLIVGWRE LHGPFSQVED LERVEGISGK QMESFLKANI LGLAAGQGCG
PS
