KIF22_RAT
ID KIF22_RAT Reviewed; 657 AA.
AC Q5I0E8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Kinesin-like protein KIF22;
GN Name=Kif22;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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DR EMBL; BC088421; AAH88421.1; -; mRNA.
DR RefSeq; NP_001009645.1; NM_001009645.1.
DR AlphaFoldDB; Q5I0E8; -.
DR SMR; Q5I0E8; -.
DR BioGRID; 254299; 1.
DR STRING; 10116.ENSRNOP00000027525; -.
DR PaxDb; Q5I0E8; -.
DR PRIDE; Q5I0E8; -.
DR Ensembl; ENSRNOT00000114752; ENSRNOP00000078862; ENSRNOG00000020281.
DR GeneID; 293502; -.
DR KEGG; rno:293502; -.
DR UCSC; RGD:1311886; rat.
DR CTD; 3835; -.
DR RGD; 1311886; Kif22.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000159632; -.
DR HOGENOM; CLU_001485_27_1_1; -.
DR InParanoid; Q5I0E8; -.
DR OMA; VIREDRW; -.
DR OrthoDB; 787964at2759; -.
DR PhylomeDB; Q5I0E8; -.
DR TreeFam; TF105233; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q5I0E8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020281; Expressed in thymus and 18 other tissues.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; ISO:RGD.
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..657
FT /note="Kinesin-like protein KIF22"
FT /id="PRO_0000262923"
FT DOMAIN 38..360
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..502
FT /evidence="ECO:0000255"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14807"
SQ SEQUENCE 657 AA; 73056 MW; CB0446720DBBD945 CRC64;
MNVRAKKKPQ QREMASASSG PSRSLSKGGV SRRPPLARVR VAVRLRPFMD EAKEPPCVRG
IDSCSLEVAN WRKYQETLKY QFDAFYGEKS TQQDVYVGSV QPILRHLLEG QNASVLAYGP
TGAGKTHTML GSPEQPGVIP RALMDLLQLT REESAEGRPW DISVAMSYLE IYQEKVLDLL
DPASGDLVIR EDCRGNILIP GLTQKPITSF SEFEQHFLPA SRNRVVGATR LNQRSSRSHA
VLLVKVEQRE RLTPFRQREG KLYLIDLAGS EDNRRTGNQG IRLKESGAIN TSLFVLGKVV
DALNQGLPRI PYRDSKLTRL LQDSLGGSAH SILIANIAPE RRFYQDTISA LNFTARSKEV
INRPFTNESL QPHALAPVKL PQKELLGPSE AKKAKGPEEE STGSPESTAA PASASQKLSL
LQKLSNMDPA MLENLLSMER LLGSQGSQGI PLLNTPKRER MVLIKTVEEK NLEIERLKMK
QKELEAKVLA QEALDPKEKE NTPTILQPSS SCSGSVAKPL KKAVVMPLQR IQKQSESSNK
IHLLKKGHKR KLESSHESEA VEKDEDYWEI QISPELLARG RKKLLHLLNE GSARDLRSLQ
RIGQKKAQLI VGWRELHGPF NEVEDLEQVE GISGKQVESF LKANLLSLAA SQHSGPS
