KIF22_XENTR
ID KIF22_XENTR Reviewed; 639 AA.
AC Q6P3R1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Kinesin-like protein KIF22;
DE AltName: Full=Chromokinesin kid;
GN Name=kif22; Synonyms=kid;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) 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. {ECO:0000250|UniProtKB:Q9I869}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9I869}.
CC Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- PTM: Ubiquitinated, leading to its subsequent proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q9I869}.
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; BC063896; AAH63896.1; -; mRNA.
DR RefSeq; NP_989245.1; NM_203914.1.
DR AlphaFoldDB; Q6P3R1; -.
DR SMR; Q6P3R1; -.
DR PaxDb; Q6P3R1; -.
DR DNASU; 394855; -.
DR GeneID; 394855; -.
DR KEGG; xtr:394855; -.
DR CTD; 3835; -.
DR Xenbase; XB-GENE-979888; kif22.
DR eggNOG; KOG0242; Eukaryota.
DR InParanoid; Q6P3R1; -.
DR OrthoDB; 787964at2759; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; 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:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
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; 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 Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..639
FT /note="Kinesin-like protein KIF22"
FT /id="PRO_0000347240"
FT DOMAIN 18..345
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 358..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..484
FT /evidence="ECO:0000255"
FT MOTIF 549..552
FT /note="Important for regulated proteolytic degradation"
FT /evidence="ECO:0000250"
FT COMPBIAS 365..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 639 AA; 71391 MW; F5664F9020A6A1AA CRC64;
MAKRVSILDQ HKKPSSARVR VAVRLRPYME KEDEKAPAAC VRGLDSQSLE IVNWRNQLET
MQYQFDAFYG DSATQREIYM GSVCHILPHL LIGQNASVFA YGPTGAGKTH TMLGNPSQPG
VIPRAVRDLL QMTRTAAGGP ENENWTYTIT MSYVEIYQEK VMDLLEPKNK DLPIREDKDH
NILIPGVTQK TINSFGDFDE HFIPASQNRT VASTKLNDRS SRSHAVLLIK VQKSQQVSPF
RQLTGKLYLI DLAGSEDNRR TGNQGIRLKE SGAINSSLFT LSKVVDALNQ GLPRIPYRDS
KLTRLLQDSL GGTAHSVMIA NIAPEQKYYF DTLTALNFAA KSKQIINKPF SQETTQSIAA
LPAMKRPREE AETAAGSRQR KKSKTDSTES SPNTSMDAAS KRKLNLAALD PAVVERLLKL
DKILTEKGMK EAQLLSTPKR ERMALLKKWE ESQMEIERLK EKQKELEQKA IEAEARLEKS
TNSDCNLSDS SVSECTFRAP LRGRNTSTAK AKKVLRVLPM QGNSQLQSTI EEGIPVFEKK
KKKPVSCDGR ENQPTWEVNV RTDLLESGRE RILKLLNTGS VKELKSLQKI GDKKAKLIIG
WREVNGPFKN VEDLASLEGI SAKQVTSFIK ANILSIIAS