ID   KIF22_DANRE             Reviewed;         634 AA.
AC   A8WFU8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Kinesin-like protein KIF22;
GN   Name=kif22; ORFNames=zgc:171724;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-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. {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; BC154464; AAI54465.1; -; mRNA.
DR   RefSeq; NP_001107063.1; NM_001113591.1.
DR   AlphaFoldDB; A8WFU8; -.
DR   SMR; A8WFU8; -.
DR   STRING; 7955.ENSDARP00000103034; -.
DR   PaxDb; A8WFU8; -.
DR   PeptideAtlas; A8WFU8; -.
DR   GeneID; 561788; -.
DR   KEGG; dre:561788; -.
DR   CTD; 3835; -.
DR   ZFIN; ZDB-GENE-080204-34; kif22.
DR   eggNOG; KOG0242; Eukaryota.
DR   InParanoid; A8WFU8; -.
DR   OrthoDB; 398790at2759; -.
DR   Reactome; R-DRE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-DRE-983189; Kinesins.
DR   PRO; PR:A8WFU8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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:0007409; P:axonogenesis; IMP:ZFIN.
DR   GO; GO:0007420; P:brain development; IMP:ZFIN.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:ZFIN.
DR   GO; GO:0048592; P:eye morphogenesis; IMP:ZFIN.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR   GO; GO:0001966; P:thigmotaxis; IMP:ZFIN.
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..634
FT                   /note="Kinesin-like protein KIF22"
FT                   /id="PRO_0000347237"
FT   DOMAIN          19..345
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          357..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          421..471
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        364..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   634 AA;  70593 MW;  B9FF21ABFBBF4684 CRC64;
     MAQRVAVNDG AAGSKRTSRV RVAVRLRPYM DKQDEKSEGS CVRGLGPQKL EIINWRNATE
     TLQYQFDVFH GEETTQQEVF LTSVKPILPH ILNGQNASVF AYGPTGAGKT HTMLGSQEQP
     GVIPRAVKEV FNLVGAQKKE QDGWEYSIGM SYLEIYNEKV LDLLSPGSQD LPIREDKDRN
     ILIPGLTHTP LSSFADFDTH FIPASLNRTT ASTKLNQRSS RSHAILLIKV VKSQRGPPHR
     QQTGKLYLVD LAGSEDNRRT GNQGIRLKES GAINLSLFTL SKVVDALNTG AGGRVPYRDS
     KLTRLLQDSL GGSAHSVMIT NIAPEYKYYF DTFSALNFAA KSKQIVNRPF VRETVLAPTI
     APGKRTREEQ EAGGSGEPQN KRSKEGKKAE HSPSPPLHPQ SSPDSSVLDR LLALEKMMMG
     SAERERLNLL KTVAQSRKEI QMLKEKQKEL EDKANMFNKQ KETTEKESKD ALLFKTDLPP
     LHRKQSTAAK PRKQQAVVTP LQVSQVQPLQ QCAVVCKPSQ TLVKKKRVQT EVCDGKENIG
     VDLPPVEDVN WESRLDPALL EQSRKKILQT LNSGSLKELK SLQQIGDKKA KLIMGWREIN
     GDFTQVEDLK KIEGVTVKRF SSFIKANILS SMGK