ID   KF22A_XENLA             Reviewed;         651 AA.
AC   Q9I869; Q9I8K0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Kinesin-like protein KIF22-A;
DE   AltName: Full=Chromokinesin kid-A;
DE            Short=Xkid-A;
GN   Name=kif22-a; Synonyms=kid-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION,
RP   AND PROTEOLYTIC DEGRADATION.
RC   TISSUE=Blastula;
RX   PubMed=10966104; DOI=10.1016/s0092-8674(00)00047-7;
RA   Funabiki H., Murray A.W.;
RT   "The Xenopus chromokinesin Xkid is essential for metaphase chromosome
RT   alignment and must be degraded to allow anaphase chromosome movement.";
RL   Cell 102:411-424(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PROTEOLYTIC DEGRADATION.
RC   TISSUE=Oocyte;
RX   PubMed=10966105; DOI=10.1016/s0092-8674(00)00048-9;
RA   Antonio C., Ferby I., Wilhelm H., Jones M., Karsenti E., Nebreda A.R.,
RA   Vernos I.;
RT   "Xkid, a chromokinesin required for chromosome alignment on the metaphase
RT   plate.";
RL   Cell 102:425-435(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=12360284; DOI=10.1038/ncb850;
RA   Perez L.H., Antonio C., Flament S., Vernos I., Nebreda A.R.;
RT   "Xkid chromokinesin is required for the meiosis I to meiosis II transition
RT   in Xenopus laevis oocytes.";
RL   Nat. Cell Biol. 4:737-742(2002).
RN   [5]
RP   DEVELOPMENTAL STAGE, PROTEOLYTIC DEGRADATION, AND MUTAGENESIS OF GLY-561;
RP   LEU-562; GLU-563 AND ASN-564.
RX   PubMed=12773557; DOI=10.1128/mcb.23.12.4126-4138.2003;
RA   Castro A., Vigneron S., Bernis C., Labbe J.-C., Lorca T.;
RT   "Xkid is degraded in a D-box, KEN-box, and A-box-independent pathway.";
RL   Mol. Cell. Biol. 23:4126-4138(2003).
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:0000269|PubMed:10966104,
CC       ECO:0000269|PubMed:10966105, ECO:0000269|PubMed:12360284}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10966104}. Cytoplasm,
CC       cytoskeleton {ECO:0000305|PubMed:10966104}.
CC   -!- DEVELOPMENTAL STAGE: First detected at germinal vesicle breakdown in
CC       maturing oocytes (at protein level). {ECO:0000269|PubMed:12773557}.
CC   -!- PTM: Ubiquitinated, leading to its subsequent proteasomal degradation.
CC       {ECO:0000269|PubMed:10966104}.
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; AF267849; AAF82563.1; -; mRNA.
DR   EMBL; AF267850; AAF82564.1; -; mRNA.
DR   EMBL; AJ249840; CAB71798.1; -; mRNA.
DR   EMBL; BC070549; AAH70549.1; -; mRNA.
DR   RefSeq; NP_001165448.1; NM_001171977.1.
DR   AlphaFoldDB; Q9I869; -.
DR   SMR; Q9I869; -.
DR   GeneID; 100337510; -.
DR   KEGG; xla:100337510; -.
DR   CTD; 100337510; -.
DR   Xenbase; XB-GENE-979894; kif22.S.
DR   OrthoDB; 787964at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 100337510; Expressed in egg cell and 17 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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   1: Evidence at protein 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..651
FT                   /note="Kinesin-like protein KIF22-A"
FT                   /id="PRO_0000347238"
FT   DOMAIN          31..359
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          366..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          452..498
FT                   /evidence="ECO:0000255"
FT   MOTIF           561..564
FT                   /note="Important for regulated proteolytic degradation"
FT   COMPBIAS        379..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MUTAGEN         561
FT                   /note="G->A: Reduces regulated proteolytic degradation."
FT                   /evidence="ECO:0000269|PubMed:12773557"
FT   MUTAGEN         562
FT                   /note="L->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:12773557"
FT   MUTAGEN         563
FT                   /note="E->A: Reduces regulated proteolytic degradation."
FT                   /evidence="ECO:0000269|PubMed:12773557"
FT   MUTAGEN         564
FT                   /note="N->A: Reduces regulated proteolytic degradation."
FT                   /evidence="ECO:0000269|PubMed:12773557"
FT   CONFLICT        99
FT                   /note="H -> Y (in Ref. 1; AAF82564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   651 AA;  73066 MW;  C2ABA561C4C53C13 CRC64;
     MVLTGPLQRE SVSMAKRVSM LDQHKKSSCA RVRVAVRLRP YMDEKDEAKA TTVCVRGLDS
     QSLEIVNWRN QLETMQYQFD AFYGDSASQR EIYMGSVCHI LPHLLIGQNA SVFAYGPTGA
     GKTHTMLGNP NQPGVIPRAV RDLLQMSRTA ASAPENENWT YTINMSYVEI YQEKVMDLLE
     PKNKDLPIRE DKDHNILIPG VTQKMINSFA DFDEHFIPAS QNRTVASTKL NDRSSRSHAV
     LLIKVQKSQQ VVPFRQLTGK LYLIDLAGSE DNRRTGNQGI RLKESGAINS SLFTLSKVVD
     ALNQGLPRIP YRDSKLTRLL QDSLGGSAHS VMITNIAPEQ TYYFDTLTAL NFAAKSKQII
     NKPFSQETTQ TVVQPAMKRP REETGHIAGS QKRKKSKNDS TESSPNSSMD TAGKQKLNLA
     TLDPAVVERL LKLDKILTEK GKKKAQLLST PKRERMALLK KWEESQMEIE RLKEKQKELE
     QKAMEAEARL EKSNNSDLSD SSVSENTFRA PLRGRNTSTA KVKKVLRVLP MQGNSQLQST
     VEEGIPVFEK KKKKKQVTCE GLENQPTWEM NMRTDLLESG KERILKLLNT GSVKELKSLQ
     RIGDKKAKLI IGWREVNGPF KNVEELACLE GISAKQVSSF IKANIMSSIA S