ID KI15A_XENLA Reviewed; 1388 AA.
AC Q91785;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Kinesin-like protein KIF15-A;
DE AltName: Full=Kinesin-like protein 2-A;
DE Short=Xklp2-A;
GN Name=kif15-a; Synonyms=klp2;
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, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte;
RX PubMed=8548825; DOI=10.1016/s0092-8674(00)80992-7;
RA Boleti H., Karsenti E., Vernos I.;
RT "Xklp2, a novel Xenopus centrosomal kinesin-like protein required for
RT centrosome separation during mitosis.";
RL Cell 84:49-59(1996).
RN [2]
RP HOMODIMER, IDENTIFICATION IN A COMPLEX WITH TPX2 AND MICROTUBULES,
RP MUTAGENESIS OF LEU-1371, AND SUBCELLULAR LOCATION.
RX PubMed=9813089; DOI=10.1083/jcb.143.3.673;
RA Wittmann T., Boleti H., Antony C., Karsenti E., Vernos I.;
RT "Localization of the kinesin-like protein Xklp2 to spindle poles requires a
RT leucine zipper, a microtubule-associated protein, and dynein.";
RL J. Cell Biol. 143:673-685(1998).
RN [3]
RP IDENTIFICATION IN A COMPLEX WITH TPX2 AND MICROTUBULES, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10871281; DOI=10.1083/jcb.149.7.1405;
RA Wittmann T., Wilm M., Karsenti E., Vernos I.;
RT "TPX2, a novel Xenopus MAP involved in spindle pole organization.";
RL J. Cell Biol. 149:1405-1418(2000).
CC -!- FUNCTION: Plus-end directed kinesin-like motor enzyme involved in
CC mitotic spindle assembly. Required for centrosome separation and
CC maintenance of spindle bipolarity during mitosis.
CC {ECO:0000269|PubMed:8548825}.
CC -!- SUBUNIT: Homodimer. Dimerization is required for targeting to
CC microtubule minus ends. Found in a complex with tpx2 and microtubules.
CC Its association with microtubules and targeting to microtubule minus
CC ends requires tpx2. {ECO:0000269|PubMed:10871281,
CC ECO:0000269|PubMed:9813089}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.
CC Cytoplasm, cytoskeleton, spindle pole. Note=Localizes during metaphase
CC on spindle microtubules, with a strong enrichment at spindle poles.
CC Localizes to the minus ends of spindle pole and aster microtubules in a
CC dynein- and dynactin-dependent manner. Detected diffusively in the
CC cytoplasm. Localized (PubMed:8548825) at the centrosome during the
CC interphase and throughout mitosis. {ECO:0000269|PubMed:8548825}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in testis and weakly in lung (at
CC protein level). {ECO:0000269|PubMed:8548825}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in oocytes and eggs (at
CC protein level). {ECO:0000269|PubMed:8548825}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KLP2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; X94082; CAA63826.1; -; mRNA.
DR PIR; T30335; T30335.
DR RefSeq; NP_001081543.1; NM_001088074.1.
DR AlphaFoldDB; Q91785; -.
DR SMR; Q91785; -.
DR BioGRID; 99246; 1.
DR MaxQB; Q91785; -.
DR GeneID; 397909; -.
DR KEGG; xla:397909; -.
DR AGR; Xenbase:XB-GENE-1005657; -.
DR CTD; 397909; -.
DR OrthoDB; 2915018at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397909; Expressed in spleen and 9 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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 CDD; cd01373; KISc_KLP2_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR031794; HMMR_C.
DR InterPro; IPR044986; KIF15/KIN-12.
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 PANTHER; PTHR37739; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR PANTHER; PTHR37739:SF8; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR Pfam; PF15908; HMMR_C; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1388
FT /note="Kinesin-like protein KIF15-A"
FT /id="PRO_0000328688"
FT DOMAIN 26..364
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1127..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1388
FT /note="Necessary for its targeting to microtubule minus
FT ends"
FT /evidence="ECO:0000250"
FT COILED 369..1383
FT /evidence="ECO:0000255"
FT COMPBIAS 1131..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 1371
FT /note="L->K: Inhibits its targeting to microtubule minus
FT ends."
FT /evidence="ECO:0000269|PubMed:9813089"
SQ SEQUENCE 1388 AA; 159141 MW; 1F8825558B9AE28E CRC64;
MPPGTKGDPS NVTQPLPCLP SAEEDAIKVF VRIRPPVEGT LTGVDGEQGL CLTALSSTTI
RLHSKPEPKM FTFDHVANVD TNQESVFSSV AKNIVESCMN GYNGTIFAYG QTGSGKTFTM
LGPSESDNFT HNLRGVIPRS FEYLFFLINR EKEKAGEGKS FLCKCSFIEI YNEQIFDLLD
SASAGLFLRE HIKKGVFVVG AVEQVVTSAA EAYQVLSMGW RNRRVASTSM NRESSRSHAV
FTVTIESMEK TNDLVNIRSS QLNLVDLAGS ERQKDTQTEG VRLKEAGSIN RSLSCLGQVI
TALVDVANGR QRHICYRDSK LTFLLRDSLG GNAKTFYIAN VHPGSKCFGE TLSTLQFAQR
AKLIKNKAVV NEDTQGNVSQ LQAEVKKLKE QLSQLLSGQM PGDISVARVP SVGDNNMDYM
NNFIEAMMIL EKSDREKKVL LQKVVQLEDL CNKKEKFIQS NKMIVKFRED HISRLEKAHK
EGRISLSNNE QDDFIAELKE EIRTLKEQVE HHPRVAKYAL ENHSLREENK RLHSLQSVKR
AQEVTAQMIA ELEKAFLEVS VSEKDRQVAP MHSTPIQLDN NSLMSAARMR ERMLQLESEL
ATSKQEYEEF KELTKKKQVE QESELQSLIK SNQHLENILE AIKANKRHEV SQLNRMHAAE
TIKNMTTPTK SYNLRSRLVP RLSPDAMPNG LMDTPKSGDV MDDIINEPIP PEMSEQAYEA
IAEELRIVQE QVTALQAKLD EEEGKNIRLQ QQVNKLELCS TQIQELFNSE RSNWNKEQQD
LIAQIKSLEK QKQENKSQED VLKSEVHDLR VVLQSADREL GAVKGEYSLY REKQEKELSQ
LSARHMDVQL QLDNVRLEHE TLLEEKRSLQ DAFDNLEEVM KFEIDQLKQE ISDSKHENET
LRAEFSNLLE LLETEKERRQ KLTSQLEEDK ENKTKELLQV VDENMHLRKQ CSELMTKCEQ
QVTELHGLEH SLTSSKEMIA DLEKKNTADK EVVADLMNQI QVHRTTIIHK TESIDLLTRE
LEDIHSKYSI VLLAKEESKT VIEEQEKQIE ELRECLERKQ SADNIEKELL CDDLAHATEE
LEKLTEAFNK QEALLHTHEK ELVEKEQQIS ELTNQVKLMT DLEISREQEK IRPASSNSSS
PVVLPETPRT PEGNPYDSEI ANLQKRNTNL EILVSELNEE RTSKNEEIIR LKMQLCETEN
MRLEIQNLQG MCKELKSQLE NCNNVMKDSN DQKPSDMQDL KREIEKEVSE RMEKGKATEH
ILKLQAELEE TRNILCTKDH SLNELSKEIE RTRSLEAKAF TEKEEIRSIL EGKYEETEKL
SHELDMLRKQ VLFLAEENGK ILGHQNPNQK IQYLVKLKKE NNKLLEEAEK LRIENLFLKE
SKKCEHCN
//
