ID   KI15B_XENLA             Reviewed;        1387 AA.
AC   Q498L9; Q6GR48;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Kinesin-like protein KIF15-B;
DE   AltName: Full=Kinesin-like protein 2-B;
DE            Short=Xklp2-B;
GN   Name=kif15-b;
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 [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
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 (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC       pole {ECO:0000250}. Note=Localizes during metaphase on spindle
CC       microtubules, with a strong enrichment at spindle poles. Localizes to
CC       the minus ends of spindle pole and aster microtubules in a dynein- and
CC       dynactin-dependent manner. Detected diffusively in the cytoplasm.
CC       Localized at the centrosome during the interphase and throughout
CC       mitosis (By similarity). {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH71083.1; Type=Miscellaneous discrepancy; Note=Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; BC071083; AAH71083.1; ALT_SEQ; mRNA.
DR   EMBL; BC100163; AAI00164.1; -; mRNA.
DR   RefSeq; NP_001085266.1; NM_001091797.1.
DR   AlphaFoldDB; Q498L9; -.
DR   SMR; Q498L9; -.
DR   DNASU; 443568; -.
DR   GeneID; 443568; -.
DR   KEGG; xla:443568; -.
DR   CTD; 443568; -.
DR   Xenbase; XB-GENE-6252112; kif15.S.
DR   OrthoDB; 241787at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 443568; Expressed in egg cell and 12 other tissues.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB.
DR   GO; GO:0051299; P:centrosome separation; IMP:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:InterPro.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR031794; HMMR_C.
DR   InterPro; IPR044986; KIF15/KIN-12E.
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; PTHR37739; 1.
DR   Pfam; PF15908; HMMR_C; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 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; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1387
FT                   /note="Kinesin-like protein KIF15-B"
FT                   /id="PRO_0000328689"
FT   DOMAIN          26..364
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1138..1387
FT                   /note="Necessary for its targeting to microtubule minus
FT                   ends"
FT   COILED          369..1383
FT                   /evidence="ECO:0000255"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1387 AA;  158559 MW;  7B14ECD48511E0F3 CRC64;
     MPPGTKGDPS NVTQPLPCLP SAEEDAIKVF VRIRPPVEGT LTGVDGEQGS CLTALSSTTI
     RLHSKPEPKM FTFDHVANVD TTQESVFSSV AKNIVESCMN GYNGTIFAYG QTGSGKTFTM
     LGPSESDNFT HNLRGVIPRS FEYLFFLINR EKEKAGDGKS FLCKCSFIEI YNEQIFDLLD
     SASAGLFLRE HIKKGVFVVG AVEQVVTSAA EAYQVLSMGW RNRRVASTSM NRESSRSHAV
     FTVTIESMEK TNDIVNIRSS QLNLVDLAGS ERQKDTQTEG VRLKEAGSIN RSLSCLGQVI
     TALVDVANGR QRHICYRDSK LTFLLRDSLG GNAKTFIIAN VHPGSKCFGE TLSTLQFAQR
     AKLIKNKAVV NEDTQGNVSQ LQAEVKKLKE QLSQLLSGQM PGDISVARAP SVGDNMDYMN
     TFIEAMMLLE RSDSEKKALL QKVIQLEDLC NKKEKFIQSN KMIVKFREDH IVRLEKAHRE
     GQISLSNNEQ DNFIAELKEE IRTLKEQVEH HPRVAKYALE NHSLREENKR IGSLQSVKRA
     QEVSAQMMAE LEKAFLEASV SEKDRQVAPM HSTPIQLDNS SLMSAARMRE RMLQLESELA
     TSKQEYEEFK ELTKKKQVEQ ESELQSLMKS NQHLENILDA IKENKRHEVS QLNRMHAETI
     KNMTTPTKAY NLRSRLVPRL SLDGISNGLT DTPKSGDVMD DIINEPIPPE MSEQAYEAIA
     EELRIVQEQV TALQVKLDEE ESKNIKLEQQ VNKLELCSTQ IQELFNSERS NWNKEQQAFI
     AQIKSLEKQQ QDNKNQEDVL KSEVHDLRVV LQSADRELSA VKGEYSLFRE KQEKELSQLS
     ARHMAVQLQL DNFRLEHETL LEEKRSLQDA FDNLEEVMKF ETDQLKQELS DSKHENETLR
     AELSNLLELL ETEKERRQKL TSQLEEDKES KTKELLQVVD ENMHLRKQCS ELVTKCEHQV
     TELQRLEHSL TSSKEMIADL EKKNTADKEV VVDLMNQIQV HRTTIIHKTE SIDLLTRELE
     DINSKYSIVL LAKEECKTVN EEQEKQIEEL RESLERKQSA DNIEKELLCD DLAHATEELG
     KLTEAFNKQE TMLHACEKEL VEKEQLISEL TNKVKLMTDL EITKTEQEKI KPSHSNSNSP
     VVLAQTPRTP VGNPYESEFA NLQNRNTNLA VLISELNEER TLKNEEIIKL KMQLCETENM
     HLEIQNLQGI CKELKSQLEN CKKGMKDGNE QKPSDMQDLK REIEKEVSER MEKGKATEHI
     LKLQAELEET RNLLCAKDHS LNELNNEMER TRSLEAKAFT EKEQIRSVLE AKYEETEKLS
     QELDMLRKQV SFLAEENGKI LGHQNPNQKI QYLVKLKKEN DKLLEEAEKL RIENLFLKET
     KKCEHCD