ID   KIF15_STRPU             Reviewed;        1463 AA.
AC   Q9GYZ0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Kinesin-like protein KIF15;
DE   AltName: Full=Kinesin-related protein KRP180;
GN   Name=KIF15;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=10931863; DOI=10.1083/jcb.150.3.499;
RA   Rogers G.C., Chui K.K., Lee E.W., Wedaman K.P., Sharp D.J., Holland G.,
RA   Morris R.L., Scholey J.M.;
RT   "A kinesin-related protein, KRP(180), positions prometaphase spindle poles
RT   during early sea urchin embryonic cell division.";
RL   J. Cell Biol. 150:499-512(2000).
CC   -!- FUNCTION: Plus-end directed kinesin-like motor enzyme involved in
CC       mitotic spindle assembly. Plays a role in positioning spindle poles
CC       during mitosis, specifically at prometaphase.
CC       {ECO:0000269|PubMed:10931863}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10931863}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       spindle {ECO:0000269|PubMed:10931863}. Note=Localizes at the central
CC       spindle.
CC   -!- DEVELOPMENTAL STAGE: Expressed in eggs.
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; AF284333; AAG01844.1; -; mRNA.
DR   RefSeq; NP_999656.1; NM_214491.1.
DR   AlphaFoldDB; Q9GYZ0; -.
DR   SMR; Q9GYZ0; -.
DR   STRING; 7668.SPU_021317-tr; -.
DR   GeneID; 373236; -.
DR   KEGG; spu:373236; -.
DR   CTD; 56992; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   InParanoid; Q9GYZ0; -.
DR   OrthoDB; 241787at2759; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; 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: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   GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:InterPro.
DR   Gene3D; 3.40.850.10; -; 1.
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; 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..1463
FT                   /note="Kinesin-like protein KIF15"
FT                   /id="PRO_0000328687"
FT   DOMAIN          18..354
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          387..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1335..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1409..1444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          436..517
FT                   /evidence="ECO:0000255"
FT   COILED          586..646
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        395..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1409..1428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         99..106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1463 AA;  166590 MW;  1E8BFC2BB5AEF94D CRC64;
     MSKKLKEQAA NDASEGDAIK VFVRVRPSES HDADAAFGQC LEVRLPDTII MHSKPEPKVF
     TYDHVTAANT TQESVFTAVG KRIIESCVGG FNGTIFAYGQ TGSGKTFTML GPCEDGDNFH
     HEMRGVIPRS FEYLFSLVNR EREKHGDRYE FLCRCSFLEI YNEQIYDLLD PASLGLHLRE
     NMKKGVFVDG LIERAVASAS EAYGVLQAGW HNRRVAATSM NRESSRSHAV FTVSIESKEK
     KAGVSNIRVS QLHLVDLAGS ERQKDTKAIG VRLKEAGSIN KSLSILGNVI MALVDIAHGK
     QRHVPYRDSK LSFLLRDSLG GNAKTYIIAN VHPDAKCFGE TLSTLKFARR AKMIKNRAVV
     NEDTQGNVMH LQAEIRRLRE ALCMKGAEGS IPRGPSESGD SQMSNSSTES NGPVSGQQSG
     SSSSSKWKKY FLEAMSLRDI VEVEKREMRE KVSSLEELCS KRDQVISSNK MIIKFRNSTI
     DMLQKTKNKA LLKEDRDLLN ENLKKEIEQL QEQLEHNPFV MRYVVENQSL RAQNKKLKMM
     EAVRSGEAMA ATKAEELETL FLELREGLSK NRRYSSTPVD GEKVPTSTLV ILKSQIKKLQ
     DELENAKQEH AEQEEMTRTT RLDLESELAA YKKANLDMEK TLQGMKIKNR MDRDAMNDIH
     MQTIKSITTP KKVTYQLRSR TVLRTAGEET PGGPGFAGLS DNGSPLRSHS TNSLPPSGDI
     LVTNSSPAMS EEGIIDEEMP EHVIEQCNEA LTIELQKLQD KNANLQQQLE EHESQKHKML
     QNSSKLDHQL QQITELYSTE SQAWQEHEKD LTTRLAEATI QISTLQRDYE MTRGEAEDFK
     VMLQAADKEI GQEKKQKSKV TQDWDRVRAA LDAQVVRLEN EMCGQSRELE NLTEDREQLQ
     DAYNTLQAEH EFQQQREADL ENRLKGKKAE ITQLQEEIQK HLEKLDSERD KSMRLTAELR
     QGDNTKKDLL DAQELIDQFR EERDDLLHRL DTEALKLSSS KEDLETVNSA LTAIKKTDVE
     QKEALSSLMA ALQGQKGMVK DKEEQLASMQ MQLEDTRGQV SLLEAALEEG KASGAGLQSQ
     IAALEDRMHA QAGEYQEQIE QMRADAMDAN QHQKELLKEL EKQSEELTQL HKQMKEKEEE
     YETKESEHKD TIESLEEQLE EVKTNLSTVV VELDEPESKK RKMADAQAME IESLRDSEKR
     FKELSSVYDN MRDQMNEEIR SLKMKADELE DVRISKEILQ AQHTALTYEI EQVRNEMAEK
     ESSLKDEVNH LKRDMERQKT VLASMLRDKD EAVEKLYTVQ TTLDQVKANE EILQENMDQV
     MEELDRTSAL ESTHFKEKED IKSKLEEERE EKSKLTKDLT RLKEVYEEAE KKITELGGHQ
     NPKQKIHHLQ AVKSENYFLK EEVESLEKQL GKAQSDSEQM KRDYEALQKR LTSSSAEPPE
     EAGATTCIRC LPHSKRIMQT QTA