KIF15_RAT
ID KIF15_RAT Reviewed; 1385 AA.
AC Q7TSP2; Q7TN17;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Kinesin-like protein KIF15;
DE AltName: Full=Kinesin-like protein 2;
GN Name=Kif15; Synonyms=Klp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=14618103; DOI=10.1023/a:1027332432740;
RA Buster D.W., Baird D.H., Yu W., Solowska J.M., Chauviere M., Mazurek A.,
RA Kress M., Baas P.W.;
RT "Expression of the mitotic kinesin Kif15 in postmitotic neurons:
RT implications for neuronal migration and development.";
RL J. Neurocytol. 32:79-96(2003).
CC -!- FUNCTION: Plus-end directed kinesin-like motor enzyme involved in
CC mitotic spindle assembly. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MKI67 and TPX2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:14618103}. Note=Colocalizes with TPX2 in
CC mitosis (By similarity). Detected during the interphase in the
CC cytoplasm as finely punctuate pattern and irregularly shaped dots.
CC Localizes at the spindle poles and microtubules prior to anaphase.
CC Localizes at the central spindle at anaphase. Localizes at the sites of
CC invaginating cell membranes, a position that corresponds to the
CC location of the contractile actomyosin ring of dividing cells.
CC Colocalizes with actin in interphase. Colocalizes in dendrites and in
CC growth cone of axons with microtubules. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in sympathetic neurons.
CC {ECO:0000269|PubMed:14618103}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain at 17 dpc and in cerebellum at
CC 19 dpc. {ECO:0000269|PubMed:14618103}.
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; AY291580; AAP44512.1; -; mRNA.
DR EMBL; AY291581; AAP44513.1; -; mRNA.
DR RefSeq; NP_853666.1; NM_181635.2.
DR AlphaFoldDB; Q7TSP2; -.
DR SMR; Q7TSP2; -.
DR CORUM; Q7TSP2; -.
DR STRING; 10116.ENSRNOP00000030707; -.
DR iPTMnet; Q7TSP2; -.
DR PhosphoSitePlus; Q7TSP2; -.
DR jPOST; Q7TSP2; -.
DR PaxDb; Q7TSP2; -.
DR PRIDE; Q7TSP2; -.
DR GeneID; 353302; -.
DR KEGG; rno:353302; -.
DR UCSC; RGD:727790; rat.
DR CTD; 56992; -.
DR RGD; 727790; Kif15.
DR eggNOG; KOG4280; Eukaryota.
DR InParanoid; Q7TSP2; -.
DR OrthoDB; 241787at2759; -.
DR PhylomeDB; Q7TSP2; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q7TSP2; -.
DR Proteomes; UP000002494; Unplaced.
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; IPR031794; HMMR_C.
DR InterPro; IPR044986; KIF15/KIN-12E.
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; PS50067; KINESIN_MOTOR_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1385
FT /note="Kinesin-like protein KIF15"
FT /id="PRO_0000328686"
FT DOMAIN 26..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..1385
FT /evidence="ECO:0000255"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 1007
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS87"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS87"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS87"
FT CONFLICT 473
FT /note="L -> R (in Ref. 1; AAP44512)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="K -> I (in Ref. 1; AAP44512)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="E -> D (in Ref. 1; AAP44512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1385 AA; 159540 MW; A640E2250DA6A0F6 CRC64;
MAPGCKSELR NVTNSHSNQP SNEDDAIKVF VRIRPAEEGA RSADGEQSLC LSVLSQTALR
LHSNPDPKTF VFDYVAGMDT TQESVFSTVA KSIVESCMSG YNGTIFAYGQ TGSGKTFTMM
GPSDSDNFSH NLRGVIPRSF EYLFSLIDRE KEKAGAGKSF LCKCSFIEVY NEQIYDLLDS
ASVGLYLREH IKKGVFVVGA VEQVVASAAE AYQVLSRGWR NRRVASTSMN RESSRSHAVF
TITIESMEKS SEAVNIRTSL LNLVDLAGSE RQKDTHAEGM RLKEAGNINR SLSCLGQVIT
ALVDVGNGKQ RHVCYRDSKL TFLLRDSLGG NAKTAIIANV HPGSRCFGET LSTLNFAQRA
KLIKNKAVVN EDTQGNVSQL QAEVKRLREQ LSQFTSGQLT PGSSLARDKE KANYMEYFLE
AMLFFKKSEQ EKKSLVEKIT QLEDLTLKKE KFIQSNKMIV KFREDQIMRL ERLQKEARGS
FLPEEQDRLL SELRDEIRTL REQVEHHPRL AKYAMENHSL REENRKLKLL APVKRAHELD
AQAIARLEQA FSEVSSTETN DKGLQGLPPK AIKEPSFFTS TEKLKVQLLQ IQTELNNSKQ
EYEEFKELTR KKQLELESEL QSLQKANLNL ENLLEATKVC KRQEVSQLNK IHAETLKIIT
TPTKAYQLCS RLVPKSSPEV GSFGFLRSQS APDNDILNEP VPPEMSEQAL EAISEELRTV
QEQLSVLQVK LDEEEHKNLK LQQNVDRLEH HSTQMQELFS SERSDWSKQQ QDYLTQLSDL
EKQLQDAQTK NDFLKCEVHD LRIVLNSADK ELSLVKLEYS TFKESQEKEL SQLSERHVQV
QLQLDNARLE NEKLLESQAC LQDSYDNLQE VMKFEVDQLS KNLQNCKQEN ETLKSDLHNL
VELFEAEKER NNKLSLQFEE DKENSSKEIL KALETVRQEK QEEMARCEKQ MAKVQELEES
LLAAENVVSC LEKSRESDKE LVTNLMNQIQ ELRTSAGEKS EAIDTLKQEL QDISCKYTAA
VADKEESKEL IRRQEVDILE LKETLRLRIL SEDIERDMLC EDLAHATEQL NMLTEASKKH
SGLLQSAQEE LTKKEALIQE LQHKLNQEKE EVEQKKSEYN LKMKQLEHVM GSAPEYPQSP
KTPPHFQTHL AKLLETQEQE IEDGRASKMS LQHLVTKLNE DREVKNAEIL RMKDQLCEME
NLRLESQQLR ERTWLLQTQL DDMKRQGESS SQSRPDSQQL KNEYEEEIIR ERLAKNKLIE
EMLKMKTDLE EVQSALDSKE KFCHRMSEEV ERTRTLESRA FQEKEQLRSK LEEMYEERER
TCQEMEMLRK QLEFLAEENG KLIGHQNLHQ KIQYVVRLKK ENIRLAEETE KLRAENVFLK
ERKKE
