KIF12_DICDI
ID KIF12_DICDI Reviewed; 1499 AA.
AC Q6S000; Q55FA0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Kinesin-related protein 12;
DE AltName: Full=Kinesin family member 12;
DE AltName: Full=Kinesin-6;
GN Name=kif12; ORFNames=DDB_G0268258;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND NOMENCLATURE.
RC STRAIN=AX4;
RX PubMed=14641909; DOI=10.1186/1471-2164-4-47;
RA Kollmar M., Gloeckner G.;
RT "Identification and phylogenetic analysis of Dictyostelium discoideum
RT kinesin proteins.";
RL BMC Genomics 4:47-47(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15546981; DOI=10.1073/pnas.0407304101;
RA Lakshmikanth G.S., Warrick H.M., Spudich J.A.;
RT "A mitotic kinesin-like protein required for normal karyokinesis, myosin
RT localization to the furrow, and cytokinesis in Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16519-16524(2004).
RN [4]
RP FUNCTION.
RX PubMed=18326585; DOI=10.1128/ec.00422-07;
RA Li H., Chen Q., Kaller M., Nellen W., Graef R., De Lozanne A.;
RT "Dictyostelium Aurora kinase has properties of both Aurora A and Aurora B
RT kinases.";
RL Eukaryot. Cell 7:894-905(2008).
CC -!- FUNCTION: Microtubule-associated force-producing protein that plays a
CC role in organelle transport. Its motor activity is directed toward the
CC microtubule's plus end (By similarity). Required for cytokinesis. May
CC be involved in a vesicle-mediated transport of myosin II, the Aurora
CC kinase (aurK) and other proteins along mitotic extracellular
CC microtubules toward the center of the cell and the cleavage furrow in
CC order to ensure cell division coupled to mitosis. {ECO:0000250,
CC ECO:0000269|PubMed:15546981, ECO:0000269|PubMed:18326585}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15546981}. Nucleus {ECO:0000269|PubMed:15546981}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15546981}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:15546981}. Note=Concentrates in the nucleus in
CC interphase cells, translocates to the cytoplasm at the onset of
CC mitosis, appears in the centrosomes and spindle, and later is
CC concentrated in the spindle midbody.
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; AY484465; AAR39441.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73582.1; -; Genomic_DNA.
DR RefSeq; XP_647633.1; XM_642541.1.
DR AlphaFoldDB; Q6S000; -.
DR SMR; Q6S000; -.
DR STRING; 44689.DDB0201555; -.
DR PaxDb; Q6S000; -.
DR EnsemblProtists; EAL73582; EAL73582; DDB_G0268258.
DR GeneID; 8616448; -.
DR KEGG; ddi:DDB_G0268258; -.
DR dictyBase; DDB_G0268258; kif12.
DR eggNOG; KOG0247; Eukaryota.
DR HOGENOM; CLU_248781_0_0_1; -.
DR InParanoid; Q6S000; -.
DR OMA; DYISMEK; -.
DR PhylomeDB; Q6S000; -.
DR Reactome; R-DDI-68884; Mitotic Telophase/Cytokinesis.
DR PRO; PR:Q6S000; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000912; P:assembly of actomyosin apparatus involved in cytokinesis; IMP:dictyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0000280; P:nuclear division; IMP:dictyBase.
DR GO; GO:1905345; P:protein localization to cleavage furrow; IMP:dictyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009612; P:response to mechanical stimulus; IDA:dictyBase.
DR Gene3D; 3.40.850.10; -; 1.
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 PANTHER; PTHR24115; PTHR24115; 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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Nucleus; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1499
FT /note="Kinesin-related protein 12"
FT /id="PRO_0000365587"
FT DOMAIN 126..570
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 739..923
FT /evidence="ECO:0000255"
FT COILED 1134..1257
FT /evidence="ECO:0000255"
FT COMPBIAS 252..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1499 AA; 168307 MW; 29C0F135CAA20361 CRC64;
MKDYISSPLS PSNKKMPDNQ KISPTNTPIR KKLFENTQSP IHFISNNNNN NITTPAKGLA
SVIKFNSSNY GNHHHQHHHQ HHNNNNNSTV SGSAIKQHLN KSTFSTSGTT LTSSSDAILL
PEDKVPMSVY LRIRPLSKKE IESKESNCFT VLNTTSVSIK SSRSDSDSNK FSFSSVLPPN
TTQPQLFKTI THPLIQSFLT GHNVLLLAYG VTNAGKTYTV SGSKRNPGII PRSLDLIFKS
IPNNCLKKTE NLTLSNNNNN STNNNSKDSK DILADSSDDE YTKVDNIDSS DEDDSNAKIN
SNLLESFSTT NTTATTNAAA AASSTTATSN GDVIQISDQF NYSIWISYYE IYKKNIYDLL
DDSPSSKKKQ SLKIESDNSV VNIKGLKEIL VSSVEDARDI VEQGESNRKV GGTKLNATSS
RSHAVLTIKL FTSPRHIPKS DIHPSQIRCS KLCIIDLAGS ERASRTETTG ETFKEGSSIN
TSLFTLGKCI EGLKQQALQQ QQQQQQHSSK RQSIHHSNPI PWRESDLTRI CQEYFCGNGK
ASMIVNVSPS SCDSEETLNV LRFSASAKEI TTLSKIKPMV FLPPPPTTPS ISLKKRKSME
QPINNNNNNN NNNNNNAYYN ITQLQNSVNE IKKKIHLDNL LAVGQLPISN NNNNNNGKFD
YISMEKDQLL DQIQIYQKKL SNYEIKFVES EVTLREEFNN ELIKNYIELE NQYKERLVKE
SQLIHDRVQS KLSLIKNVNI NQTNKLNCKI EKLELQLEQQ QQKTMEANNK ALVIVPQTNK
RTDDEWIIEI TEVQTERDNI QNKLNSILFE LDEQRQHNQF SLERIQQFTL QTEQLEIERE
NLLTEIESMQ SKGQELIKLR ELEMMQLKES MNSDAQKDRE NLEIQHNFET SNLNNQLQME
RQEKLQIIEE MRMLKLELQQ FKSNQSIEQQ RNNNLIKNQY YNHNHPTAAT AMTTTTPPIM
STPPIMSTPI KISSVGKFKA TPSKSLIKNI LGAHSNSPFK NANIESSVGG GFKVQLNIPG
SPIQLAPGTP NSIQSQTPDR PILDPNQYSD SGLLMQEIDD DDYLNITGGG SANDGNWTDI
NVNDDSASEY DDLNSSSKSF TKKPKKTKSF GTIKRIKAVA MIPANIASSA LNSSTTNIDE
KEKLEKLEKL EKEKERLEKE RLEKEKEKER LEKEREKEKE RLEKERERLE KEKEKERERL
EKEREKEKES KPKVVKKTTS SSSIISKKPS SKTTSSLTNN NNNNNNNNNN NNNNNNNNNN
NNNNKSISPI KTVQSPNSPS PTKLQPHSSP NTNAKEYFNL MNPQVIIHFR EPETNFVPSV
TANTTTSTST STSKSSKKTL DSLKDTPKKI ANIFSSKSSK EKEASTSSKS SSKISSSTST
TSTAPKLKRF AAITASHSIE NGSESSPIEV DTPPRITKKP PVPIVSKVSS KKVSSSSSST
SSSSSSAATI KRVRKIVNEK KNYLEDDDDD VITKMATETP RKTLGLRPRN LISQPIQFR
