KIF2_DICDI
ID KIF2_DICDI Reviewed; 792 AA.
AC Q9BPU3; O15718; Q55GP9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Kinesin-related protein 2;
DE AltName: Full=Kinesin family member 2;
DE AltName: Full=Kinesin-14;
GN Name=kif2; Synonyms=GPK2, K2, ksnB; ORFNames=DDB_G0267396;
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], AND INDUCTION.
RC STRAIN=AX2;
RX PubMed=9693369; DOI=10.1091/mbc.9.8.2093;
RA de Hostos E.L., McCaffrey G., Sucgang R., Pierce D.W., Vale R.D.;
RT "A developmentally regulated kinesin-related motor protein from
RT Dictyostelium discoideum.";
RL Mol. Biol. Cell 9:2093-2106(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=AX2;
RX PubMed=10854856; DOI=10.1016/s0014-5793(00)01619-7;
RA Iwai S., Suyama E., Adachi H., Sutoh K.;
RT "Characterization of a C-terminal-type kinesin-related protein from
RT Dictyostelium discoideum.";
RL FEBS Lett. 475:47-51(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 89-792.
RC STRAIN=AX3;
RA Mayorga O., de Hostos E.L.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND NOMENCLATURE.
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).
CC -!- FUNCTION: Microtubule-dependent motor that is probably involved in
CC microtubule organization in the mitotic spindle.
CC {ECO:0000269|PubMed:10854856}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10854856}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:10854856}. Note=Localizes in
CC the nucleus at the interphase and on the mitotic spindle during
CC mitosis.
CC -!- INDUCTION: During the developmental stage.
CC {ECO:0000269|PubMed:9693369}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC16438.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AB037280; BAB21252.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73150.1; -; Genomic_DNA.
DR EMBL; AF015712; AAC16438.1; ALT_SEQ; mRNA.
DR RefSeq; XP_647135.1; XM_642043.1.
DR AlphaFoldDB; Q9BPU3; -.
DR SMR; Q9BPU3; -.
DR STRING; 44689.DDB0191126; -.
DR PaxDb; Q9BPU3; -.
DR EnsemblProtists; EAL73150; EAL73150; DDB_G0267396.
DR GeneID; 8615938; -.
DR KEGG; ddi:DDB_G0267396; -.
DR dictyBase; DDB_G0267396; kif2.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_1_1; -.
DR InParanoid; Q9BPU3; -.
DR OMA; ECFFLEI; -.
DR PhylomeDB; Q9BPU3; -.
DR PRO; PR:Q9BPU3; -.
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; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0003777; F:microtubule motor activity; IDA:dictyBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:dictyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PS50067; KINESIN_MOTOR_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Nucleus; Reference proteome; Transport.
FT CHAIN 1..792
FT /note="Kinesin-related protein 2"
FT /id="PRO_0000365577"
FT DOMAIN 437..781
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 22..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..423
FT /evidence="ECO:0000255"
FT BINDING 528..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 792 AA; 89360 MW; 023EA2EFD99EB76F CRC64;
MEKRQLYSSQ SQSQPLNIIT NTINSRPSLL RKPASSSSQS NDRISYPPST DSKFIQQQYH
QPLLTNTDIK LEDIESSSSN NNPLKNSINN VSMQISQLNS SHHSRALLMQ KRNNPTTNIR
PTVKKKLDDT HKPLTSNFKK PITPISKLNT NMNNNNINNK NNNININSNN SSNSNNNILS
PVQNNTISPN SNLLNSSIKF EKSNFFSTMY SSPTTITTTS TTLNNDNNNN ISISSSCSNN
SSFDLQQQHA LHERMNKIDQ FTQTVRGNLQ SQFDNISEQL KPPRLSLSIQ DIKTRLDFEE
KNKEVEKIKL ELKNVLQSLK EKEKELMEAH YKVSQVSVLK DNMERDLQQS NQMILDLQHE
IRSSSLKAIQ VDEKFNNMKD VTKDLDDEIL RLNQLVRERD TEIESLRKEN RELLEKSRSD
EKVRRKLHNT IQELKGNIRV FCRIRPDFSS GQGANGSVFN IPAGTDNLVE VKSPTIDSFN
GEASIKKSTF TFDRVFGPSS TQELVFEDIS QLVQSSLDGY NTCIFTYGQT GSGKTHSILG
DLKVPSQRGM IPRTVEKIFS SIQDLTEKGW TYQIECFFLE IYNETINDLL NTTTTTTGGN
SKSNEIKYEI KHNPDTNVTT VTNMTVVPVT HPSQVYELLN LANKNRSVAK TLCNERSSRS
HTVFQLKLIG YNQQSSERTQ GLLNLIDLAG SERVSRSGVE GKQLKETQAI NKSLSSLGDV
ISALANKEQH IPYRNSKLTF LLQNSIGGNS KTLMFVNISP ELKDLQESTS SLRFAAKVNS
CELGAARKQK II
