KIF5_DICDI
ID KIF5_DICDI Reviewed; 990 AA.
AC Q8T135; Q551S3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Kinesin-related protein 5;
DE AltName: Full=Kinesin family member 5;
DE AltName: Full=Kinesin-1;
GN Name=kif5; Synonyms=kin5; ORFNames=DDB_G0276369;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH ACTIN.
RX PubMed=14623897; DOI=10.1074/jbc.m308022200;
RA Iwai S., Ishiji A., Mabuchi I., Sutoh K.;
RT "A novel actin-bundling kinesin-related protein from Dictyostelium
RT discoideum.";
RL J. Biol. Chem. 279:4696-4704(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
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 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-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). May connect microtubules to
CC actin filaments. Associates with actin-based structures in cells and is
CC likely involved in the organization of actin cytoskeletons in such
CC structures. {ECO:0000250, ECO:0000269|PubMed:14623897}.
CC -!- SUBUNIT: Interacts with actin. {ECO:0000269|PubMed:14623897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14623897}.
CC -!- DOMAIN: Composed of three structural domains: a large globular N-
CC terminal domain which is responsible for the motor activity of kinesin
CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC coiled coil domain that mediates the heavy chain dimerization; and a
CC small globular C-terminal domain which interacts with other proteins,
CC vesicles and membranous organelles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AB102778; BAC56910.1; -; mRNA.
DR EMBL; AAFI02000014; EAL69265.1; -; Genomic_DNA.
DR RefSeq; XP_643173.1; XM_638081.1.
DR AlphaFoldDB; Q8T135; -.
DR SMR; Q8T135; -.
DR STRING; 44689.DDB0185205; -.
DR PaxDb; Q8T135; -.
DR PRIDE; Q8T135; -.
DR EnsemblProtists; EAL69265; EAL69265; DDB_G0276369.
DR GeneID; 8620445; -.
DR KEGG; ddi:DDB_G0276369; -.
DR dictyBase; DDB_G0276369; kif5.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_301776_0_0_1; -.
DR InParanoid; Q8T135; -.
DR OMA; MATSCNI; -.
DR PRO; PR:Q8T135; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; TAS:dictyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:dictyBase.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
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 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; Transport.
FT CHAIN 1..990
FT /note="Kinesin-related protein 5"
FT /id="PRO_0000365580"
FT DOMAIN 6..330
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 401..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 513..948
FT /evidence="ECO:0000255"
FT COMPBIAS 732..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 990 AA; 110435 MW; AA682C4877079440 CRC64;
MATSCNIRVM CRFRPLNERE KALKENQTCV TFPDETQVIV SGQPFTFDRV FTPESTQKEV
FESVKDTIHD VLLGYNGTLL AYGQTGSGKT FTMGSAAAES DFENVEQLGI IPRGNHLIFN
TIAEESDGNA EFTIKCSYLE IYMENIQDLL NPKNNKQLKI RESKSQGIYV EGLTEEYVAS
EEDIMELIQV GESSRSVAKT NMNQRSSRSH SILIIAIEQK SSDGSKKRGK LNLVDLAGSE
KVSKTGAEGI VLEQAKKINQ SLSLLGNCIH ALTDSKREHI PFRDSKLTRL LQDSLGGNTK
TTLLVTASPH FNNVDETIST LKFGARAKSI KNNVKVNQEK SAAELQIIVN ALTKELSILK
VYSISLENLV NYFKSSSYQP GNPIPKELEP NKQNLLLLQQ QSNSSSGGGG SGSSGGSSNG
SLMMKPRSTT PTPPSINRPH SSASTHRHSI AITGTHSKEG SGGGLTSSIS SSSISSMSSL
SSSIDNDYNG SSLDDSNGSN GLFNPLAIVE MSIEMEKMKE DTQLLIEKFK DEISEITIQY
QSTQEELNQC RQQLDQIKEQ LEQQRSQFIK EQSLLKESER NATLDSTSKD LKIQSLISKI
EDLRLLASQV IQYLERKRLS DDFDIGIFMG SQDGANGDSA NMFSLISNSI DQGTYEDDVN
IEDIIRYLSE EEVLTMQVKL QLQNKVHQLE QKIQQLVSDL NTTEINYNQS ILQCQKFESE
NSLIKRKFKS MFSSSNNNNN NNNSPPSSPS SKLLIQSSNN NNNFDSNLNS SSLSSSLPSS
NGIEQDQQVD HQVDHQVEND HLVNDEDNKL LDENSKLKEN ELKLLLEIKN LKLQSEKSND
ETLKWKDELS IKSALYQNQI LNLQNENQSL SNKLNVEKQQ KQSSQSQQIE FATKLNDLIK
SSEDDKELYR NEKNQMELEI ASLKASLDEM DLKNKELQDQ LISTQRLIGA RRVVKIVRGG
ADSMKTALAT KEVFGQFTLR KTENSKTLFQ
