KIF1_DICDI
ID KIF1_DICDI Reviewed; 2205 AA.
AC Q9NGQ2; Q54F81;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Kinesin-related protein 1;
DE AltName: Full=Kinesin family member 1;
DE AltName: Full=Kinesin-3;
GN Name=kif1; Synonyms=kif1A, unc104; ORFNames=DDB_G0290963;
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, AND SUBUNIT.
RX PubMed=10545495; DOI=10.1083/jcb.147.3.493;
RA Pollock N., de Hostos E.L., Turck C.W., Vale R.D.;
RT "Reconstitution of membrane transport powered by a novel dimeric kinesin
RT motor of the Unc104/KIF1A family purified from Dictyostelium.";
RL J. Cell Biol. 147:493-506(1999).
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, SUBCELLULAR LOCATION, DOMAINS, AND MUTAGENESIS OF
RP 1530-LYS--LYS-1533.
RX PubMed=12015984; DOI=10.1016/s0092-8674(02)00708-0;
RA Klopfenstein D.R., Tomishige M., Stuurman N., Vale R.D.;
RT "Role of phosphatidylinositol(4,5)bisphosphate organization in membrane
RT transport by the Unc104 kinesin motor.";
RL Cell 109:347-358(2002).
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. Transports cytoplasmic vesicles and
CC particularly phosphatidylinositol 4,5-bisphosphate-containing liposomes
CC along microtubules. {ECO:0000269|PubMed:10545495,
CC ECO:0000269|PubMed:12015984}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10545495}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12015984}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:12015984}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12015984}; Cytoplasmic side
CC {ECO:0000269|PubMed:12015984}.
CC -!- DOMAIN: The PH domain is required for kif1-mediated transport probably
CC through its binding and docking onto membrane of cargo vesicles.
CC {ECO:0000269|PubMed:12015984}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AF245277; AAF63384.1; -; mRNA.
DR EMBL; AAFI02000174; EAL61912.1; -; Genomic_DNA.
DR RefSeq; XP_635456.1; XM_630364.1.
DR AlphaFoldDB; Q9NGQ2; -.
DR SMR; Q9NGQ2; -.
DR STRING; 44689.DDB0201559; -.
DR PaxDb; Q9NGQ2; -.
DR PRIDE; Q9NGQ2; -.
DR EnsemblProtists; EAL61912; EAL61912; DDB_G0290963.
DR GeneID; 8627956; -.
DR KEGG; ddi:DDB_G0290963; -.
DR dictyBase; DDB_G0290963; kif1.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_231165_0_0_1; -.
DR InParanoid; Q9NGQ2; -.
DR OMA; NPSTGPY; -.
DR PRO; PR:Q9NGQ2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:dictyBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:dictyBase.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0072386; P:plus-end-directed organelle transport along microtubule; IDA:dictyBase.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; IDA:dictyBase.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:dictyBase.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 3.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF49879; SSF49879; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Membrane; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..2205
FT /note="Kinesin-related protein 1"
FT /id="PRO_0000365576"
FT DOMAIN 2..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 483..595
FT /note="FHA"
FT DOMAIN 1523..1616
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 525..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..448
FT /evidence="ECO:0000255"
FT COILED 1879..1918
FT /evidence="ECO:0000255"
FT COILED 1946..2034
FT /evidence="ECO:0000255"
FT COILED 2075..2149
FT /evidence="ECO:0000255"
FT COMPBIAS 525..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 1531..1533
FT /note="KKK->EEE: Decreases liposome transport in vitro."
SQ SEQUENCE 2205 AA; 248003 MW; 02C5101E9D61C9ED CRC64;
MNVQVAVRVR PFNSREKERN AELIVQMNNK STILTRPSAL RANPLAAPTA DDEKSFSFDY
SYWSYDSNDP HFASQSTVYN DLGKEVLKNA WDGFNCSIFA YGQTGSGKSY SMMGYGEEKG
IIPLICEELF QRIQSTPSNS NEQTIYKTTV SYMEIYNEKV KDLLNPNNNK TGGLKVRNNP
STGPYVEDLS KLAVKSFSEI DMLMDEGSKA RTVASTNMNA TSSRSHAVFT IVFTQSKIDK
TRGTAIDRVS KISLVDLAGS ERANSTGATG VRLKEGANIN KSLSTLGKVI SALAENSTSK
KAVFVPYRDS VLTYLLKETL GGNSKTIMIA AISPADINYE ESLSTLRYAD SAKKIKTVAV
VNEDAQSKLI RELQGEVERL RAMMDQGGQY HANDSKLMNS DYDETVSTLN EKIEQYEKLM
AELNKSWEEK LSEAEAIRED RMAALKDMGV AIKVVSSIPH LINLNEDPLM SESLIYYVKE
GKTRIGRSDS EIPQDIILNG LNIHKEHCIF ENINGKVIIS PSNNFMNNNN NKENSSSTTP
TSSKSPSKPK SEKEKENNND DDDGEKKLDR SYIYVNGVEI NKPTILTTGN RVILGNNHIF
RFNNPEEAIK IARERNQTTG GIVSSTKSPV DQIMDYDFAL NELASIQGTL AMSKHINDKQ
EYKKQMRALY DQIRLQLEND CDPEVKEQRE KLALLAFRRW RSKVHRSKLL NKISFIILSL
NEANAISSTL NKKINLSLKL YSVFPEPDQI SDNIEPEIDW RKTQILIKAT DSSTGESTLV
TDQDFVDRIY LMRELYQNDG RLDTELPEDP FQFTFTKDSL IGVSHVYLKN TLYLVESNRP
VPILDENGNQ KGYLNLLVSS SSTDITESER GLYLENPSNN KSLLLGKNLE ITIGFEGFSE
FIDENKFSDV FIKFNFPNQN GTIVDTFLTE PQPISAFIDQ KRIVITSLTE SLINLLQTQY
VSFEIRGHKK SKQQPKLTSS SSSASTTSSS SKNQPMLENF EFLATLNILE SEKNTGTDDQ
YKPVHILEDP DVYNTHLPSV TFRLKKDKTN RQILFKVIKN ESNSIIKECK SARISDIKIF
GKRDNPLLSS SATPNTPNTP NNSRIAGIQN TPGTPMTPYS NQTNNQQSSS SQPPLPQQQG
TPYNPQSNNP NVISNAPPTP NSNLLKDLSL AANVQTSSSS SSSSLNVLLN NQQQQQQSQQ
SQQQQQQQSQ QSSETSSTTN SITNSASNSS LSLLVNNQTT NSNNSGGNIF EIPVLSCTDD
SVLLLWKTND PSFIFNQKTR KGDKILFKLT FDLLIQGFPD VVSISKDIAI KILSSESMPS
ATMPDGTSSS SMSNLLDKFK THFKGESILS EPSIHAGSVF SINLTKSRQQ EHQNRIGEMI
DAHQENILKL GYAMKMEKLR QELDLREKLT NLKEKTIDST NTDDVNAANG VAESSNSSTI
DVEEIVKKML LMNSTHQQQQ QNFSSPSSTS PTLVNGESSP KSGRSSNTTS SSSGGGGGGG
RKRSSTIVEV KVKEVPSSAL LKEDETSGYL KKKSAFKEEW KPRWFVFKKP YLYYSHNQKD
THKLKKIDLT NSSVAITQDE VPFGFAIIQL RRVWLLQANS VEDRDKWVQT LDPLRKVTEL
KDEELRTAKQ QIEKSSSQLD QIKSQLQTGQ QIVLAKQKEI EELTNTISQL QLEKEINTQQ
FDGLRDEIQN RDEELEQYKS QQSQKINQLS GQVNKLENVT QEKELTIGSL SSTLNNTNQI
IELINEQSKS YKNVAEMEIE SLRDETTQLR ETSQLLANRL KECRSSIQSA ESLLSERDLE
ITQLKALLTQ QEESSGITSL NLKNLQSDQT MKQGQIDILS KTVQQSTATI QNISSQLDST
TKASDSKDEQ ITSINSAYKD ESDRLKDQTT QLNSLTTNLR QQMRSLEQTH LQQKETSASD
QKTLLLLLHD MEQGLTRASQ TITDQSAQVT VLKKQLEDSK KSNEQLPTVE KQLSLMKDRL
IQSENQLIDR ECENTILSDK LKLWEEEIKI KDSKLSLLEN NVKEVRAEYA NGMAFSREFS
QHHTDSGSIS GKFNRRSKQI SAEEQMETLR ESSIAHQSHN AFLNSQIQRL ETEMRTQEKV
YSDTIQRIKK DLQQRNQQNI AFMKHQVGDE IVKKMEDVTA SMEILKKKYF VSLVVAAKLQ
NAMMGNICNV DAYELYEQSV VEHILDQDQW PNWIAQTIST QNKHL
