KIF7_DICDI
ID KIF7_DICDI Reviewed; 1255 AA.
AC Q54TL0; Q94463;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Kinesin-related protein 7;
DE AltName: Full=Kinesin family member 7;
DE AltName: Full=Kinesin-1;
GN Name=kif7; Synonyms=K7, ksnG; ORFNames=DDB_G0281555;
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, INDUCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=AX2, and AX3;
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 [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 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. May be involved in cell motility or cell
CC differentiation during prestalk formation.
CC {ECO:0000269|PubMed:9693369}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:9693369};
CC Single-pass membrane protein {ECO:0000269|PubMed:9693369}. Cytoplasm,
CC cytoskeleton {ECO:0000305|PubMed:9693369}.
CC -!- INDUCTION: During the developmental stage with highest levels
CC detectable between 12 and 16 h of development.
CC {ECO:0000269|PubMed:9693369}.
CC -!- DISRUPTION PHENOTYPE: Kif7-null cells have a problem in the
CC localization or differentiation of prestalk cells in a kif7-null/wild
CC type mixed aggregate. {ECO:0000269|PubMed:9693369}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB07748.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U41289; AAB07748.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000042; EAL66539.1; -; Genomic_DNA.
DR RefSeq; XP_640581.1; XM_635489.1.
DR AlphaFoldDB; Q54TL0; -.
DR SMR; Q54TL0; -.
DR STRING; 44689.DDB0206583; -.
DR PaxDb; Q54TL0; -.
DR EnsemblProtists; EAL66539; EAL66539; DDB_G0281555.
DR GeneID; 8623189; -.
DR KEGG; ddi:DDB_G0281555; -.
DR dictyBase; DDB_G0281555; kif7.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_265425_0_0_1; -.
DR InParanoid; Q54TL0; -.
DR OMA; REHKQNG; -.
DR PRO; PR:Q54TL0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; 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:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW Motor protein; Nucleotide-binding; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1255
FT /note="Kinesin-related protein 7"
FT /id="PRO_0000365582"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 28..349
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1088..1223
FT /evidence="ECO:0000255"
FT COMPBIAS 548..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..831
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 171
FT /note="D -> I (in Ref. 1; AAB07748)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..262
FT /note="ERA -> DIS (in Ref. 1; AAB07748)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="A -> V (in Ref. 1; AAB07748)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="Missing (in Ref. 1; AAB07748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1255 AA; 141959 MW; 97D5D6B98EE1E8D4 CRC64;
MESPVVEGNS GEVATPTLPQ PPTPVSSNIR VVCRVRPLTE LEKGRNEHSI VHFFDSKSIS
IRANGPQFTF DRIFGYQETQ SQIFEDVAEP IVNDFLDGYH GTIIAYGQTA SGKTFTMVGD
PDSHGIIPRV IESIFVGISK MREKDTSLSL AFCLKISALE LYNEKLYDLY DASKSNLNIR
EHKQNGIYVE GISEIVITSI EEAYNFLNIS NNNRAIASTK MSAASSRSHS VLMIELSQQN
LSMESSKISK LFLVDLAGSE RAHKTGAEGD RMQEAKNINL SLSALGKVIN ALTCGANYVP
YRDSKLTRVL QDSLGGNSKT SLIINCSPSN NNEHETITTL QFGTRAKTIK NQPKINKKIT
YHELELFIIK LAKDLEKSRK ECEEITRSKN LEINNLLIQL ENNQKMVVES NQKLELLNSQ
ISSNHSFDNT FKEIENTCEN SKIIFDDLND HINNNNNVDE NNNTNNNDNN NNDNNNNNQY
QEESNQYQQE NNQKDGDQNN SSFDSIKVED LRDLDDEPDI EDIILNSTLG NISDDDDDDD
DHHSNNNNVD DNNNGEINND SDGYLNRSLK DIKIPEISDL NDHNINNNNN NNNNINNDNN
SNSGGLRVST SYITSSPNLS PSKSMDVNNS PPLFSYFKTK DFPPSSDEND KFFNDLIAKG
ENEQQQQQQQ HNDDDEDIKS TTSNATTTTI TTIDMNASHP SGIDDPIEFT IIKSDKTITS
TIERETIQPS SLSNSTSLLD IETVESSTLP APPPVTTTTT LTTVTTTKLT KTTNIPSNTN
DINSIDDFGF SKIEEEGSSS NRKPNDTAIL SFGDDDDEEN EDNENEDVIV DSDEDTHSGK
NNLLNTFKND HHRGDFGATP TKSIFNKNGN ITIKEFETPQ QQQQQQQQQQ QQQQQQQQQQ
QPLILQTTST NPTIISIKSN KEPSPSSSTT TSIKKKNFNK RRSWIIFTII LTITLVSSSL
LCLYLPEYKE RLVQRRGYLN KLGIYSDYPT NEKISLAQHN QISLAKELYG GNSKQYYDEM
SSFNTAYNHL IEMNHLETAV SKIFGSAIDL RFSGDDVINS IECKRAIHKL KTNNYVNGDL
DQQQQQHNYI TKIDQLSEQS KEQNQLIENF KLDLKNKTSE IEKLEKEIKQ KDNKIKEKEE
KIELIESRVL NEEKGGEKVL EDQIISLRND KNTLSTQILN LEGDKKSLGV LVIKLNSDKT
EIQNEVKELK RKVQELEDAP IALIPNPFVK WVKSFYVEKK SWFVENIYKI WNWFK
