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KLP68_DROPS
ID   KLP68_DROPS             Reviewed;         797 AA.
AC   Q29DY1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Kinesin-like protein Klp68D;
GN   Name=Klp68D {ECO:0000250|UniProtKB:P46867}; ORFNames=GA20244;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1] {ECO:0000312|EMBL:EAL30282.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Plus-end directed microtubule motor that may be used for
CC       anterograde axonal transport and could conceivably move cargos in fly
CC       neurons different than those moved by kinesin heavy chain or other
CC       plus-end directed motors. {ECO:0000250|UniProtKB:P46867}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Kinesin II subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL30282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH379070; EAL30282.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001352782.1; XM_001352746.3.
DR   RefSeq; XP_015043852.1; XM_015188366.1.
DR   AlphaFoldDB; Q29DY1; -.
DR   SMR; Q29DY1; -.
DR   STRING; 7237.FBpp0286237; -.
DR   PRIDE; Q29DY1; -.
DR   EnsemblMetazoa; FBtr0287799; FBpp0286237; FBgn0080239.
DR   EnsemblMetazoa; FBtr0377361; FBpp0338404; FBgn0080239.
DR   GeneID; 4812180; -.
DR   KEGG; dpo:Dpse_GA20244; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   HOGENOM; CLU_001485_22_4_1; -.
DR   InParanoid; Q29DY1; -.
DR   OMA; CKHDHNQ; -.
DR   PhylomeDB; Q29DY1; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0080239; Expressed in insect adult head and 2 other tissues.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:EnsemblMetazoa.
DR   GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:EnsemblMetazoa.
DR   GO; GO:0007018; P:microtubule-based movement; ISS:UniProtKB.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:EnsemblMetazoa.
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; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..797
FT                   /note="Kinesin-like protein Klp68D"
FT                   /id="PRO_0000270579"
FT   DOMAIN          19..344
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          371..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          350..384
FT                   /evidence="ECO:0000255"
FT   COILED          432..580
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        420..434
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         106..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   797 AA;  89225 MW;  37D6B08E3F6FA23C CRC64;
     MSAKSRRPGT ASSQTPNECV QVVVRCRPMS NRERSEGSPE VVNVYPNRGV VELQNVVDAN
     KEQRKVFTYD AAYDASASQT TLYHEVVFPL VSSVLEGFNG CIFAYGQTGT GKTFTMEGVR
     GNDDLMGIIP RTFEQIWLHI NRTENFQFLV DVSYLEIYME ELRDLLKPNS KHLEVRERGS
     GVYVPNLHAI NCKSVDDMIR VMKVGNKNRT VGFTNMNEHS SRSHAIFMIK IEMCDTETNT
     IKVGKLNLID LAGSERQSKT GASAERLKEA SKINLALSSL GNVISALAES SPHVPYRDSK
     LTRLLQDSLG GNSKTIMIAN IGPSNYNYNE TLTTLRYASR AKSIQNQPIK NEDPQDAKLK
     EYQEEIERLK RLIAPQQQQR SEKQGTIKKQ RVKKPKKEPI SQELIGSALQ ASSADLQVDE
     DRDSDGDGAE SESDKENEAE VAKSNEELER ERVENAKLAA KLAELEGQLV RGGKNLLDTY
     SERQIELEKK LVEIAERKKR EIEIQQQLEL QEETTLEIRE RNVSLEQEVE LKKRKLSKCY
     AKYLALQQEL NDCKHDHNQD LRELEMAQNE LVKELKRQLL IIDNFVPIEV KQRLYTQAKY
     DEEQEEWKFS SFPLPLPPSG GDGRQGYRRP VSHPQRRRPT SEHALQEAKS NAPSSLRFKS
     ENIVSYELEM PCRTTQEYRT PKVSASLQAV LAQAMQTGGD DIDIVDSHTN SLRSRLENII
     NANSSSNGGP GSGAGPLAAN TAGSGVGSMP NVRNIKSSRG LPSAGTALDS NRRPPTGRIP
     AKKPASAYPK ARGLVNK
 
 
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