UniProt: E3LQP4

Database: UniProt
Entry: E3LQP4_CAERE

LinkDB:  E3LQP4_CAERE 
Original site:  E3LQP4_CAERE

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Ontology (36)   
   GO (36)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (24)   
   InterPro (12)   
   Pfam (6)   
   PROSITE (3)   
   SMART (3)   
All databases (64)   

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ID   E3LQP4_CAERE            Unreviewed;      1633 AA.
AC   E3LQP4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Kinesin-like protein unc-104 {ECO:0000256|ARBA:ARBA00020751};
GN   Name=Cre-unc-104 {ECO:0000313|EMBL:EFP07741.1};
GN   ORFNames=CRE_26470 {ECO:0000313|EMBL:EFP07741.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; DS268413; EFP07741.1; -; Genomic_DNA.
DR   RefSeq; XP_003113829.1; XM_003113781.1.
DR   STRING; 31234.E3LQP4; -.
DR   EnsemblMetazoa; CRE26470.1; CRE26470.1; WBGene00054230.
DR   GeneID; 9815300; -.
DR   KEGG; crq:GCK72_006395; -.
DR   CTD; 9815300; -.
DR   eggNOG; KOG0245; Eukaryota.
DR   HOGENOM; CLU_001485_10_0_1; -.
DR   InParanoid; E3LQP4; -.
DR   OMA; IKITICH; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0030425; C:dendrite; IEA:EnsemblMetazoa.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IEA:EnsemblMetazoa.
DR   GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0098793; C:presynapse; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:EnsemblMetazoa.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:EnsemblMetazoa.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblMetazoa.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IEA:EnsemblMetazoa.
DR   GO; GO:0048156; F:tau protein binding; IEA:EnsemblMetazoa.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; IEA:EnsemblMetazoa.
DR   GO; GO:0030421; P:defecation; IEA:EnsemblMetazoa.
DR   GO; GO:0007631; P:feeding behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:EnsemblMetazoa.
DR   GO; GO:1904810; P:negative regulation of dense core granule transport; IEA:EnsemblMetazoa.
DR   GO; GO:0002119; P:nematode larval development; IEA:EnsemblMetazoa.
DR   GO; GO:0016322; P:neuron remodeling; IEA:EnsemblMetazoa.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; IEA:EnsemblMetazoa.
DR   GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IEA:EnsemblMetazoa.
DR   GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; IEA:EnsemblMetazoa.
DR   GO; GO:0040010; P:positive regulation of growth rate; IEA:EnsemblMetazoa.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; IEA:EnsemblMetazoa.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:EnsemblMetazoa.
DR   GO; GO:1903746; P:positive regulation of nematode pharyngeal pumping; IEA:EnsemblMetazoa.
DR   GO; GO:1905608; P:positive regulation of presynapse assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0043113; P:receptor clustering; IEA:EnsemblMetazoa.
DR   GO; GO:0045055; P:regulated exocytosis; IEA:EnsemblMetazoa.
DR   GO; GO:0030516; P:regulation of axon extension; IEA:EnsemblMetazoa.
DR   GO; GO:1902473; P:regulation of protein localization to synapse; IEA:EnsemblMetazoa.
DR   GO; GO:0006942; P:regulation of striated muscle contraction; IEA:EnsemblMetazoa.
DR   GO; GO:0000003; P:reproduction; IEA:EnsemblMetazoa.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IEA:EnsemblMetazoa.
DR   GO; GO:0007419; P:ventral cord development; IEA:EnsemblMetazoa.
DR   CDD; cd22705; FHA_KIF1; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
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; IPR049780; PH_KIFIA_KIFIB.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF5; -; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 2.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT   DOMAIN          3..347
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1509..1607
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1415..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1424..1465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1633 AA;  185015 MW;  A5726C1B8756EF17 CRC64;
     MSSVKVAVRV RPFNQREISN ASKCVLQVNG NTTTINGHAI NKENFSFNFD HSYWSFTKND
     PHFISQKQVY EELGVEMLAH AFEGYNVCIF AYGQTGSGKS YTMMGKANDK EEMGIIPRLC
     DDLFERIDNN NDKNVQYSVE VSYMEIYCER VKDLLNPSSG GNLRVREHPL LGPYVDDLTK
     MAVCSYNDIC NLMDEGNKAR TVAATNMNST SSRSHAVFTI VLTQKKHCSD TNLDTEKVSK
     ISLVDLAGSE RANSTGAEGQ RLKEGANINK SLTTLGLVIS KLAEEAGNKK KRAKGVVPYR
     DSVLTWLLRE NLGGNSKTAM LAALSPADIN FDETLSTLRY ADRAKQIVCQ AVVNEDPNAK
     LIRELKEEVN KLRHILDEKG IDVADVQDTP GRPNKGPKLS AQVHNTIEQL QASEKLIAEL
     DKTWEQKLVK TEEIRKQREE ELREMGLACL DDGTTLGVFS PKKLPHLVNL NEDPLMSECL
     IYYLKEGVTS VGRPEAEHRP DILLSGEAIL DLHCEFINED GNVTLAMQPD ASVYINGKQV
     KTPTVMHTGS RVILGEHHVF RYNDPQEARQ SRHNLAAITA EQPIDWKYAQ QELLEKQGID
     LKADMEKKLL EMESQYRKEK VELEKKMYLQ TKEYETLIES LQRQVDLAQS VISSGGSIWE
     GERMLTSSLM EFPEELKWTS DQKRVVRKAA IKWRYHQFTS VRDDLWGNAI FVKEANAISV
     ELKKKVQFQF ALLTDTMYSP LPPDLLPPGE DLTLRPYPKT VVAIQVQDLK NGATHYWSIE
     KLKQRLEDMR IFYNSELSVA GTPVECPYPP VASEGWLAAL HFNPTRLIPD RQRLEAMRDM
     YETDVQMSPT DGDPMMDALM GTDPFYDRFP WFRMVGRAFV YLNNLLHNVP LIHKVAVVNE
     KGEVKGYLKV AIEPVQKDEV QNQKKGVRQT AKLHFRKEDF LKTHKNGETD ESSDLTFPDH
     MPEKIEFCFR VVVLQAIDVA DAYSDVFCQF NFLHRHDEAF STEPMKNSKS PLTFEHTQNL
     HIKMSKTFLH YLHHFPIIFE VFGHFQPKKE QFNFERQNSA LGRRLSTKLT FQQPSLVIST
     PVKSKKANAP IHNNTASVKS KHDLLVWFEI CELANNGEYV PTIVDHAQGL PTHGIFLLHQ
     GIQRRIKITI CHEKGELKWK DCQELVVGRI RAGPEWAGGD DVDVLSLGLF PGTFMEFSMD
     DRTFFQFEAA WDSSLHNSPL LNRVSNYGDQ IYMTLSAYME LDGCAQPAVI TKDLCLLIYA
     RDSKISAASR FCRSLIGGIS KSPEMNRVPG VYQLCLKDGS DSGSPGAIRR QRRVLDTSSA
     YVRGEENLGQ WRPRGDSLIF EHQWELEKLT RLQQVERVRL FLRLRDRLKG KKNKGEARTP
     VSPCDPVCAI PESVKLDEKE KGIVGKVLGL IKRRIPMNKD PPTGNKAQEL SDESGSNSIT
     SPTSDKSLIK SSQSSDLLCR QKSKSDQNLA SNDDILDSIG GMKRSLSGSR ILQLNILVPE
     VLEERVGVVV SKKGYMNFLE EKTQGWTRRW VVVRRPYILL FRDDRDLVIR GIINLANARI
     EHSEDLQAMV KVPNTFSVCT NQRGFLMQMM PGDEMYDWLY AINPLMAGQM KLHGNQNGTT
     LKSPSPSSTT IAP
//

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