UN104_CAEEL
ID UN104_CAEEL Reviewed; 1584 AA.
AC P23678; Q8MQ97; Q8MQ98;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Kinesin-like protein unc-104;
DE AltName: Full=Uncoordinated protein 104;
GN Name=unc-104; ORFNames=C52E12.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1846075; DOI=10.1016/0896-6273(91)90126-k;
RA Otsuka A.J., Jeyaprakash A., Garcia-Anoveros J., Tang L.Z., Fisk G.,
RA Hartshorne T., Franco R., Born T.;
RT "The C. elegans unc-104 gene encodes a putative kinesin heavy chain-like
RT protein.";
RL Neuron 6:113-122(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF ASP-1497.
RX PubMed=12657671; DOI=10.1523/jneurosci.23-06-02122.2003;
RA Jacob T.C., Kaplan J.M.;
RT "The EGL-21 carboxypeptidase E facilitates acetylcholine release at
RT Caenorhabditis elegans neuromuscular junctions.";
RL J. Neurosci. 23:2122-2130(2003).
RN [4]
RP FUNCTION.
RX PubMed=20510931; DOI=10.1016/j.cell.2010.04.011;
RA Ou C.Y., Poon V.Y., Maeder C.I., Watanabe S., Lehrman E.K., Fu A.K.,
RA Park M., Fu W.Y., Jorgensen E.M., Ip N.Y., Shen K.;
RT "Two cyclin-dependent kinase pathways are essential for polarized
RT trafficking of presynaptic components.";
RL Cell 141:846-858(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-1497.
RX PubMed=22101643; DOI=10.1038/nn.2970;
RA Maniar T.A., Kaplan M., Wang G.J., Shen K., Wei L., Shaw J.E.,
RA Koushika S.P., Bargmann C.I.;
RT "UNC-33 (CRMP) and ankyrin organize microtubules and localize kinesin to
RT polarize axon-dendrite sorting.";
RL Nat. Neurosci. 15:48-56(2011).
RN [6]
RP FUNCTION.
RX PubMed=21609829; DOI=10.1016/j.neuron.2011.04.002;
RA Park M., Watanabe S., Poon V.Y., Ou C.Y., Jorgensen E.M., Shen K.;
RT "CYY-1/cyclin Y and CDK-5 differentially regulate synapse elimination and
RT formation for rewiring neural circuits.";
RL Neuron 70:742-757(2011).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-1497.
RX PubMed=22157748; DOI=10.1038/emboj.2011.447;
RA Troulinaki K., Tavernarakis N.;
RT "Endocytosis and intracellular trafficking contribute to necrotic
RT neurodegeneration in C. elegans.";
RL EMBO J. 31:654-666(2012).
CC -!- FUNCTION: Motor protein involved in microtubule-associated anterograde
CC transport (PubMed:1846075). Regulates the transport of synaptic vesicle
CC precursors in the axon of DA motor neurons (PubMed:20510931). Regulates
CC the polarized sorting of axonal proteins (PubMed:22101643). Essential
CC for the transport of synaptic components during the synaptic remodeling
CC of the DD motor neuron, probably downstream of cdk-5 and/or pct-1/cyy-1
CC complex (PubMed:21609829). Required for the anterograde transport of
CC neuropeptide-containing dense core vesicles along axons
CC (PubMed:12657671). Involved in necrotic cell death (PubMed:22157748).
CC {ECO:0000269|PubMed:12657671, ECO:0000269|PubMed:1846075,
CC ECO:0000269|PubMed:20510931, ECO:0000269|PubMed:21609829,
CC ECO:0000269|PubMed:22101643, ECO:0000269|PubMed:22157748}.
CC -!- INTERACTION:
CC P23678-1; Q21049: syd-2; NbExp=9; IntAct=EBI-15812209, EBI-327903;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, axon {ECO:0000269|PubMed:22101643}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P23678-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P23678-2; Sequence=VSP_011760, VSP_011761;
CC -!- TISSUE SPECIFICITY: Expressed in nerve ring, amphid commissure and
CC ventral nerve cord (at protein level). {ECO:0000269|PubMed:22101643}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit uncoordinated and slow movement.
CC {ECO:0000269|PubMed:1846075}.
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; M58582; AAA03517.1; -; mRNA.
DR EMBL; BX284602; CCD64622.2; -; Genomic_DNA.
DR EMBL; BX284602; CCD64623.2; -; Genomic_DNA.
DR PIR; JN0114; JN0114.
DR RefSeq; NP_001022041.2; NM_001026870.5. [P23678-2]
DR RefSeq; NP_741019.3; NM_171017.8. [P23678-1]
DR AlphaFoldDB; P23678; -.
DR SMR; P23678; -.
DR BioGRID; 39482; 15.
DR DIP; DIP-49010N; -.
DR IntAct; P23678; 1.
DR STRING; 6239.C52E12.2b; -.
DR iPTMnet; P23678; -.
DR EPD; P23678; -.
DR PaxDb; P23678; -.
DR PeptideAtlas; P23678; -.
DR PRIDE; P23678; -.
DR EnsemblMetazoa; C52E12.2a.1; C52E12.2a.1; WBGene00006831. [P23678-1]
DR EnsemblMetazoa; C52E12.2a.2; C52E12.2a.2; WBGene00006831. [P23678-1]
DR EnsemblMetazoa; C52E12.2b.1; C52E12.2b.1; WBGene00006831. [P23678-2]
DR GeneID; 174144; -.
DR KEGG; cel:CELE_C52E12.2; -.
DR UCSC; C52E12.2a; c. elegans. [P23678-1]
DR CTD; 36876; -.
DR WormBase; C52E12.2a; CE48050; WBGene00006831; unc-104. [P23678-1]
DR WormBase; C52E12.2b; CE47855; WBGene00006831; unc-104. [P23678-2]
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000168546; -.
DR HOGENOM; CLU_001485_10_0_1; -.
DR InParanoid; P23678; -.
DR OMA; KITICHE; -.
DR OrthoDB; 76316at2759; -.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:P23678; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006831; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IDA:WormBase.
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; IDA:WormBase.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:WormBase.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:WormBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:WormBase.
DR GO; GO:0048156; F:tau protein binding; IPI:WormBase.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IDA:WormBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0007631; P:feeding behavior; IMP:WormBase.
DR GO; GO:0007018; P:microtubule-based movement; IDA:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:1904810; P:negative regulation of dense core granule transport; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:UniProtKB.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:WormBase.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IMP:UniProtKB.
DR GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; IMP:UniProtKB.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR GO; GO:1903746; P:positive regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:1905608; P:positive regulation of presynapse assembly; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:WormBase.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0043113; P:receptor clustering; IMP:WormBase.
DR GO; GO:0045055; P:regulated exocytosis; IMP:WormBase.
DR GO; GO:0030516; P:regulation of axon extension; IMP:WormBase.
DR GO; GO:1902473; P:regulation of protein localization to synapse; IMP:UniProtKB.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IMP:WormBase.
DR GO; GO:0050807; P:regulation of synapse organization; IGI:UniProtKB.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0007419; P:ventral cord development; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:WormBase.
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; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
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; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 4.
DR Pfam; PF12473; DUF3694; 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; SSF49879; SSF49879; 1.
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 Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Necrosis; Neurogenesis; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..1584
FT /note="Kinesin-like protein unc-104"
FT /id="PRO_0000125413"
FT DOMAIN 3..347
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 1460..1558
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 183..335
FT /note="Microtubule-binding"
FT REGION 1366..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 425..445
FT /evidence="ECO:0000255"
FT COILED 598..652
FT /evidence="ECO:0000255"
FT COILED 777..797
FT /evidence="ECO:0000255"
FT COMPBIAS 1375..1416
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:0000255|PROSITE-ProRule:PRU00283"
FT VAR_SEQ 786
FT /note="E -> EDMRIFYNSELSVAGTPVDVPYPPVAEGWLAALNRNSARLIPDRQRL
FT E (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011760"
FT VAR_SEQ 1255..1257
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011761"
FT VARIANT 598
FT /note="I -> T"
FT VARIANT 930
FT /note="V -> M"
FT MUTAGEN 1497
FT /note="D->N: In e1265; mislocalized presynaptic proteins to
FT dendrites in PVD neurons. increased survival in response to
FT hypoxia induced by sodium azide. Abnormal accumulation of
FT egl-21, egl-3, FMRFamide-like peptides (FaRPs) and snb-1 in
FT neuronal cell bodies. Reduced number of neuron cell corpses
FT in a hyperactive mec-4 or deg-3 mutant background."
FT /evidence="ECO:0000269|PubMed:12657671,
FT ECO:0000269|PubMed:22101643, ECO:0000269|PubMed:22157748"
FT CONFLICT 905
FT /note="A -> R (in Ref. 1; AAA03517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1584 AA; 179652 MW; D558DD367545544B CRC64;
MSSVKVAVRV RPFNQREISN TSKCVLQVNG NTTTINGHSI NKENFSFNFD HSYWSFARND
PHFITQKQVY EELGVEMLEH AFEGYNVCIF AYGQTGSGKS YTMMGKANDP DEMGIIPRLC
NDLFARIDNN NDKDVQYSVE VSYMEIYCER VKDLLNPNSG GNLRVREHPL LGPYVDDLTK
MAVCSYHDIC NLMDEGNKAR TVAATNMNST SSRSHAVFTI VLTQKRHCAD SNLDTEKHSK
ISLVDLAGSE RANSTGAEGQ RLKEGANINK SLTTLGLVIS KLAEESTKKK KSNKGVIPYR
DSVLTWLLRE NLGGNSKTAM LAALSPADIN FDETLSTLRY ADRAKQIVCQ AVVNEDPNAK
LIRELNEEVI KLRHILKDKG IDVTDVQETP GKHKKGPKLP AHVHEQLEKL QESEKLMAEI
GKTWEQKLIH TEEIRKQREE ELRDMGLACA EDGTTLGVFS PKKLPHLVNL NEDPLMSECL
IYYLKEGVTS VGRPEAEHRP DILLSGEAIL ELHCEFINED GNVTLTMKPN ASCYINGKQV
TTPTVLHTGS RVILGEHHVF RYNDPQEARQ SRHNLAAIAE QPIDWKYAQQ ELLDKQGIDL
KADMEKKMLE MESQYRREKV ELEQKMYHQT REYESMIENL QKQVDLAQSY ISGGGSIWEG
ERMLTSSLLE FPEELKWTSD QKRVVLKAAI KWRYHQFTSV RDDLWGNAIF VKEANAISVE
LKKKVQFQFA LLTDTMYSPL PPDLLPPGED LTLRPYPKTV VAIQVQDLKN GATHYWSIEK
LKQRLEAMRD MYETDAEMSP ADGDPMMDAL MGTDPFYDRF PWFRMVGRAF VYLNNLLHNV
PLIHKVAVVN EKGEVKGYLK VAIEPVQKDE VINQKKGVRQ TAKLHFRKED FLKSHKNGET
SDSDALAFPE HMQEEVEFCF RVVVLQAIDV ADTYSDVFCQ FNFLHRHDEA FSTEPMKNSK
SPLTFEHTQN LHIKMSKTFL HYLHHFPIIF EVFGHFQPKS EQFNFERQNS ALGRRLSTKL
TFQQPSLVIS TPVKSKKANA PIQNNNASVK SKHDLLVWFE ICELANNGEY VPTIVDHAQG
LPTHGIFLLH QGIQRRIKIT ICHEKGELKW KDCQELVVGR IRAGPEWAGG DDVDVLSLGL
FPGTFMEFSM DDRTFFQFEA AWDSSLHNSP LLNRVSNYGD QIYMTLSAYM ELDGCAQPAV
VTKDLCLLIY ARDSKISAAS RFCRSLVGGI SKSPEMNRVP GVYQLCLKDG SDSGSPGAIR
RQRRVLDTSS AYVRGEENLG QWRPRGDSLI FEHQWELEKL TRLQQVERVR LFLRLRDRLK
GKKNKGEART PVSPCDPVCA IPESIKLDEK DKGIVGKVLG LIRRKIPMNK DPPTGNKAQE
LSDESGSNSI TSPVSDKSLI KSSRSSDLLC RQKSKSDQNL ASNDDIVDNL GGMKRSLSGS
RILQLNILVP EVLEERVGVV VSKKGYMNFL EEKTQGWTRR WVIVRRPYIL LFRDDRDLVI
RGIINLANAR IEHSEDQQAM VKVPNTFSVC TNQRGFLMQM MPGDEMYDWL YAINPLMAGQ
MKLHGNQNGT TLKSPTSSSS IAAS
