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Kinesin-like protein unc-104 (Uncoordinated protein 104)

 UN104_CAEEL             Reviewed;        1584 AA.
P23678; Q8MQ97; Q8MQ98;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
24-JUL-2013, sequence version 4.
22-NOV-2017, entry version 152.
RecName: Full=Kinesin-like protein unc-104;
AltName: Full=Uncoordinated protein 104;
Name=unc-104; ORFNames=C52E12.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION
PHENOTYPE.
PubMed=1846075; DOI=10.1016/0896-6273(91)90126-K;
Otsuka A.J., Jeyaprakash A., Garcia-Anoveros J., Tang L.Z., Fisk G.,
Hartshorne T., Franco R., Born T.;
"The C. elegans unc-104 gene encodes a putative kinesin heavy chain-
like protein.";
Neuron 6:113-122(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, AND MUTAGENESIS OF ASP-1497.
PubMed=12657671;
Jacob T.C., Kaplan J.M.;
"The EGL-21 carboxypeptidase E facilitates acetylcholine release at
Caenorhabditis elegans neuromuscular junctions.";
J. Neurosci. 23:2122-2130(2003).
[4]
FUNCTION.
PubMed=20510931; DOI=10.1016/j.cell.2010.04.011;
Ou C.Y., Poon V.Y., Maeder C.I., Watanabe S., Lehrman E.K., Fu A.K.,
Park M., Fu W.Y., Jorgensen E.M., Ip N.Y., Shen K.;
"Two cyclin-dependent kinase pathways are essential for polarized
trafficking of presynaptic components.";
Cell 141:846-858(2010).
[5]
FUNCTION.
PubMed=21609829; DOI=10.1016/j.neuron.2011.04.002;
Park M., Watanabe S., Poon V.Y., Ou C.Y., Jorgensen E.M., Shen K.;
"CYY-1/cyclin Y and CDK-5 differentially regulate synapse elimination
and formation for rewiring neural circuits.";
Neuron 70:742-757(2011).
[6]
FUNCTION, AND MUTAGENESIS OF ASP-1497.
PubMed=22157748; DOI=10.1038/emboj.2011.447;
Troulinaki K., Tavernarakis N.;
"Endocytosis and intracellular trafficking contribute to necrotic
neurodegeneration in C. elegans.";
EMBO J. 31:654-666(2012).
-!- FUNCTION: Motor protein involved in microtubule-associated
anterograde transport (PubMed:1846075). Regulates the transport of
synaptic vesicle precursors in the axon of DA motor neurons
(PubMed:20510931). Essential for the transport of synaptic
components during the synaptic remodeling of the DD motor neuron,
probably downstream of cdk-5 and/or pct-1/cyy-1 complex
(PubMed:21609829). Required for the anterograde transport of
neuropeptide-containing dense core vesicles along axons
(PubMed:12657671). Involved in necrotic cell death
(PubMed:22157748). {ECO:0000269|PubMed:12657671,
ECO:0000269|PubMed:1846075, ECO:0000269|PubMed:20510931,
ECO:0000269|PubMed:21609829, ECO:0000269|PubMed:22157748}.
-!- INTERACTION:
Q21049:syd-2; NbExp=9; IntAct=EBI-15812209, EBI-327903;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=P23678-1; Sequence=Displayed;
Name=b;
IsoId=P23678-2; Sequence=VSP_011760, VSP_011761;
Note=No experimental confirmation available.;
-!- DISRUPTION PHENOTYPE: Worms exhibit uncoordinated and slow
movement. {ECO:0000269|PubMed:1846075}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. Unc-104 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00283}.
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EMBL; M58582; AAA03517.1; -; mRNA.
EMBL; FO080554; CCD64622.2; -; Genomic_DNA.
EMBL; FO080554; CCD64623.2; -; Genomic_DNA.
PIR; JN0114; JN0114.
RefSeq; NP_001022041.2; NM_001026870.5. [P23678-2]
RefSeq; NP_741019.3; NM_171017.8. [P23678-1]
ProteinModelPortal; P23678; -.
SMR; P23678; -.
BioGrid; 39482; 2.
DIP; DIP-49010N; -.
IntAct; P23678; 1.
STRING; 6239.C52E12.2b; -.
iPTMnet; P23678; -.
EPD; P23678; -.
PaxDb; P23678; -.
PeptideAtlas; P23678; -.
PRIDE; P23678; -.
EnsemblMetazoa; C52E12.2a; C52E12.2a; WBGene00006831. [P23678-1]
GeneID; 174144; -.
KEGG; cel:CELE_C52E12.2; -.
UCSC; C52E12.2a; c. elegans. [P23678-1]
CTD; 36876; -.
WormBase; C52E12.2a; CE48050; WBGene00006831; unc-104. [P23678-1]
WormBase; C52E12.2b; CE47855; WBGene00006831; unc-104. [P23678-2]
eggNOG; KOG0245; Eukaryota.
eggNOG; COG5059; LUCA.
GeneTree; ENSGT00890000139327; -.
HOGENOM; HOG000165968; -.
InParanoid; P23678; -.
KO; K10392; -.
OMA; WGNAVYL; -.
OrthoDB; EOG091G009V; -.
PRO; PR:P23678; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00006831; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0030425; C:dendrite; IDA:WormBase.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IEA:GOC.
GO; GO:0098793; C:presynapse; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008574; F:ATP-dependent microtubule motor activity, plus-end-directed; IDA:WormBase.
GO; GO:0008017; F:microtubule binding; IDA:WormBase.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:WormBase.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:WormBase.
GO; GO:0048156; F:tau protein binding; IPI:WormBase.
GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
GO; GO:0048490; P:anterograde synaptic vesicle transport; IDA:WormBase.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030421; P:defecation; IMP:WormBase.
GO; GO:0007631; P:feeding behavior; IMP:WormBase.
GO; GO:0007018; P:microtubule-based movement; IDA:WormBase.
GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
GO; GO:1904810; P:negative regulation of dense core granule transport; IMP:UniProtKB.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0016322; P:neuron remodeling; IMP:UniProtKB.
GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:WormBase.
GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; IMP:UniProtKB.
GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
GO; GO:1903746; P:positive regulation of pharyngeal pumping; IMP:WormBase.
GO; GO:1905608; P:positive regulation of presynapse assembly; IMP:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IMP:WormBase.
GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
GO; GO:0043113; P:receptor clustering; IMP:WormBase.
GO; GO:0045055; P:regulated exocytosis; IMP:WormBase.
GO; GO:0030516; P:regulation of axon extension; IMP:WormBase.
GO; GO:1902473; P:regulation of protein localization to synapse; IMP:UniProtKB.
GO; GO:0006942; P:regulation of striated muscle contraction; IMP:WormBase.
GO; GO:0050807; P:regulation of synapse organization; IGI:UniProtKB.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
GO; GO:0016192; P:vesicle-mediated transport; IMP:WormBase.
CDD; cd00060; FHA; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR000253; FHA_dom.
InterPro; IPR022164; Kinesin-like.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR022140; Kinesin-like_KIF1-typ.
InterPro; IPR032405; Kinesin_assoc.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR008984; SMAD_FHA_dom_sf.
PANTHER; PTHR24115; PTHR24115; 1.
Pfam; PF12473; DUF3694; 1.
Pfam; PF12423; KIF1B; 1.
Pfam; PF00225; Kinesin; 1.
Pfam; PF16183; Kinesin_assoc; 2.
Pfam; PF00169; PH; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00240; FHA; 1.
SMART; SM00129; KISc; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF50729; SSF50729; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule;
Motor protein; Necrosis; Neurogenesis; Nucleotide-binding;
Reference proteome; Transport.
CHAIN 1 1584 Kinesin-like protein unc-104.
/FTId=PRO_0000125413.
DOMAIN 3 347 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
DOMAIN 1460 1558 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
NP_BIND 93 100 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
REGION 183 335 Microtubule-binding.
COILED 425 445 {ECO:0000255}.
COILED 598 652 {ECO:0000255}.
COILED 777 797 {ECO:0000255}.
COMPBIAS 957 1052 Arg/Lys-rich (basic).
COMPBIAS 1203 1584 Arg/Lys-rich (basic).
VAR_SEQ 786 786 E -> EDMRIFYNSELSVAGTPVDVPYPPVAEGWLAALNRN
SARLIPDRQRLE (in isoform b).
{ECO:0000305}.
/FTId=VSP_011760.
VAR_SEQ 1255 1257 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_011761.
VARIANT 598 598 I -> T.
VARIANT 930 930 V -> M.
MUTAGEN 1497 1497 D->N: In e1265; increased survival in
response to hypoxia induced by sodium
azide. Abnormal accumulation of egl-21,
egl-3, FMRFamide-like peptides (FaRPs)
and snb-1 in neuronal cell bodies.
Reduced number of neuron cell corpses in
a hyperactive mec-4 or deg-3 mutant
background. {ECO:0000269|PubMed:12657671,
ECO:0000269|PubMed:22157748}.
CONFLICT 905 905 A -> R (in Ref. 1; AAA03517).
{ECO:0000305}.
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


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