UNC17_CAEEL
ID UNC17_CAEEL Reviewed; 532 AA.
AC P34711;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Vesicular acetylcholine transporter unc-17;
DE AltName: Full=Uncoordinated protein 17;
GN Name=unc-17 {ECO:0000312|WormBase:ZC416.8a};
GN ORFNames=ZC416.8 {ECO:0000312|WormBase:ZC416.8a};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-230 AND GLY-347.
RC STRAIN=Bristol N2;
RX PubMed=8342028; DOI=10.1126/science.8342028;
RA Alfonso A., Grundahl K., Duerr J.S., Han H.-P., Rand J.B.;
RT "The Caenorhabditis elegans unc-17 gene: a putative vesicular acetylcholine
RT transporter.";
RL Science 261:617-619(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=8057385; DOI=10.1006/jmbi.1994.1538;
RA Alfonso A., Grundahl K., McManus J.R., Asbury J.M., Rand J.B.;
RT "Alternative splicing leads to two cholinergic proteins in Caenorhabditis
RT elegans.";
RL J. Mol. Biol. 241:627-630(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=28244369; DOI=10.7554/elife.24846;
RA Schwarz J., Bringmann H.;
RT "Analysis of the NK2 homeobox gene ceh-24 reveals sublateral motor neuron
RT control of left-right turning during sleep.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Involved in acetylcholine transport into synaptic vesicles.
CC {ECO:0000269|PubMed:8342028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:8342028}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:8342028}.
CC -!- TISSUE SPECIFICITY: Detected in most regions of the nervous system
CC including the nerve ring, the ventral and dorsal nerve cords, and the
CC pharyngeal nervous system (PubMed:8342028). Expressed in most
CC cholinergic neurons (PubMed:8342028, PubMed:28244369). In addition,
CC expressed in SIA, SIB and SMB sublateral motor neurons
CC (PubMed:28244369). {ECO:0000269|PubMed:28244369,
CC ECO:0000269|PubMed:8342028}.
CC -!- DISRUPTION PHENOTYPE: Newly hatched animals are small and coiled, do
CC not grow or feed, can barely move and die within a few days.
CC {ECO:0000269|PubMed:8342028}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
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DR EMBL; L19621; AAC14456.1; -; mRNA.
DR EMBL; U09277; AAC13764.1; -; Genomic_DNA.
DR EMBL; FO080977; CCD68241.1; -; Genomic_DNA.
DR PIR; S53603; S53603.
DR RefSeq; NP_001023602.1; NM_001028431.3.
DR AlphaFoldDB; P34711; -.
DR SMR; P34711; -.
DR BioGRID; 2550363; 1.
DR IntAct; P34711; 1.
DR MINT; P34711; -.
DR STRING; 6239.ZC416.8a; -.
DR TCDB; 2.A.1.2.13; the major facilitator superfamily (mfs).
DR PeptideAtlas; P34711; -.
DR EnsemblMetazoa; ZC416.8a.1; ZC416.8a.1; WBGene00006756.
DR GeneID; 24105312; -.
DR CTD; 24105312; -.
DR WormBase; ZC416.8a; CE17307; WBGene00006756; unc-17.
DR eggNOG; KOG3764; Eukaryota.
DR GeneTree; ENSGT00940000159449; -.
DR HOGENOM; CLU_001265_10_9_1; -.
DR OMA; PDYIAHM; -.
DR OrthoDB; 956763at2759; -.
DR PhylomeDB; P34711; -.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P34711; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006756; Expressed in larva and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central.
DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
DR GO; GO:0060076; C:excitatory synapse; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; NAS:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0031090; C:organelle membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015870; P:acetylcholine transport; ISS:WormBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Glycoprotein; Membrane; Neurotransmitter transport;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..532
FT /note="Vesicular acetylcholine transporter unc-17"
FT /id="PRO_0000127525"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..101
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..160
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..219
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..303
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..367
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..418
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 230
FT /note="C->F: In p1160; severely uncoordinated."
FT /evidence="ECO:0000269|PubMed:8342028"
FT MUTAGEN 347
FT /note="G->A: In e245; severely uncoordinated."
FT /evidence="ECO:0000269|PubMed:8342028"
SQ SEQUENCE 532 AA; 58643 MW; 5F37A44C305D32BB CRC64;
MGFNVPVINR DSEILKADAK KWLEQQDNQK KCVLVIVSIA LLLDNMLYMV IVPIIPKYLR
DIHNYQVTFE GYHNETSQLA NGTYLVREVG GRINFLDEEL ELGWLFASKA LLQIFVNPFS
GYIIDRVGYE IPMILGLCTM FFSTAIFALG KSYGVLLFAR SLQGFGSAFA DTSGLAMIAD
RFTEENERSA ALGIALAFIS FGCLVAPPFG SVLYSLAGKP VPFLILSFVC LADAIAVFMV
INPHRRGTDS HGEKVQGTPM WRLFMDPFIA CCSGALIMAN VSLAFLEPTI TTWMSEMMPD
TPGWLVGVIW LPPFFPHVLG VYVTVKMLRA FPHHTWAIAM VGLAMEGIAC FAIPYTTSVM
QLVIPLSFVC FGIALIDTSL LPMLGHLVDT RHVSVYGSVY AIADISYSLA YAFGPIIAGW
IVTNWGFTAL NIIIFATNVT YAPVLFLLRK VHSYDTLGAK GDTAEMTQLN SSAPAGGYNG
KPEATTAESY QGWEDQQSYQ NQAQIPNHAV SFQDSRPQAE FPAGYDPLNP QW
