SUP1_CAEEL
ID SUP1_CAEEL Reviewed; 103 AA.
AC Q9XWU2;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein SUP-1 {ECO:0000312|EMBL:CAA21550.1};
DE Flags: Precursor;
GN Name=sup-1 {ECO:0000312|EMBL:CAA21550.1, ECO:0000312|WormBase:Y41C4A.13};
GN ORFNames=Y41C4A.13;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAA21550.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA21550.1};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-84.
RX PubMed=23051648; DOI=10.1534/genetics.112.145771;
RA Mathews E.A., Mullen G.P., Hodgkin J., Duerr J.S., Rand J.B.;
RT "Genetic interactions between UNC-17/VAChT and a novel transmembrane
RT protein in Caenorhabditis elegans.";
RL Genetics 192:1315-1325(2012).
CC -!- FUNCTION: May be involved in trafficking or stabilization of the
CC vesicular acetylcholine transporter unc-17.
CC {ECO:0000303|PubMed:23051648}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23051648};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:23051648}.
CC Perikaryon {ECO:0000269|PubMed:23051648}. Cell projection
CC {ECO:0000269|PubMed:23051648}. Synapse {ECO:0000269|PubMed:23051648}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000269|PubMed:23051648}.
CC -!- TISSUE SPECIFICITY: Expressed in a subset of neurons and in body wall
CC muscles. In the nervous system, expressed specifically in cholinergic
CC motor neurons of the ventral nerve cord, a subset of cholinergic head
CC neurons, anterior sublateral neurons, and body sublateral neurons (at
CC protein level). {ECO:0000269|PubMed:23051648}.
CC -!- DEVELOPMENTAL STAGE: First detected in the embryo and persists
CC throughout development (at protein level).
CC {ECO:0000269|PubMed:23051648}.
CC -!- DISRUPTION PHENOTYPE: Mild decrease in swimming behavior but otherwise
CC no apparent phenotype. {ECO:0000269|PubMed:23051648}.
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DR EMBL; AL032627; CAA21550.1; -; Genomic_DNA.
DR PIR; T26806; T26806.
DR RefSeq; NP_499520.1; NM_067119.4.
DR AlphaFoldDB; Q9XWU2; -.
DR SMR; Q9XWU2; -.
DR BioGRID; 54439; 2.
DR STRING; 6239.Y41C4A.13; -.
DR EPD; Q9XWU2; -.
DR PaxDb; Q9XWU2; -.
DR PeptideAtlas; Q9XWU2; -.
DR EnsemblMetazoa; Y41C4A.13.1; Y41C4A.13.1; WBGene00012759.
DR GeneID; 189815; -.
DR KEGG; cel:CELE_Y41C4A.13; -.
DR UCSC; Y41C4A.13; c. elegans.
DR CTD; 189815; -.
DR WormBase; Y41C4A.13; CE20253; WBGene00012759; sup-1.
DR eggNOG; ENOG502STS7; Eukaryota.
DR GeneTree; ENSGT00970000196367; -.
DR HOGENOM; CLU_178014_0_0_1; -.
DR InParanoid; Q9XWU2; -.
DR OMA; FNLQTWV; -.
DR OrthoDB; 1523940at2759; -.
DR PhylomeDB; Q9XWU2; -.
DR PRO; PR:Q9XWU2; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012759; Expressed in larva and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR InterPro; IPR022559; SUP-1-like.
DR PANTHER; PTHR34149; PTHR34149; 1.
DR Pfam; PF10853; DUF2650; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Membrane;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..103
FT /note="Protein SUP-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424559"
FT TOPO_DOM 17..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 84
FT /note="G->E: In e995; suppresses the uncoordinated
FT phenotype of the unc-17 G347R mutation."
FT /evidence="ECO:0000269|PubMed:23051648"
SQ SEQUENCE 103 AA; 11310 MW; C479263E483BD377 CRC64;
MMSYIALAAC IGLAMAANVD HDVKSAVNEV TTTKDGDTYC PVPLVGTKCG TSSIFHYWKC
CGELNKECCF NLQTWVWVTL ALFGVIFIAS FVISLVRCIC CRK
