TMED2_CAEEL
ID TMED2_CAEEL Reviewed; 203 AA.
AC O17528;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Suppressor/enhancer of lin-12 protein 9;
DE Flags: Precursor;
GN Name=sel-9; ORFNames=W02D7.7;
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 [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF VAL-47;
RP GLY-51 AND SER-97.
RX PubMed=10366590; DOI=10.1083/jcb.145.6.1165;
RA Wen C., Greenwald I.;
RT "p24 proteins and quality control of LIN-12 and GLP-1 trafficking in
RT Caenorhabditis elegans.";
RL J. Cell Biol. 145:1165-1175(1999).
RN [2]
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 [3]
RP FUNCTION, AND MUTAGENESIS OF SER-140.
RX PubMed=27528192; DOI=10.7554/elife.17721;
RA Lehrbach N.J., Ruvkun G.;
RT "Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic
RT protease DDI-1.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: May have a role in the negative regulation of lin-12 and glp-
CC 1 transport to the cell surface (PubMed:10366590). May also have a role
CC in a quality control mechanism for endoplasmic reticulum-Golgi
CC transport; the budding of coatomer-coated and other species of coated
CC vesicles, could bind cargo molecules to collect them into budding
CC vesicles (PubMed:10366590). Involved in regulating the expression of
CC proteasomal subunits such as rpt-3 in order to confer resistance to
CC proteasomal dysfunction (PubMed:27528192).
CC {ECO:0000269|PubMed:10366590, ECO:0000269|PubMed:27528192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I
CC membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Single-pass type I membrane protein. Golgi apparatus membrane; Single-
CC pass type I membrane protein. Note=Golgi-derived coatomer-coated
CC vesicles.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; FO081199; CCD69837.1; -; Genomic_DNA.
DR PIR; T29844; T29844.
DR RefSeq; NP_505145.1; NM_072744.4.
DR AlphaFoldDB; O17528; -.
DR SMR; O17528; -.
DR BioGRID; 44254; 11.
DR STRING; 6239.W02D7.7; -.
DR EPD; O17528; -.
DR PaxDb; O17528; -.
DR PeptideAtlas; O17528; -.
DR EnsemblMetazoa; W02D7.7.1; W02D7.7.1; WBGene00004766.
DR GeneID; 179213; -.
DR UCSC; W02D7.7.1; c. elegans.
DR CTD; 179213; -.
DR WormBase; W02D7.7; CE14448; WBGene00004766; sel-9.
DR eggNOG; KOG1692; Eukaryota.
DR GeneTree; ENSGT00940000167055; -.
DR HOGENOM; CLU_066963_4_1_1; -.
DR InParanoid; O17528; -.
DR OMA; WHNTEDG; -.
DR OrthoDB; 1328081at2759; -.
DR PhylomeDB; O17528; -.
DR Reactome; R-CEL-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; O17528; -.
DR PRO; PR:O17528; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004766; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; NAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IGI:WormBase.
DR GO; GO:0051049; P:regulation of transport; IMP:UniProtKB.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..203
FT /note="Suppressor/enhancer of lin-12 protein 9"
FT /id="PRO_0000010406"
FT TOPO_DOM 19..170
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..110
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT MUTAGEN 47
FT /note="V->I: In allele sel-9(ar26); suppression of lin-
FT 12(n676n930) egg laying defect."
FT /evidence="ECO:0000269|PubMed:10366590"
FT MUTAGEN 51
FT /note="G->R: In allele sel-9(ar174) and allele sel-
FT 9(ar175); multivulval phenotype in combination with lin-
FT 12(n676n930)."
FT /evidence="ECO:0000269|PubMed:10366590"
FT MUTAGEN 51
FT /note="G->S: In allele sel-9(ar176); multivulval phenotype
FT in combination with lin-12(n676n930)."
FT /evidence="ECO:0000269|PubMed:10366590"
FT MUTAGEN 97
FT /note="S->N: In allele sel-9(ar22) and allele sel-9(ar177);
FT suppression of lin-12(n676n930) egg laying defect."
FT /evidence="ECO:0000269|PubMed:10366590"
FT MUTAGEN 140
FT /note="S->F: In mg550; defective expression of the
FT proteasomal subunit rpt-3 in a pbs-5 (proteasomal subunit)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:27528192"
SQ SEQUENCE 203 AA; 22986 MW; 1BF41F88511E9148 CRC64;
MNSLTWILAV LFVTPAASYF IHVDANEEQC FFDRLTSGTK MGLMFEVAEG GFLDIDVKIT
GPDNKEIYKG ERESSGKFTF AAHMDGVYTY CFGNKMSTMT PKAVMFTVEI TEPHQQAPGA
AANQDAADNA KLEEMVRELS SALMSVKHEQ EYMEVRERVH RNINENTNSR VVMWAAFEAF
VLVGMTVGQI FYLKRFFEVR TMV
