CUP15_CAEEL
ID CUP15_CAEEL Reviewed; 322 AA.
AC Q09322;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Coelomocyte uptake defective protein 15 {ECO:0000312|WormBase:F42A8.3};
DE Flags: Precursor;
GN Name=cup-15 {ECO:0000303|PubMed:28122949, ECO:0000312|WormBase:F42A8.3};
GN ORFNames=F42A8.3 {ECO:0000312|WormBase:F42A8.3};
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 [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 [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98 AND ASN-144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 233-TRP--ARG-322.
RX PubMed=28122949; DOI=10.1534/g3.116.037515;
RA Gee K., Zamora D., Horm T., George L., Upchurch C., Randall J., Weaver C.,
RA Sanford C., Miller A., Hernandez S., Dang H., Fares H.;
RT "Regulators of Lysosome Function and Dynamics in Caenorhabditis elegans.";
RL G3 (Bethesda) 7:991-1000(2017).
CC -!- FUNCTION: Modulates the transport of substances from the endosomal to
CC lysosomal compartments. Plays a role in lysosome formation and function
CC in coelomocytes. {ECO:0000269|PubMed:28122949}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the
CC accumulation of substances in coelomocytes within the body wall cavity,
CC which may be indicative of lysosomal defects.
CC {ECO:0000269|PubMed:28122949}.
CC -!- SIMILARITY: Belongs to the OSTM1 family. {ECO:0000305}.
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DR EMBL; BX284602; CAA87781.2; -; Genomic_DNA.
DR PIR; T22084; T22084.
DR RefSeq; NP_495993.2; NM_063592.3.
DR AlphaFoldDB; Q09322; -.
DR SMR; Q09322; -.
DR BioGRID; 39807; 1.
DR STRING; 6239.F42A8.3; -.
DR iPTMnet; Q09322; -.
DR EPD; Q09322; -.
DR PaxDb; Q09322; -.
DR PeptideAtlas; Q09322; -.
DR EnsemblMetazoa; F42A8.3.1; F42A8.3.1; WBGene00009627.
DR UCSC; F42A8.3; c. elegans.
DR WormBase; F42A8.3; CE35875; WBGene00009627; cup-15.
DR eggNOG; KOG4617; Eukaryota.
DR GeneTree; ENSGT00390000012341; -.
DR HOGENOM; CLU_858513_0_0_1; -.
DR InParanoid; Q09322; -.
DR OMA; FQQVASK; -.
DR OrthoDB; 1105868at2759; -.
DR PhylomeDB; Q09322; -.
DR Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR PRO; PR:Q09322; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009627; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007040; P:lysosome organization; IMP:WormBase.
DR InterPro; IPR019172; Osteopetrosis-assoc_TM_1.
DR PANTHER; PTHR15644; PTHR15644; 1.
DR Pfam; PF09777; OSTMP1; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..322
FT /note="Coelomocyte uptake defective protein 15"
FT /evidence="ECO:0000305"
FT /id="PRO_0000014283"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 233..322
FT /note="Missing: In cd33; results in viable animals, but
FT hermaphrodites have larger early endosomes in coelomocytes
FT within the body wall cavity. Coelomocytes are able to
FT undergo endocytic uptake, but defects are most likely due
FT to a delay in the transport of substances from the
FT endosomal to lysosomal compartments and maybe irregular
FT lysosomal degradation in coelomocytes."
FT /evidence="ECO:0000269|PubMed:28122949"
SQ SEQUENCE 322 AA; 37104 MW; 63B540971E55E749 CRC64;
MVNSLSRILF CSLLIFSVIS LREERLETAP ITDDPWDLDG PCQKYVEKLA VVQSEMVACA
TNWSIPPVVC TKCFQNYINF KQFEYETKNL NNVYSLDNRT CSQVIYDNYL LSYSTDISKA
LTSEIWEKSR CDSCITIKWN FPQNKSEVSF SERTMQFQNR MYEWRNCVVN YTSGGVLDDN
LTNGSKICNL CKTTFDELFG YYWKIYTTPD VDFCVDVETT MNDTIHLWDD VWKCAEKQDR
NRDLFGIMIT FGTLLLLTAL FYAASYIQGG GETRRLIQYA RLSDPHGQRS RLLSSGMSDA
DLVSRVSPGS SVLYNVPIHQ TR
