Y92H3_CAEEL
ID Y92H3_CAEEL Reviewed; 637 AA.
AC Q9BPN8; Q3V5I6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Uncharacterized protein Y92H12BR.3;
GN ORFNames=Y92H12BR.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], AND ALTERNATIVE SPLICING.
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-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102; ASN-111; ASN-253 AND
RP ASN-277, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102; ASN-111; ASN-178; ASN-461;
RP ASN-537 AND ASN-552, AND 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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9BPN8-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9BPN8-2; Sequence=VSP_020302;
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DR EMBL; FO081323; CCD70784.1; -; Genomic_DNA.
DR EMBL; FO081323; CCD70785.1; -; Genomic_DNA.
DR RefSeq; NP_001032990.1; NM_001037901.3. [Q9BPN8-1]
DR RefSeq; NP_001032991.1; NM_001037902.1. [Q9BPN8-2]
DR AlphaFoldDB; Q9BPN8; -.
DR BioGRID; 37203; 1.
DR STRING; 6239.Y92H12BR.3a; -.
DR iPTMnet; Q9BPN8; -.
DR EPD; Q9BPN8; -.
DR PaxDb; Q9BPN8; -.
DR PeptideAtlas; Q9BPN8; -.
DR EnsemblMetazoa; Y92H12BR.3a.1; Y92H12BR.3a.1; WBGene00022369. [Q9BPN8-1]
DR EnsemblMetazoa; Y92H12BR.3b.1; Y92H12BR.3b.1; WBGene00022369. [Q9BPN8-2]
DR GeneID; 171707; -.
DR KEGG; cel:CELE_Y92H12BR.3; -.
DR UCSC; Y92H12BR.3b; c. elegans. [Q9BPN8-1]
DR CTD; 171707; -.
DR WormBase; Y92H12BR.3a; CE29936; WBGene00022369; -. [Q9BPN8-1]
DR WormBase; Y92H12BR.3b; CE39075; WBGene00022369; -. [Q9BPN8-2]
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_436957_0_0_1; -.
DR InParanoid; Q9BPN8; -.
DR OMA; NFFFKQI; -.
DR OrthoDB; 783817at2759; -.
DR PRO; PR:Q9BPN8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022369; Expressed in adult organism and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..637
FT /note="Uncharacterized protein Y92H12BR.3"
FT /id="PRO_0000248542"
FT TOPO_DOM 1..600
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT VAR_SEQ 105..470
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020302"
SQ SEQUENCE 637 AA; 71086 MW; 749AEA6080732EE9 CRC64;
MKAQLAILSL LVGLLAAQDL RSLLDICANP PKTTPKTLSD KISLPESYKI SGSMTDWMKA
STSLLVESAS KEFRVLEKQT RDQMPEKWIQ ELTGAKLTSF INVTSGECIG NVSKPDLFKI
SRFESIIGAD TSSLYSIILG LIEFDKSHTG FFVEDHVEVV GGVNAQKWVT CIDGATANDT
KVLLEVRYAG EETIRPAQSP FSNPLLLSIR LAELPNFNST VALNHVSVEL DRYELPVGNE
AAVVHGVWCK NRNDTVLVLK PLDEYAAILN YFDPSTNRSD VVEVLYSKTK KVIHIAGDSF
ENGVKLFKAT PKRYKNGTDY ILHDFNYGYE FTMSHGACQS FSPLDDSSED VLVKNGTDHF
IMNNMEWLLV DPGLRFSLYE SDVDMVGTAF KTYRAYDGRD ETIVELHVTE DMEVHSMARF
RMGSRHLAVS LTVQRIPMES SRLNMKTVQL SNCYDEQKFA NNTLMVQIKD KTLSDLSQVG
LNGLNEAVAS SISKNVHPII PYRVIVFYVE SRDSGLEMIV RVAEKTEKKP GNVVGYNYTT
ELTTAEIFKL MNDSMTLDKM PIEVLKNNGV KEEWMADAST MKMYPPENDD GFIGYTGGAM
FVLAIFCLLI GVSIGAVGVF VATRRQRIST LAYQVFE