ID   YVRI_CAEEL              Reviewed;         277 AA.
AC   O17861;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=GILT-like protein F37H8.5;
DE   Flags: Precursor;
GN   ORFNames=F37H8.5;
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-77, 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-77, AND IDENTIFICATION BY MASS
RP   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-77, AND IDENTIFICATION BY MASS
RP   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: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GILT family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z81534; CAB04345.1; -; Genomic_DNA.
DR   PIR; T21922; T21922.
DR   RefSeq; NP_496397.1; NM_063996.3.
DR   AlphaFoldDB; O17861; -.
DR   SMR; O17861; -.
DR   BioGRID; 532192; 18.
DR   STRING; 6239.F37H8.5; -.
DR   iPTMnet; O17861; -.
DR   EPD; O17861; -.
DR   PaxDb; O17861; -.
DR   PeptideAtlas; O17861; -.
DR   EnsemblMetazoa; F37H8.5.1; F37H8.5.1; WBGene00009514.
DR   GeneID; 3564874; -.
DR   KEGG; cel:CELE_F37H8.5; -.
DR   UCSC; F37H8.5; c. elegans.
DR   CTD; 3564874; -.
DR   WormBase; F37H8.5; CE15997; WBGene00009514; -.
DR   eggNOG; KOG3160; Eukaryota.
DR   HOGENOM; CLU_066886_0_0_1; -.
DR   InParanoid; O17861; -.
DR   OMA; PTLLCEW; -.
DR   OrthoDB; 803513at2759; -.
DR   PhylomeDB; O17861; -.
DR   PRO; PR:O17861; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00009514; Expressed in larva and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; HDA:WormBase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR   InterPro; IPR004911; Interferon-induced_GILT.
DR   PANTHER; PTHR13234; PTHR13234; 1.
DR   Pfam; PF03227; GILT; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..277
FT                   /note="GILT-like protein F37H8.5"
FT                   /id="PRO_0000248561"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   277 AA;  30844 MW;  990F2C2E03EC3532 CRC64;
     MDTTCRCLLT PTIQPVLLKM LYRLVAAILL LGAVQATINC AAIPTSLWCS NKDLEAKCGF
     ASFCDKHRAA THNQKINITV LIEALCPDCQ NFLTKQLYPI VFKNFANYVN IELVPFGNAK
     VLEDGTIKCQ HGEEECSINK FEGCFIDSMQ DQSPLPTLSC IEESLQKKVE FADAVQQCFE
     KLQIGGDIQR LTQSCLVSKL GADLQNKAAA ATANVWPEQH KFVPWVIING VSLTSFQGFQ
     NQLPTLLCEW YSGDKAIPYC EAALKLKYKK ASIRSFF