ID   ER442_CAEEL             Reviewed;         413 AA.
AC   Q17688;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Endoplasmic reticulum resident protein 44.2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=erp-44.2 {ECO:0000312|WormBase:C06A6.5};
GN   ORFNames=C06A6.5 {ECO:0000312|WormBase:C06A6.5};
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-264, 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-264, 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: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:Q9BS26}.
CC   -!- DOMAIN: The thioredoxin domain lacks the 2 redox-active Cys. This
CC       strongly suggests that it lacks thioredoxin activity.
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DR   EMBL; BX284604; CCD63307.1; -; Genomic_DNA.
DR   PIR; T29269; T29269.
DR   RefSeq; NP_501303.1; NM_068902.4.
DR   AlphaFoldDB; Q17688; -.
DR   SMR; Q17688; -.
DR   BioGRID; 42689; 2.
DR   DIP; DIP-25109N; -.
DR   STRING; 6239.C06A6.5; -.
DR   iPTMnet; Q17688; -.
DR   EPD; Q17688; -.
DR   PaxDb; Q17688; -.
DR   PeptideAtlas; Q17688; -.
DR   EnsemblMetazoa; C06A6.5.1; C06A6.5.1; WBGene00015510.
DR   GeneID; 177572; -.
DR   KEGG; cel:CELE_C06A6.5; -.
DR   UCSC; C06A6.5; c. elegans.
DR   CTD; 177572; -.
DR   WormBase; C06A6.5; CE27661; WBGene00015510; erp-44.2.
DR   eggNOG; KOG0912; Eukaryota.
DR   HOGENOM; CLU_054449_1_0_1; -.
DR   InParanoid; Q17688; -.
DR   OMA; FQHMFLF; -.
DR   OrthoDB; 623253at2759; -.
DR   PhylomeDB; Q17688; -.
DR   PRO; PR:Q17688; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00015510; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03072; PDI_b'_ERp44; 1.
DR   CDD; cd03070; PDI_b_ERp44; 1.
DR   InterPro; IPR041862; ERp44_PDI_b.
DR   InterPro; IPR041870; ERp44_PDI_b.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..413
FT                   /note="Endoplasmic reticulum resident protein 44.2"
FT                   /id="PRO_0000250587"
FT   DOMAIN          22..136
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          367..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           410..413
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        397..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   DISULFID        184..233
FT                   /evidence="ECO:0000250|UniProtKB:Q9BS26"
SQ   SEQUENCE   413 AA;  47197 MW;  F8DC1FCE63D65DD5 CRC64;
     MNLASVLLLL AACHLSVSVN GQEHKEAIEL SMANHDHVLG SAQVVFVAFC ADWCPFSRRL
     KPIFEESARV FHQENPQASA VWAIVDSQRQ ADIGDKYFVN KYPTMKVFVN GELITKEYRS
     TRSVEALTNF VKFQLSTAIN EFSSQDQLNQ EMDKSKRNVV AWLKKDGPEF ANLKKVASIL
     REDCSFWVPT DHFGTQTNDN KLSFFDPDSN EEAKFTGNFN DYDFVKQWVT DKCIPLVREV
     TFENVEELTE EGMPFLIYFR DPDNKTTDKV FGEAVARELY DQRSAINPLL ADGHKFAHPL
     KHLGKTKEDL PVLAIDSFQH MYLFPDMTQM NIPGKLREFV MDLHSGKLHK DFHENLDQRM
     IELAKAKAAR GITDDHEAQA PSTRPIDTTP PPSVFKELKP SDKRYSILQK SEL