ID ERO1B_HUMAN Reviewed; 467 AA. AC Q86YB8; B4DF57; Q5T1H4; Q8IZ11; Q9NR62; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 28-JAN-2026, entry version 178. DE RecName: Full=ERO1-like protein beta {ECO:0000303|PubMed:10818100}; DE Short=ERO1-L-beta {ECO:0000303|PubMed:10818100}; DE EC=1.8.3.2 {ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:21091435}; DE AltName: Full=Endoplasmic reticulum oxidoreductase beta {ECO:0000312|HGNC:HGNC:14355}; DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein B; DE AltName: Full=Oxidoreductin-1-L-beta; DE Flags: Precursor; GN Name=ERO1B {ECO:0000312|HGNC:HGNC:14355}; Synonyms=ERO1LB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, GLYCOSYLATION, INDUCTION, AND VARIANT GLN-465. RX PubMed=10818100; DOI=10.1074/jbc.m003061200; RA Pagani M., Fabbri M., Benedetti C., Fassio A., Pilati S., Bulleid N.J., RA Cabibbo A., Sitia R.; RT "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene RT induced in the course of the unfolded protein response."; RL J. Biol. Chem. 275:23685-23692(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-129. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, POSSIBLE HOMODIMERIZATION, AND ASSOCIATION RP WITH P4HB. RX PubMed=11707400; DOI=10.1093/emboj/20.22.6288; RA Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I., Sitia R.; RT "Manipulation of oxidative protein folding and PDI redox state in mammalian RT cells."; RL EMBO J. 20:6288-6296(2001). RN [6] RP INTERACTION WITH ERP44. RX PubMed=11847130; DOI=10.1093/emboj/21.4.835; RA Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., RA Sitia R.; RT "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin RT family."; RL EMBO J. 21:835-844(2002). RN [7] RP INDUCTION. RX PubMed=12752442; DOI=10.1046/j.1432-1033.2003.03590.x; RA Gess B., Hofbauer K.H., Wenger R.H., Lohaus C., Meyer H.E., Kurtz A.; RT "The cellular oxygen tension regulates expression of the endoplasmic RT oxidoreductase ERO1-Lalpha."; RL Eur. J. Biochem. 270:2228-2235(2003). RN [8] RP ACTIVITY REGULATION. RX PubMed=15161913; DOI=10.1074/jbc.m404992200; RA Nerini Molteni S., Fassio A., Ciriolo M.R., Filomeni G., Pasqualetto E., RA Fagioli C., Sitia R.; RT "Glutathione limits Ero1-dependent oxidation in the endoplasmic RT reticulum."; RL J. Biol. Chem. 279:32667-32673(2004). RN [9] RP INTERACTION WITH ERO1L AND P4HB, HOMODIMERIZATION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF CYS-390; CYS-393 AND CYS-396. RX PubMed=16012172; DOI=10.1074/jbc.m505023200; RA Dias-Gunasekara S., Gubbens J., van Lith M., Dunne C., Williams J.A., RA Kataky R., Scoones D., Lapthorn A., Bulleid N.J., Benham A.M.; RT "Tissue-specific expression and dimerization of the endoplasmic reticulum RT oxidoreductase Ero1beta."; RL J. Biol. Chem. 280:33066-33075(2005). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140. RC TISSUE=Platelet; RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200; RA Lewandrowski U., Moebius J., Walter U., Sickmann A.; RT "Elucidation of N-glycosylation sites on human platelet proteins: a RT glycoproteomic approach."; RL Mol. Cell. Proteomics 5:226-233(2006). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, HOMODIMERIZATION, DISULFIDE BONDS, RP AND MUTAGENESIS OF CYS-90; CYS-95; CYS-100; CYS-130; CYS-393 AND CYS-396. RX PubMed=21091435; DOI=10.1042/bj20101357; RA Wang L., Zhu L., Wang C.C.; RT "The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient RT oxidative protein folding with loose regulation."; RL Biochem. J. 434:113-121(2011). CC -!- FUNCTION: Oxidoreductase involved in disulfide bond formation in the CC endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme CC catalyzing protein disulfide formation, in order to allow P4HB to CC sustain additional rounds of disulfide formation. Other protein CC disulfide isomerase family members can also be reoxidized, but at lower CC rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), CC as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB CC reoxidation, passes its electrons to molecular oxygen via FAD, leading CC to the production of reactive oxygen species (ROS) in the cell. May be CC involved in oxidative proinsulin folding in pancreatic cells, hence may CC play a role in glucose homeostasis. {ECO:0000269|PubMed:11707400, CC ECO:0000269|PubMed:21091435}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2; CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; CC Evidence={ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:21091435}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17358; CC Evidence={ECO:0000305|PubMed:11707400, ECO:0000305|PubMed:21091435}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-dithiol + O2 = [protein]-disulfide + H2O2; CC Xref=Rhea:RHEA:59116, Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:50058; Evidence={ECO:0000269|PubMed:11707400, CC ECO:0000269|PubMed:21091435}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59117; CC Evidence={ECO:0000305|PubMed:11707400, ECO:0000305|PubMed:21091435}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:21091435}; CC -!- ACTIVITY REGULATION: Glutathione may be required to regulate its CC activity in the endoplasmic reticulum. {ECO:0000269|PubMed:15161913}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with ERO1A; CC disulfide-linked. Also detected as monomer. Homodimers may be somewhat CC less active than monomers. Interacts with P4HB. Interacts with ERP44. CC {ECO:0000269|PubMed:11847130, ECO:0000269|PubMed:16012172, CC ECO:0000269|PubMed:21091435}. CC -!- INTERACTION: CC Q86YB8; P30101: PDIA3; NbExp=2; IntAct=EBI-2806988, EBI-979862; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:10818100}; Peripheral membrane protein CC {ECO:0000269|PubMed:10818100}; Lumenal side CC {ECO:0000269|PubMed:10818100}. Note=The association with ERP44 may be CC essential for its retention in the endoplasmic reticulum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q86YB8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86YB8-2; Sequence=VSP_056988; CC -!- TISSUE SPECIFICITY: Highly expressed in the digestive tract, including CC the duodenum and lower digestive tract. In the stomach, highly CC expressed in enzyme-producing chief cells (at protein level). In the CC pancreas, expressed in islets of Langerhans and, at lower levels, in CC enzyme-secreting cells (at protein level). Detected at low level in CC many other tissues. {ECO:0000269|PubMed:10818100, CC ECO:0000269|PubMed:16012172}. CC -!- INDUCTION: Up-regulated by inducers of the unfolded protein response CC (UPR). {ECO:0000269|PubMed:10818100, ECO:0000269|PubMed:12752442}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10818100, CC ECO:0000269|PubMed:16263699}. CC -!- PTM: The Cys-90/Cys-95 and Cys-393/Cys-396 disulfide bonds constitute CC the redox-active center. The Cys-90/Cys-95 disulfide bond accepts CC electron from P4HB and funnel them to the active site disulfide Cys- CC 393/Cys-396. The Cys-81/Cys-390 disulfide bond may be critical for CC structural stability. Two long-range disulfide bonds participate in CC loose feedback regulation. The Cys-90/Cys-130 disulfide bond may be the CC predominant regulatory switch to modulate the catalytic activity, while CC the Cys-100/Cys-262 disulfide bond may play an auxiliary regulatory CC role. {ECO:0000305|PubMed:21091435}. CC -!- SIMILARITY: Belongs to the EROs 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; AF252538; AAF97547.1; -; mRNA. DR EMBL; AK293941; BAG57318.1; -; mRNA. DR EMBL; AL139162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL450309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032823; AAH32823.2; -; mRNA. DR EMBL; BC044573; AAH44573.1; -; mRNA. DR CCDS; CCDS31064.1; -. [Q86YB8-1] DR RefSeq; NP_063944.3; NM_019891.3. [Q86YB8-1] DR AlphaFoldDB; Q86YB8; -. DR SMR; Q86YB8; -. DR BioGRID; 121155; 58. DR FunCoup; Q86YB8; 1790. DR IntAct; Q86YB8; 39. DR MINT; Q86YB8; -. DR STRING; 9606.ENSP00000346635; -. DR DrugBank; DB01902; 1-Ethyl-Pyrrolidine-2,5-Dione. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR GlyConnect; 1226; 3 N-Linked glycans (1 site). DR GlyCosmos; Q86YB8; 4 sites, 3 glycans. DR GlyGen; Q86YB8; 4 sites, 12 N-linked glycans (3 sites). DR iPTMnet; Q86YB8; -. DR PhosphoSitePlus; Q86YB8; -. DR BioMuta; ERO1B; -. DR DMDM; 116241353; -. DR jPOST; Q86YB8; -. DR MassIVE; Q86YB8; -. DR PaxDb; 9606-ENSP00000346635; -. DR PeptideAtlas; Q86YB8; -. DR ProteomicsDB; 4009; -. DR ProteomicsDB; 70394; -. [Q86YB8-1] DR Pumba; Q86YB8; -. DR Antibodypedia; 34698; 190 antibodies from 25 providers. DR DNASU; 56605; -. DR Ensembl; ENST00000354619.10; ENSP00000346635.5; ENSG00000086619.15. [Q86YB8-1] DR GeneID; 56605; -. DR KEGG; hsa:56605; -. DR MANE-Select; ENST00000354619.10; ENSP00000346635.5; NM_019891.4; NP_063944.3. DR UCSC; uc001hxt.4; human. [Q86YB8-1] DR AGR; HGNC:14355; -. DR ClinPGx; PA134918597; -. DR CTD; 56605; -. DR DisGeNET; 56605; -. DR GeneCards; ERO1B; -. DR HGNC; HGNC:14355; ERO1B. DR HPA; ENSG00000086619; Tissue enriched (pancreas). DR MIM; 615437; gene. DR OpenTargets; ENSG00000086619; -. DR VEuPathDB; HostDB:ENSG00000086619; -. DR eggNOG; KOG2608; Eukaryota. DR GeneTree; ENSGT00390000007753; -. DR HOGENOM; CLU_023061_2_2_1; -. DR InParanoid; Q86YB8; -. DR OMA; CYKDRLH; -. DR OrthoDB; 269384at2759; -. DR PAN-GO; Q86YB8; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q86YB8; -. DR BioCyc; MetaCyc:ENSG00000086619-MONOMER; -. DR PathwayCommons; Q86YB8; -. DR Reactome; R-HSA-264876; Insulin processing. DR SignaLink; Q86YB8; -. DR SIGNOR; Q86YB8; -. DR Agora; ENSG00000086619; -. DR BioGRID-ORCS; 56605; 11 hits in 1154 CRISPR screens. DR ChiTaRS; ERO1B; human. DR GeneWiki; ERO1LB; -. DR GenomeRNAi; 56605; -. DR Pharos; Q86YB8; Tbio. DR PRO; PR:Q86YB8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q86YB8; protein. DR Bgee; ENSG00000086619; Expressed in body of pancreas and 163 other cell types or tissues. DR ExpressionAtlas; Q86YB8; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; NAS:UniProtKB. DR GO; GO:0015035; F:protein-disulfide reductase activity; EXP:Reactome. DR GO; GO:0016972; F:thiol oxidase activity; IDA:FlyBase. DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl. DR GO; GO:0030070; P:insulin processing; TAS:Reactome. DR GO; GO:0006457; P:protein folding; TAS:UniProtKB. DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IDA:FlyBase. DR InterPro; IPR007266; Ero1. DR InterPro; IPR037192; ERO1-like_sf. DR PANTHER; PTHR12613:SF2; ERO1-LIKE PROTEIN BETA; 1. DR PANTHER; PTHR12613; ERO1-RELATED; 1. DR Pfam; PF04137; ERO1; 1. DR PIRSF; PIRSF017205; ERO1; 1. DR SUPFAM; SSF110019; ERO1-like; 1. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; Electron transport; KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Membrane; KW Oxidoreductase; Proteomics identification; Redox-active center; KW Reference proteome; Signal; Transport. FT SIGNAL 1..33 FT /evidence="ECO:0000255" FT CHAIN 34..467 FT /note="ERO1-like protein beta" FT /id="PRO_0000008418" FT BINDING 186 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q96HE7" FT BINDING 188 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q96HE7" FT BINDING 199 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q96HE7" FT BINDING 251 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q96HE7" FT BINDING 254 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q96HE7" FT BINDING 286 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q96HE7" FT BINDING 299 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:Q96HE7" FT CARBOHYD 122 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16263699" FT CARBOHYD 145 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 383 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 81..390 FT /evidence="ECO:0000269|PubMed:21091435" FT DISULFID 90..130 FT /note="Alternate" FT /evidence="ECO:0000269|PubMed:21091435" FT DISULFID 90..95 FT /note="Redox-active; alternate" FT /evidence="ECO:0000269|PubMed:21091435" FT DISULFID 100..262 FT /evidence="ECO:0000269|PubMed:21091435" FT DISULFID 207..240 FT /evidence="ECO:0000269|PubMed:21091435" FT DISULFID 393..396 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:21091435" FT VAR_SEQ 144..466 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056988" FT VARIANT 129 FT /note="D -> V (in dbSNP:rs2477599)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_028012" FT VARIANT 465 FT /note="H -> Q (in dbSNP:rs1055851)" FT /evidence="ECO:0000269|PubMed:10818100" FT /id="VAR_019492" FT MUTAGEN 90 FT /note="C->A: No effect on thiol oxidase activity when DTT FT is used as an electron donor; when associated with A-95. FT Loss of thiol oxidase activity when P4HB is used as an FT electron donor; when associated with A-95." FT /evidence="ECO:0000269|PubMed:21091435" FT MUTAGEN 95 FT /note="C->A: No effect on thiol oxidase activity when DTT FT is used as an electron donor; when associated with A-90. FT Loss of thiol oxidase activity when P4HB is used as an FT electron donor; when associated with A-90." FT /evidence="ECO:0000269|PubMed:21091435" FT MUTAGEN 100 FT /note="C->A: Slightly decreased thiol oxidase activity. FT Significant increased thiol oxidase activity; when FT associated with A-130." FT /evidence="ECO:0000269|PubMed:21091435" FT MUTAGEN 130 FT /note="C->A: Small increase in thiol oxidase activity. FT Significant increased thiol oxidase activity; when FT associated with A-130." FT /evidence="ECO:0000269|PubMed:21091435" FT MUTAGEN 390 FT /note="C->A: Strong decrease in P4HB-binding. Efficient FT homodimerization with both wild-type and A-390 mutated FT protein." FT /evidence="ECO:0000269|PubMed:16012172" FT MUTAGEN 393 FT /note="C->A: Some decrease in P4HB-binding. Efficient FT homodimerization with wild-type protein. Loss of thiol FT oxidase activity when DTT or P4HB are used as an electron FT donor; when associated with A-396." FT /evidence="ECO:0000269|PubMed:16012172, FT ECO:0000269|PubMed:21091435" FT MUTAGEN 396 FT /note="C->A: Some decrease in P4HB-binding. Efficient FT homodimerization with wild-type protein, but loss of FT homodimerization with A-396 mutated protein. Loss of thiol FT oxidase activity when DTT or P4HB are used as an electron FT donor; when associated with A-393." FT /evidence="ECO:0000269|PubMed:16012172, FT ECO:0000269|PubMed:21091435" SQ SEQUENCE 467 AA; 53543 MW; 4DA8753DDEE15314 CRC64; MSQGVRRAGA GQGVAAAVQL LVTLSFLRSV VEAQVTGVLD DCLCDIDSID NFNTYKIFPK IKKLQERDYF RYYKVNLKRP CPFWAEDGHC SIKDCHVEPC PESKIPVGIK AGHSNKYLKM ANNTKELEDC EQANKLGAIN STLSNQSKEA FIDWARYDDS RDHFCELDDE RSPAAQYVDL LLNPERYTGY KGTSAWRVWN SIYEENCFKP RSVYRPLNPL APSRGEDDGE SFYTWLEGLC LEKRVFYKLI SGLHASINLH LCANYLLEET WGKPSWGPNI KEFKHRFDPV ETKGEGPRRL KNLYFLYLIE LRALSKVAPY FERSIVDLYT GNAEEDADTK TLLLNIFQDT KSFPMHFDEK SMFAGDKKGA KSLKEEFRLH FKNISRIMDC VGCDKCRLWG KLQTQGLGTA LKILFSEKEI QKLPENSPSK GFQLTRQEIV ALLNAFGRLS TSIRDLQNFK VLLQHSR //