ERO1B_HUMAN
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 03-AUG-2022, entry version 161.
DE RecName: Full=ERO1-like protein beta;
DE Short=ERO1-L-beta;
DE EC=1.8.4.-;
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, POSSIBLE HOMODIMERIZATION, AND ASSOCIATION 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, COFACTOR, HOMODIMERIZATION, DISULFIDE BONDS, AND MUTAGENESIS OF
RP 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 -!- 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; 51.
DR IntAct; Q86YB8; 21.
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 GlyGen; Q86YB8; 4 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q86YB8; -.
DR PhosphoSitePlus; Q86YB8; -.
DR BioMuta; ERO1B; -.
DR DMDM; 116241353; -.
DR EPD; Q86YB8; -.
DR jPOST; Q86YB8; -.
DR MassIVE; Q86YB8; -.
DR MaxQB; Q86YB8; -.
DR PaxDb; Q86YB8; -.
DR PeptideAtlas; Q86YB8; -.
DR PRIDE; Q86YB8; -.
DR ProteomicsDB; 4009; -.
DR ProteomicsDB; 70394; -. [Q86YB8-1]
DR Antibodypedia; 34698; 202 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 CTD; 56605; -.
DR DisGeNET; 56605; -.
DR GeneCards; ERO1B; -.
DR HGNC; HGNC:14355; ERO1B.
DR HPA; ENSG00000086619; Tissue enhanced (pancreas).
DR MIM; 615437; gene.
DR neXtProt; NX_Q86YB8; -.
DR OpenTargets; ENSG00000086619; -.
DR PharmGKB; PA134918597; -.
DR VEuPathDB; HostDB:ENSG00000086619; -.
DR eggNOG; KOG2608; Eukaryota.
DR GeneTree; ENSGT00390000007753; -.
DR HOGENOM; CLU_023061_2_2_1; -.
DR InParanoid; Q86YB8; -.
DR OMA; RDYCVPD; -.
DR OrthoDB; 1181226at2759; -.
DR PhylomeDB; Q86YB8; -.
DR TreeFam; TF314471; -.
DR BioCyc; MetaCyc:ENSG00000086619-MON; -.
DR PathwayCommons; Q86YB8; -.
DR Reactome; R-HSA-264876; Insulin processing.
DR SignaLink; Q86YB8; -.
DR SIGNOR; Q86YB8; -.
DR BioGRID-ORCS; 56605; 9 hits in 1073 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 162 other tissues.
DR ExpressionAtlas; Q86YB8; baseline and differential.
DR Genevisible; Q86YB8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0016972; F:thiol oxidase activity; IDA:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
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; PTHR12613; 1.
DR Pfam; PF04137; ERO1; 1.
DR PIRSF; PIRSF017205; ERO1; 1.
DR SUPFAM; SSF110019; SSF110019; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Electron transport;
KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Membrane;
KW Oxidoreductase; Redox-active center; 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 catalytic activity when DTT is
FT used as an electron donor; when associated with A-95. Loss
FT of catalytic activity when P4HB is used as an electron
FT donor; when associated with A-95."
FT /evidence="ECO:0000269|PubMed:21091435"
FT MUTAGEN 95
FT /note="C->A: No effect on catalytic activity when DTT is
FT used as an electron donor; when associated with A-90. Loss
FT of catalytic activity when P4HB is used as an electron
FT donor; when associated with A-90."
FT /evidence="ECO:0000269|PubMed:21091435"
FT MUTAGEN 100
FT /note="C->A: Slightly decrease in activity. Significant
FT increased activity; when associated with A-130."
FT /evidence="ECO:0000269|PubMed:21091435"
FT MUTAGEN 130
FT /note="C->A: Small increase in activity. Significant
FT increased activity; when 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 catalytic
FT activity when DTT or P4HB are used as an electron donor;
FT 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
FT catalytic 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
