VKORL_HUMAN
ID VKORL_HUMAN Reviewed; 176 AA.
AC Q8N0U8; B4E222; E7ETM5; Q6AHW9; Q6TEK6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Vitamin K epoxide reductase complex subunit 1-like protein 1;
DE Short=VKORC1-like protein 1;
DE EC=1.17.4.4 {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:23928358, ECO:0000269|PubMed:24532791};
GN Name=VKORC1L1;
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).
RC TISSUE=Kidney;
RX PubMed=14765194; DOI=10.1038/nature02214;
RA Rost S., Fregin A., Ivaskevicius V., Conzelmann E., Hoertnagel K.,
RA Pelz H.-J., Lappegard K., Seifried E., Scharrer I., Tuddenham E.G.D.,
RA Mueller C.R., Strom T.M., Oldenburg J.;
RT "Mutations in VKORC1 cause warfarin resistance and multiple coagulation
RT factor deficiency type 2.";
RL Nature 427:537-541(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-176 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AND INDUCTION BY OXIDATIVE STRESS.
RX PubMed=21367861; DOI=10.1074/jbc.m110.210971;
RA Westhofen P., Watzka M., Marinova M., Hass M., Kirfel G., Muller J.,
RA Bevans C.G., Muller C.R., Oldenburg J.;
RT "Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1)
RT mediates vitamin K-dependent intracellular antioxidant function.";
RL J. Biol. Chem. 286:15085-15094(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=23928358; DOI=10.1074/jbc.m113.457119;
RA Hammed A., Matagrin B., Spohn G., Prouillac C., Benoit E., Lattard V.;
RT "VKORC1L1, an enzyme rescuing the vitamin K 2,3-epoxide reductase activity
RT in some extrahepatic tissues during anticoagulation therapy.";
RL J. Biol. Chem. 288:28733-28742(2013).
RN [10]
RP TOPOLOGY, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF CYS-50 AND CYS-58.
RX PubMed=24532791; DOI=10.1074/jbc.m113.534446;
RA Tie J.K., Jin D.Y., Stafford D.W.;
RT "Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-
RT like 1 (VKORC1L1) are involved in its active site regeneration.";
RL J. Biol. Chem. 289:9396-9407(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in vitamin K metabolism. Can reduce inactive vitamin
CC K 2,3-epoxide to active vitamin K (in vitro), and may contribute to
CC vitamin K-mediated protection against oxidative stress. Plays a role in
CC vitamin K-dependent gamma-carboxylation of Glu residues in target
CC proteins. {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:23928358,
CC ECO:0000269|PubMed:24532791}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + H2O + phylloquinone = 2,3-
CC epoxyphylloquinone + [protein]-dithiol; Xref=Rhea:RHEA:13817,
CC Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15759, ChEBI:CHEBI:18067, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058; EC=1.17.4.4;
CC Evidence={ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:23928358,
CC ECO:0000269|PubMed:24532791};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + phylloquinol = [protein]-dithiol +
CC phylloquinone; Xref=Rhea:RHEA:57744, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:18067, ChEBI:CHEBI:28433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058; EC=1.17.4.4;
CC Evidence={ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:23928358,
CC ECO:0000269|PubMed:24532791};
CC -!- ACTIVITY REGULATION: Inhibited by warfarin (coumadin).
CC {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:23928358,
CC ECO:0000269|PubMed:24532791}.
CC -!- INTERACTION:
CC Q8N0U8; P01019: AGT; NbExp=3; IntAct=EBI-11337915, EBI-751728;
CC Q8N0U8; Q13520: AQP6; NbExp=3; IntAct=EBI-11337915, EBI-13059134;
CC Q8N0U8; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-11337915, EBI-2837444;
CC Q8N0U8; P78371: CCT2; NbExp=3; IntAct=EBI-11337915, EBI-357407;
CC Q8N0U8; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-11337915, EBI-1045797;
CC Q8N0U8; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-11337915, EBI-781551;
CC Q8N0U8; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-11337915, EBI-3917143;
CC Q8N0U8; Q8TED1: GPX8; NbExp=3; IntAct=EBI-11337915, EBI-11721746;
CC Q8N0U8; P03952: KLKB1; NbExp=3; IntAct=EBI-11337915, EBI-10087153;
CC Q8N0U8; P06858: LPL; NbExp=3; IntAct=EBI-11337915, EBI-715909;
CC Q8N0U8; Q6IN84: MRM1; NbExp=3; IntAct=EBI-11337915, EBI-5454865;
CC Q8N0U8; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-11337915, EBI-12806656;
CC Q8N0U8; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-11337915, EBI-3923617;
CC Q8N0U8; P49585: PCYT1A; NbExp=3; IntAct=EBI-11337915, EBI-2563309;
CC Q8N0U8; Q9Y5K3-3: PCYT1B; NbExp=8; IntAct=EBI-11337915, EBI-12280028;
CC Q8N0U8; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-11337915, EBI-11742770;
CC Q8N0U8; P40337-2: VHL; NbExp=3; IntAct=EBI-11337915, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21367861, ECO:0000269|PubMed:24532791}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:21367861,
CC ECO:0000269|PubMed:24532791}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N0U8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N0U8-2; Sequence=VSP_055709;
CC -!- INDUCTION: Up-regulated in response to oxidative stress induced by
CC hydrogen peroxide treatment. {ECO:0000269|PubMed:21367861}.
CC -!- MISCELLANEOUS: The location of two cysteine active-site residues within
CC a proposed transmembrane is consistent both with the known hydrophobic
CC environment of the thiol redox site of the enzyme and with the
CC lipophilicity of vitamin K and warfarin (coumadin).
CC -!- SIMILARITY: Belongs to the VKOR family. {ECO:0000305}.
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DR EMBL; AY423045; AAR82915.1; -; mRNA.
DR EMBL; AK304077; BAG64984.1; -; mRNA.
DR EMBL; AC073261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027734; AAH27734.2; -; mRNA.
DR EMBL; CR627471; CAH10673.1; -; mRNA.
DR CCDS; CCDS5529.1; -. [Q8N0U8-1]
DR CCDS; CCDS64663.1; -. [Q8N0U8-2]
DR RefSeq; NP_001271271.1; NM_001284342.2. [Q8N0U8-2]
DR RefSeq; NP_775788.2; NM_173517.5. [Q8N0U8-1]
DR AlphaFoldDB; Q8N0U8; -.
DR SMR; Q8N0U8; -.
DR BioGRID; 127558; 116.
DR IntAct; Q8N0U8; 34.
DR MINT; Q8N0U8; -.
DR STRING; 9606.ENSP00000403077; -.
DR BindingDB; Q8N0U8; -.
DR DrugBank; DB00170; Menadione.
DR DrugCentral; Q8N0U8; -.
DR iPTMnet; Q8N0U8; -.
DR PhosphoSitePlus; Q8N0U8; -.
DR SwissPalm; Q8N0U8; -.
DR BioMuta; VKORC1L1; -.
DR DMDM; 62511214; -.
DR EPD; Q8N0U8; -.
DR jPOST; Q8N0U8; -.
DR MassIVE; Q8N0U8; -.
DR MaxQB; Q8N0U8; -.
DR PaxDb; Q8N0U8; -.
DR PeptideAtlas; Q8N0U8; -.
DR PRIDE; Q8N0U8; -.
DR ProteomicsDB; 18242; -.
DR ProteomicsDB; 71463; -. [Q8N0U8-1]
DR Antibodypedia; 57350; 98 antibodies from 17 providers.
DR DNASU; 154807; -.
DR Ensembl; ENST00000360768.5; ENSP00000353998.2; ENSG00000196715.7. [Q8N0U8-1]
DR Ensembl; ENST00000434382.2; ENSP00000403077.2; ENSG00000196715.7. [Q8N0U8-2]
DR Ensembl; ENST00000648179.1; ENSP00000497394.1; ENSG00000196715.7. [Q8N0U8-1]
DR GeneID; 154807; -.
DR KEGG; hsa:154807; -.
DR MANE-Select; ENST00000360768.5; ENSP00000353998.2; NM_173517.6; NP_775788.2.
DR UCSC; uc003tum.3; human. [Q8N0U8-1]
DR CTD; 154807; -.
DR DisGeNET; 154807; -.
DR GeneCards; VKORC1L1; -.
DR HGNC; HGNC:21492; VKORC1L1.
DR HPA; ENSG00000196715; Low tissue specificity.
DR MIM; 608838; gene.
DR neXtProt; NX_Q8N0U8; -.
DR OpenTargets; ENSG00000196715; -.
DR PharmGKB; PA134931578; -.
DR VEuPathDB; HostDB:ENSG00000196715; -.
DR GeneTree; ENSGT00940000157044; -.
DR HOGENOM; CLU_105471_0_0_1; -.
DR InParanoid; Q8N0U8; -.
DR OMA; CDISENI; -.
DR OrthoDB; 1351312at2759; -.
DR PhylomeDB; Q8N0U8; -.
DR TreeFam; TF328467; -.
DR BioCyc; MetaCyc:G66-30969-MON; -.
DR BRENDA; 1.17.4.4; 2681.
DR BRENDA; 1.17.4.5; 2681.
DR PathwayCommons; Q8N0U8; -.
DR Reactome; R-HSA-6806664; Metabolism of vitamin K.
DR SignaLink; Q8N0U8; -.
DR SIGNOR; Q8N0U8; -.
DR BioGRID-ORCS; 154807; 40 hits in 1070 CRISPR screens.
DR ChiTaRS; VKORC1L1; human.
DR GenomeRNAi; 154807; -.
DR Pharos; Q8N0U8; Tbio.
DR PRO; PR:Q8N0U8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8N0U8; protein.
DR Bgee; ENSG00000196715; Expressed in adipose tissue and 181 other tissues.
DR ExpressionAtlas; Q8N0U8; baseline and differential.
DR Genevisible; Q8N0U8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0047057; F:vitamin-K-epoxide reductase (warfarin-sensitive) activity; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; IMP:UniProtKB.
DR GO; GO:0042373; P:vitamin K metabolic process; IDA:UniProtKB.
DR CDD; cd12917; VKOR_euk; 1.
DR Gene3D; 1.20.1440.130; -; 1.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR038354; VKOR_sf.
DR InterPro; IPR042406; VKORC1/VKORC1L1.
DR PANTHER; PTHR14519; PTHR14519; 1.
DR Pfam; PF07884; VKOR; 1.
DR SMART; SM00756; VKc; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Membrane;
KW Oxidoreductase; Quinone; Redox-active center; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..176
FT /note="Vitamin K epoxide reductase complex subunit 1-like
FT protein 1"
FT /id="PRO_0000191671"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24532791"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..91
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24532791"
FT SITE 50
FT /note="Important for the reduction of the redox-active
FT cysteines"
FT /evidence="ECO:0000305"
FT SITE 58
FT /note="Important for the reduction of the redox-active
FT cysteines"
FT /evidence="ECO:0000305"
FT DISULFID 139..142
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT VAR_SEQ 66..176
FT /note="WGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALILMTSS
FT IMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLIINYKRLVYLNEAWKRQLQPKQD
FT -> HDSKRCGGFDPHDVLHHVGRGVPVPGLHSVLCAEGVLHHLHRHVRAELPSSHYQLQ
FT TTSLLERGLEAAAATQAGLTPDRLHPNSLKPLSIQFILQQVFIIIIIIIIHNRHFP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055709"
FT MUTAGEN 50
FT /note="C->S: Abolishes enzyme activity in cell-based
FT assays. Reduces enzyme activity moderately in assays that
FT regenerate the redox-active cysteines with dithiothreitol
FT (in vitro)."
FT /evidence="ECO:0000269|PubMed:24532791"
FT MUTAGEN 58
FT /note="C->S: Abolishes enzyme activity in cell-based
FT assays. Reduces enzyme activity moderately in assays that
FT regenerate the redox-active cysteines with dithiothreitol
FT (in vitro)."
FT /evidence="ECO:0000269|PubMed:24532791"
FT CONFLICT Q8N0U8-2:163
FT /note="F -> FI (in Ref. 2; BAG64984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 19836 MW; 1AB0FCDCC2B00E00 CRC64;
MAAPVLLRVS VPRWERVARY AVCAAGILLS IYAYHVEREK ERDPEHRALC DLGPWVKCSA
ALASRWGRGF GLLGSIFGKD GVLNQPNSVF GLIFYILQLL LGMTASAVAA LILMTSSIMS
VVGSLYLAYI LYFVLKEFCI ICIVTYVLNF LLLIINYKRL VYLNEAWKRQ LQPKQD
