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GSTO2_HUMAN
ID   GSTO2_HUMAN             Reviewed;         243 AA.
AC   Q9H4Y5; A8K771; B4DJW6; E7ESD6; Q49TW5; Q5GM70; Q5JU15; Q86WP3;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Glutathione S-transferase omega-2;
DE            Short=GSTO-2;
DE            EC=2.5.1.18 {ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127};
DE   AltName: Full=Glutathione S-transferase omega 2-2;
DE            Short=GSTO 2-2;
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE            EC=1.8.5.1 {ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127};
DE   AltName: Full=Monomethylarsonic acid reductase;
DE            Short=MMA(V) reductase;
DE            EC=1.20.4.2 {ECO:0000269|PubMed:15970797};
GN   Name=GSTO2;
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).
RA   Wang L., Xie Y., Mao Y.;
RT   "Cloning and characterization of human GSTO-2 gene.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Xu J., Xie Y., Mao Y.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skeletal muscle, and Thalamus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and Pancreatic carcinoma;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-243 (ISOFORM 1), VARIANT ASP-142, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=12618591; DOI=10.1097/01.fpc.0000054062.98065.6e;
RA   Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.;
RT   "Characterization of the human Omega class glutathione transferase genes
RT   and associated polymorphisms.";
RL   Pharmacogenetics 13:131-144(2003).
RN   [8]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX   PubMed=15970797; DOI=10.1097/01.fpc.0000165725.81559.e3;
RA   Schmuck E.M., Board P.G., Whitbread A.K., Tetlow N., Cavanaugh J.A.,
RA   Blackburn A.C., Masoumi A.;
RT   "Characterization of the monomethylarsonate reductase and dehydroascorbate
RT   reductase activities of Omega class glutathione transferase variants:
RT   implications for arsenic metabolism and the age-at-onset of Alzheimer's and
RT   Parkinson's diseases.";
RL   Pharmacogenet. Genomics 15:493-501(2005).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-239 ALONE AND IN COMPLEX WITH
RP   GLUTATHIONE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-34.
RX   PubMed=22522127; DOI=10.1016/j.jmb.2012.04.014;
RA   Zhou H., Brock J., Liu D., Board P.G., Oakley A.J.;
RT   "Structural insights into the dehydroascorbate reductase activity of human
RT   omega-class glutathione transferases.";
RL   J. Mol. Biol. 420:190-203(2012).
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity.
CC       Has high dehydroascorbate reductase activity and may contribute to the
CC       recycling of ascorbic acid. Participates in the biotransformation of
CC       inorganic arsenic and reduces monomethylarsonic acid (MMA).
CC       {ECO:0000269|PubMed:15970797}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC         + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC         Evidence={ECO:0000269|PubMed:15970797};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:15970797};
CC   -!- INTERACTION:
CC       Q9H4Y5; P28676: GCA; NbExp=3; IntAct=EBI-10194609, EBI-947242;
CC       Q9H4Y5; Q9H4Y5: GSTO2; NbExp=8; IntAct=EBI-10194609, EBI-10194609;
CC       Q9H4Y5; P31273: HOXC8; NbExp=3; IntAct=EBI-10194609, EBI-1752118;
CC       Q9H4Y5; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10194609, EBI-6509505;
CC       Q9H4Y5; Q6JEL2: KLHL10; NbExp=3; IntAct=EBI-10194609, EBI-6426253;
CC       Q9H4Y5; Q9H6H2: MUM1; NbExp=3; IntAct=EBI-10194609, EBI-10307610;
CC       Q9H4Y5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10194609, EBI-741158;
CC       Q9H4Y5; Q99471: PFDN5; NbExp=3; IntAct=EBI-10194609, EBI-357275;
CC       Q9H4Y5; O15160: POLR1C; NbExp=3; IntAct=EBI-10194609, EBI-1055079;
CC       Q9H4Y5; Q92922: SMARCC1; NbExp=3; IntAct=EBI-10194609, EBI-355653;
CC       Q9H4Y5; P05549: TFAP2A; NbExp=4; IntAct=EBI-10194609, EBI-347351;
CC       Q9H4Y5; P05549-5: TFAP2A; NbExp=6; IntAct=EBI-10194609, EBI-12194905;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9H4Y5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H4Y5-2; Sequence=VSP_042567;
CC       Name=3;
CC         IsoId=Q9H4Y5-3; Sequence=VSP_045267;
CC   -!- TISSUE SPECIFICITY: Expressed in a range of tissues, including the
CC       liver, kidney, skeletal muscle and prostate. Strongest expression in
CC       the testis. {ECO:0000269|PubMed:12618591}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
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DR   EMBL; AY350731; AAR02452.1; -; mRNA.
DR   EMBL; AY209189; AAP47743.1; -; mRNA.
DR   EMBL; AK291886; BAF84575.1; -; mRNA.
DR   EMBL; AK296266; BAG58978.1; -; mRNA.
DR   EMBL; AL139341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL162742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49600.1; -; Genomic_DNA.
DR   EMBL; BC046194; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC056918; AAH56918.1; -; mRNA.
DR   EMBL; AY191318; AAO23573.1; -; mRNA.
DR   CCDS; CCDS53574.1; -. [Q9H4Y5-2]
DR   CCDS; CCDS53575.1; -. [Q9H4Y5-3]
DR   CCDS; CCDS7556.1; -. [Q9H4Y5-1]
DR   RefSeq; NP_001177942.1; NM_001191013.1. [Q9H4Y5-2]
DR   RefSeq; NP_001177943.1; NM_001191014.1. [Q9H4Y5-3]
DR   RefSeq; NP_001177944.1; NM_001191015.1.
DR   RefSeq; NP_899062.1; NM_183239.1. [Q9H4Y5-1]
DR   RefSeq; XP_011537572.1; XM_011539270.2. [Q9H4Y5-1]
DR   PDB; 3Q18; X-ray; 1.70 A; A/B=1-239.
DR   PDB; 3Q19; X-ray; 1.90 A; A/B=1-239.
DR   PDB; 3QAG; X-ray; 2.00 A; A=1-239.
DR   PDBsum; 3Q18; -.
DR   PDBsum; 3Q19; -.
DR   PDBsum; 3QAG; -.
DR   AlphaFoldDB; Q9H4Y5; -.
DR   SMR; Q9H4Y5; -.
DR   BioGRID; 125638; 27.
DR   IntAct; Q9H4Y5; 15.
DR   STRING; 9606.ENSP00000345023; -.
DR   ChEMBL; CHEMBL2161; -.
DR   DrugBank; DB00143; Glutathione.
DR   iPTMnet; Q9H4Y5; -.
DR   PhosphoSitePlus; Q9H4Y5; -.
DR   BioMuta; GSTO2; -.
DR   DMDM; 34922124; -.
DR   MassIVE; Q9H4Y5; -.
DR   PaxDb; Q9H4Y5; -.
DR   PeptideAtlas; Q9H4Y5; -.
DR   PRIDE; Q9H4Y5; -.
DR   ProteomicsDB; 63249; -.
DR   ProteomicsDB; 80881; -. [Q9H4Y5-1]
DR   ProteomicsDB; 80882; -. [Q9H4Y5-2]
DR   Antibodypedia; 31611; 316 antibodies from 29 providers.
DR   DNASU; 119391; -.
DR   Ensembl; ENST00000338595.7; ENSP00000345023.1; ENSG00000065621.15. [Q9H4Y5-1]
DR   Ensembl; ENST00000369707.2; ENSP00000358721.1; ENSG00000065621.15. [Q9H4Y5-3]
DR   Ensembl; ENST00000450629.6; ENSP00000390986.2; ENSG00000065621.15. [Q9H4Y5-2]
DR   GeneID; 119391; -.
DR   KEGG; hsa:119391; -.
DR   MANE-Select; ENST00000338595.7; ENSP00000345023.1; NM_183239.2; NP_899062.1.
DR   UCSC; uc001kyb.4; human. [Q9H4Y5-1]
DR   CTD; 119391; -.
DR   DisGeNET; 119391; -.
DR   GeneCards; GSTO2; -.
DR   HGNC; HGNC:23064; GSTO2.
DR   HPA; ENSG00000065621; Tissue enhanced (testis).
DR   MIM; 612314; gene.
DR   neXtProt; NX_Q9H4Y5; -.
DR   OpenTargets; ENSG00000065621; -.
DR   PharmGKB; PA133787053; -.
DR   VEuPathDB; HostDB:ENSG00000065621; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   GeneTree; ENSGT00940000162030; -.
DR   HOGENOM; CLU_011226_9_2_1; -.
DR   InParanoid; Q9H4Y5; -.
DR   OMA; ESMVICE; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q9H4Y5; -.
DR   TreeFam; TF105325; -.
DR   BRENDA; 1.8.5.1; 2681.
DR   BRENDA; 2.5.1.18; 2681.
DR   PathwayCommons; Q9H4Y5; -.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
DR   SignaLink; Q9H4Y5; -.
DR   BioGRID-ORCS; 119391; 12 hits in 1074 CRISPR screens.
DR   ChiTaRS; GSTO2; human.
DR   GeneWiki; GSTO2; -.
DR   GenomeRNAi; 119391; -.
DR   Pharos; Q9H4Y5; Tbio.
DR   PRO; PR:Q9H4Y5; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9H4Y5; protein.
DR   Bgee; ENSG00000065621; Expressed in body of pancreas and 147 other tissues.
DR   Genevisible; Q9H4Y5; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Oxidoreductase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..243
FT                   /note="Glutathione S-transferase omega-2"
FT                   /id="PRO_0000185888"
FT   DOMAIN          22..101
FT                   /note="GST N-terminal"
FT   DOMAIN          106..231
FT                   /note="GST C-terminal"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT   BINDING         59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:22522127"
FT   BINDING         72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:22522127"
FT   BINDING         85..86
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:22522127"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045267"
FT   VAR_SEQ         123..156
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042567"
FT   VARIANT         130
FT                   /note="C -> Y (in dbSNP:rs45582439)"
FT                   /id="VAR_049492"
FT   VARIANT         142
FT                   /note="N -> D (in dbSNP:rs156697)"
FT                   /evidence="ECO:0000269|PubMed:12618591"
FT                   /id="VAR_016812"
FT   MUTAGEN         34
FT                   /note="Y->A: Abolishes DHAR activity."
FT                   /evidence="ECO:0000269|PubMed:22522127"
FT   CONFLICT        215
FT                   /note="A -> V (in Ref. 2; AAP47743)"
FT                   /evidence="ECO:0000305"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           33..44
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           61..65
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:3QAG"
FT   HELIX           86..96
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           107..119
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           123..136
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           141..161
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           173..183
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           185..188
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           191..194
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           198..208
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           211..216
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           220..231
FT                   /evidence="ECO:0007829|PDB:3Q18"
FT   HELIX           235..238
FT                   /evidence="ECO:0007829|PDB:3Q18"
SQ   SEQUENCE   243 AA;  28254 MW;  45A959432BCF490A CRC64;
     MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE VVNINLRNKP
     EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR KLFPYDPYER ARQKMLLELF
     CKVPHLTKEC LVALRCGREC TNLKAALRQE FSNLEEILEY QNTTFFGGTC ISMIDYLLWP
     WFERLDVYGI LDCVSHTPAL RLWISAMKWD PTVCALLMDK SIFQGFLNLY FQNNPNAFDF
     GLC
 
 
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