DHRS2_HUMAN
ID DHRS2_HUMAN Reviewed; 280 AA.
AC Q13268; D3DS54; Q53GS4; Q7Z789; Q9H2R2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Dehydrogenase/reductase SDR family member 2, mitochondrial {ECO:0000303|PubMed:19027726};
DE EC=1.1.1.- {ECO:0000269|PubMed:16685466};
DE AltName: Full=Dicarbonyl reductase HEP27 {ECO:0000303|PubMed:7556196};
DE AltName: Full=Protein D;
DE AltName: Full=Short chain dehydrogenase/reductase family 25C member 1 {ECO:0000303|PubMed:19027726};
DE Short=Protein SDR25C1 {ECO:0000303|PubMed:19027726};
DE Flags: Precursor;
GN Name=DHRS2 {ECO:0000312|HGNC:HGNC:18349}; Synonyms=SDR25C1;
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), AND PROTEIN SEQUENCE OF 24-41.
RC TISSUE=Hepatoma;
RX PubMed=7556196; DOI=10.1111/j.1432-1033.1995.473zz.x;
RA Gabrielli F., Donadel G., Bensi G., Heguy A., Melli M.;
RT "A nuclear protein, synthesized in growth-arrested human hepatoblastoma
RT cells, is a novel member of the short-chain alcohol dehydrogenase family.";
RL Eur. J. Biochem. 232:473-477(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=11997086; DOI=10.1016/s0167-4781(01)00323-2;
RA Pellegrini S., Censini S., Guidotti S., Iacopetti P., Rocchi M.,
RA Bianchi M., Covacci A., Gabrielli F.;
RT "A human short-chain dehydrogenase/reductase gene: structure, chromosomal
RT localization, tissue expression and subcellular localization of its
RT product.";
RL Biochim. Biophys. Acta 1574:215-222(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 10-280 (ISOFORM 1).
RC TISSUE=Skin;
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 PROTEIN SEQUENCE OF 80-88; 141-146; 148-162 AND 198-205, AND SUBCELLULAR
RP LOCATION.
RX PubMed=1847869; DOI=10.1111/j.1432-1033.1991.tb15759.x;
RA Donadel G., Garzelli C., Frank R., Gabrielli F.;
RT "Identification of a novel nuclear protein synthesized in growth-arrested
RT human hepatoblastoma HepG2 cells.";
RL Eur. J. Biochem. 195:723-729(1991).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11944995; DOI=10.1006/geno.2002.6743;
RA Heinz S., Krause S.W., Gabrielli F., Wagner H.M., Andreesen R., Rehli M.;
RT "Genomic organization of the human gene HEP27: alternative promoter usage
RT in HepG2 cells and monocyte-derived dendritic cells.";
RL Genomics 79:608-615(2002).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16685466; DOI=10.1007/s00018-006-6013-y;
RA Shafqat N., Shafqat J., Eissner G., Marschall H.U., Tryggvason K.,
RA Eriksson U., Gabrielli F., Lardy H., Jornvall H., Oppermann U.;
RT "Hep27, a member of the short-chain dehydrogenase/reductase family, is an
RT NADPH-dependent dicarbonyl reductase expressed in vascular endothelial
RT tissue.";
RL Cell. Mol. Life Sci. 63:1205-1213(2006).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
RN [11]
RP FUNCTION, INTERACTION WITH MDM2, IDENTIFICATION OF MITOCHONDRIAL TRANSIT
RP PEPTIDE CLEAVAGE SITE, AND SUBCELLULAR LOCATION.
RX PubMed=20547751; DOI=10.1128/mcb.01284-09;
RA Deisenroth C., Thorner A.R., Enomoto T., Perou C.M., Zhang Y.;
RT "Mitochondrial Hep27 is a c-Myb target gene that inhibits Mdm2 and
RT stabilizes p53.";
RL Mol. Cell. Biol. 30:3981-3993(2010).
RN [12]
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 [13]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-272.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP FUNCTION.
RX PubMed=29106393; DOI=10.1038/onc.2017.383;
RA Zhou Y., Wang L., Ban X., Zeng T., Zhu Y., Li M., Guan X.Y., Li Y.;
RT "DHRS2 inhibits cell growth and motility in esophageal squamous cell
RT carcinoma.";
RL Oncogene 37:1086-1094(2018).
CC -!- FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction
CC of dicarbonyl compounds. Displays reductase activity in vitro with 3,4-
CC hexanedione, 2,3-heptanedione and 1-phenyl-1,2-propanedione as
CC substrates (PubMed:16685466). May function as a dicarbonyl reductase in
CC the enzymatic inactivation of reactive carbonyls involved in covalent
CC modification of cellular components (PubMed:16685466). Also displays a
CC minor hydroxysteroid dehydrogenase activity toward bile acids such as
CC ursodeoxycholic acid (UDCA) and isoursodeoxycholic acid (isoUDCA),
CC which makes it unlikely to control hormone levels (PubMed:16685466).
CC Doesn't show any activity in vitro with retinoids and sugars as
CC substrates (PubMed:16685466). Attenuates MDM2-mediated p53/TP53
CC degradation, leading to p53/TP53 stabilization and increased
CC transcription activity, resulting in the accumulation of MDM2 and
CC CDKN1A/p21 (PubMed:20547751). Reduces proliferation, migration and
CC invasion of cancer cells and well as the production of ROS in cancer
CC (PubMed:29106393). {ECO:0000269|PubMed:16685466,
CC ECO:0000269|PubMed:20547751, ECO:0000269|PubMed:29106393}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for 1-phenyl-1,2-propanedione
CC {ECO:0000269|PubMed:16685466};
CC KM=1.1 mM for 2,3-heptanedione {ECO:0000269|PubMed:16685466};
CC KM=0.8 mM for 3,4-hexanedione {ECO:0000269|PubMed:16685466};
CC Note=kcat is 15.2 min(-1) with 1-phenyl-1,2-propanedione as
CC substrate. kcat is 40.0 min(-1) with 2,3-heptanedione as substrate.
CC kcat is 11.7 min(-1) with 3,4-hexanedione as substrate.;
CC -!- SUBUNIT: Directly interacts with MDM2; this interaction occurs in the
CC nucleus and does not target DHRS2 to degradation.
CC {ECO:0000269|PubMed:20547751}.
CC -!- INTERACTION:
CC Q13268; Q92624: APPBP2; NbExp=3; IntAct=EBI-354324, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Nucleus. Note=A minor
CC fraction of the protein is translocated from the mitochondria to the
CC nucleus, after cleavage of the targeting signal.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13268-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13268-2; Sequence=VSP_038179;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in liver and
CC kidney, followed by heart, spleen, skeletal muscle and placenta. In
CC hemopoietic cells, expressed in dendritic cells, but not in monocytes,
CC macrophages, granulocytes, nor in B and T lymphocytes.
CC {ECO:0000269|PubMed:11944995}.
CC -!- INDUCTION: Up-regulated by IL4 and CSF2 in monocytes/macrophages. Down-
CC regulated by bacterial lipopolysaccharides (LPS) and TNF in monocytice-
CC derived dendritic cells. Up-regulated by MYB.
CC {ECO:0000269|PubMed:11944995}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U31875; AAA82048.1; -; mRNA.
DR EMBL; AF244132; AAG33703.1; -; Genomic_DNA.
DR EMBL; AK222857; BAD96577.1; -; mRNA.
DR EMBL; AL135999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66130.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66131.1; -; Genomic_DNA.
DR EMBL; BC002786; AAH02786.1; -; mRNA.
DR EMBL; BC007339; AAH07339.2; -; mRNA.
DR CCDS; CCDS41927.1; -. [Q13268-2]
DR CCDS; CCDS9604.1; -. [Q13268-1]
DR PIR; S66665; S66665.
DR RefSeq; NP_005785.1; NM_005794.3. [Q13268-1]
DR RefSeq; NP_878912.1; NM_182908.4. [Q13268-2]
DR RefSeq; XP_005267306.1; XM_005267249.1. [Q13268-1]
DR RefSeq; XP_006720064.1; XM_006720001.3. [Q13268-1]
DR AlphaFoldDB; Q13268; -.
DR SMR; Q13268; -.
DR BioGRID; 115497; 84.
DR IntAct; Q13268; 49.
DR STRING; 9606.ENSP00000344674; -.
DR iPTMnet; Q13268; -.
DR PhosphoSitePlus; Q13268; -.
DR BioMuta; DHRS2; -.
DR DMDM; 527504085; -.
DR EPD; Q13268; -.
DR jPOST; Q13268; -.
DR MassIVE; Q13268; -.
DR MaxQB; Q13268; -.
DR PaxDb; Q13268; -.
DR PeptideAtlas; Q13268; -.
DR PRIDE; Q13268; -.
DR ProteomicsDB; 59268; -. [Q13268-1]
DR ProteomicsDB; 59269; -. [Q13268-2]
DR Antibodypedia; 22541; 289 antibodies from 28 providers.
DR DNASU; 10202; -.
DR Ensembl; ENST00000250383.11; ENSP00000250383.7; ENSG00000100867.15. [Q13268-1]
DR Ensembl; ENST00000344777.11; ENSP00000344674.7; ENSG00000100867.15. [Q13268-2]
DR Ensembl; ENST00000611765.4; ENSP00000481607.1; ENSG00000100867.15. [Q13268-2]
DR GeneID; 10202; -.
DR KEGG; hsa:10202; -.
DR MANE-Select; ENST00000250383.11; ENSP00000250383.7; NM_005794.4; NP_005785.1.
DR UCSC; uc001wkt.5; human. [Q13268-1]
DR CTD; 10202; -.
DR DisGeNET; 10202; -.
DR GeneCards; DHRS2; -.
DR HGNC; HGNC:18349; DHRS2.
DR HPA; ENSG00000100867; Tissue enhanced (breast, urinary bladder).
DR MIM; 615194; gene.
DR neXtProt; NX_Q13268; -.
DR OpenTargets; ENSG00000100867; -.
DR PharmGKB; PA38318; -.
DR VEuPathDB; HostDB:ENSG00000100867; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000162664; -.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q13268; -.
DR OMA; NISSMWG; -.
DR OrthoDB; 1194344at2759; -.
DR TreeFam; TF315405; -.
DR PathwayCommons; Q13268; -.
DR SABIO-RK; Q13268; -.
DR SignaLink; Q13268; -.
DR BioGRID-ORCS; 10202; 9 hits in 1084 CRISPR screens.
DR ChiTaRS; DHRS2; human.
DR GeneWiki; DHRS2; -.
DR GenomeRNAi; 10202; -.
DR Pharos; Q13268; Tbio.
DR PRO; PR:Q13268; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q13268; protein.
DR Bgee; ENSG00000100867; Expressed in mucosa of urinary bladder and 126 other tissues.
DR ExpressionAtlas; Q13268; baseline and differential.
DR Genevisible; Q13268; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0008207; P:C21-steroid hormone metabolic process; NAS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR InterPro; IPR027052; DHRS2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43943:SF3; PTHR43943:SF3; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW Mitochondrion; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7556196"
FT CHAIN 24..280
FT /note="Dehydrogenase/reductase SDR family member 2,
FT mitochondrial"
FT /id="PRO_0000054642"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT MOD_RES 96
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 96
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 219
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 219
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 237
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT VAR_SEQ 226..280
FT /note="FHGNESLWKNFKEHHQLQRIGESEDCAGIVSFLCSPDASYVNGENIAVAGYS
FT TRL -> VRIGFMGMSLSGRTSRNIISCRGLGSQRTVQESCPSCALQMPATSTGRTLRW
FT QATPLGSERSGGGCVAVVPGPGA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038179"
FT VARIANT 272
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs148991912)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035846"
FT CONFLICT 14
FT /note="H -> R (in Ref. 3; BAD96577)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="L -> V (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="L -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="L -> P (in Ref. 3; BAD96577)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="I -> V (in Ref. 3; BAD96577)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="N -> S (in Ref. 3; BAD96577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 29927 MW; FE76ED9CB28AB95C CRC64;
MLSAVARGYQ GWFHPCARLS VRMSSTGIDR KGVLANRVAV VTGSTSGIGF AIARRLARDG
AHVVISSRKQ QNVDRAMAKL QGEGLSVAGI VCHVGKAEDR EQLVAKALEH CGGVDFLVCS
AGVNPLVGST LGTSEQIWDK ILSVNVKSPA LLLSQLLPYM ENRRGAVILV SSIAAYNPVV
ALGVYNVSKT ALLGLTRTLA LELAPKDIRV NCVVPGIIKT DFSKVFHGNE SLWKNFKEHH
QLQRIGESED CAGIVSFLCS PDASYVNGEN IAVAGYSTRL
