ID   ADH7_MOUSE              Reviewed;         374 AA.
AC   Q64437;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH7 {ECO:0000305};
DE            EC=1.1.1.105 {ECO:0000250|UniProtKB:P40394};
DE   AltName: Full=ADH-C2;
DE   AltName: Full=Alcohol dehydrogenase 7;
DE   AltName: Full=Alcohol dehydrogenase class 4 mu/sigma chain;
DE            EC=1.1.1.1 {ECO:0000250|UniProtKB:P40394};
DE   AltName: Full=Alcohol dehydrogenase class IV mu/sigma chain;
DE   AltName: Full=Gastric alcohol dehydrogenase;
DE   AltName: Full=Omega-hydroxydecanoate dehydrogenase ADH7 {ECO:0000250|UniProtKB:P40394};
DE            EC=1.1.1.66 {ECO:0000250|UniProtKB:P40394};
DE   AltName: Full=Retinol dehydrogenase;
GN   Name=Adh7; Synonyms=Adh-3, Adh3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N; TISSUE=Gastric mucosa;
RX   PubMed=7738026; DOI=10.1074/jbc.270.18.10868;
RA   Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.;
RT   "Cloning of the mouse class IV alcohol dehydrogenase (retinol
RT   dehydrogenase) cDNA and tissue-specific expression patterns of the murine
RT   ADH gene family.";
RL   J. Biol. Chem. 270:10868-10877(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=9126489; DOI=10.1006/geno.1997.4637;
RA   Zgombic-Knight M., Deltour L., Haselbeck R.J., Foglio M.H., Duester G.;
RT   "Gene structure and promoter for Adh-3 encoding mouse class IV alcohol
RT   dehydrogenase (retinol dehydrogenase).";
RL   Genomics 41:105-109(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Catalyzes the NAD-dependent oxidation of all-trans-retinol,
CC       alcohol, aldehyde and omega-hydroxy fatty acids and their derivatives.
CC       Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol,
CC       9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such
CC       as juniperic acid. In vitro can also catalyzes the NADH-dependent
CC       reduction of all-trans-retinal and aldehydes and their derivatives.
CC       Reduces preferentially all trans-retinal, all-trans-4-oxoretinal and
CC       hexanal. Catalyzes in the oxidative direction with higher efficiency.
CC       Therefore may participate in retinoid metabolism, fatty acid omega-
CC       oxidation, and elimination of cytotoxic aldehydes produced by lipid
CC       peroxidation. {ECO:0000250|UniProtKB:P40394}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10737;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10738;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-hydroxydecanoate + NAD(+) = 10-oxodecanoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:20880, ChEBI:CHEBI:11305, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58022; EC=1.1.1.66;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20881;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH;
CC         Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH;
CC         Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42053;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-3,4-didehydroretinol + NAD(+) = all-trans-3,4-
CC         didehydroretinal + H(+) + NADH; Xref=Rhea:RHEA:55940,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28537, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132246;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55941;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-4-hydroxyretinol + NAD(+) = all-trans-4-
CC         hydroxyretinal + H(+) + NADH; Xref=Rhea:RHEA:55936,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132259, ChEBI:CHEBI:139346;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55937;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-4-oxoretinol + NAD(+) = all-trans-4-oxoretinal +
CC         H(+) + NADH; Xref=Rhea:RHEA:60632, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:44597, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:139347; Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60634;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-hydroxydodecanoate + NAD(+) = 12-oxododecanoate + H(+) +
CC         NADH; Xref=Rhea:RHEA:60980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36204,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144067;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60981;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16-hydroxyhexadecanoate + NAD(+) = 16-oxohexadecanoate + H(+)
CC         + NADH; Xref=Rhea:RHEA:60984, ChEBI:CHEBI:15378, ChEBI:CHEBI:55329,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144068;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60985;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexan-1-ol + NAD(+) = H(+) + hexanal + NADH;
CC         Xref=Rhea:RHEA:60972, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:87393, ChEBI:CHEBI:88528;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60973;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60974;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-hex-2-en-1-ol + NAD(+) = (E)-hex-2-enal + H(+) + NADH;
CC         Xref=Rhea:RHEA:60988, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:141205;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60989;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60990;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-hydroxynon-2-en-1-ol + NAD(+) = (E)-4-hydroxynon-2-enal
CC         + H(+) + NADH; Xref=Rhea:RHEA:60976, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58968,
CC         ChEBI:CHEBI:142617; Evidence={ECO:0000250|UniProtKB:P40394};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60978;
CC         Evidence={ECO:0000250|UniProtKB:P40394};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Retinol oxidation is inhibited by the detergent
CC       Tween 80. Ethanol inhibits both all-trans-retinol and 9-cis-retinol
CC       oxidation. 13-cis-retinol is an effective competitive inhibitor of the
CC       9-cis-retinol oxidation. All-trans-retinoic acid is a powerful
CC       inhibitor of all-trans-retinol oxidation. 13-cis-retinoic acid is a
CC       powerful inhibitor of all-trans-retinol oxidation. Cimetidine
CC       competitively inhibited ethanol oxidation.
CC       {ECO:0000250|UniProtKB:P40394}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: High expression in the stomach mucosa. Lower
CC       expression in eye, thymus, skin and ovary. Very low expression in small
CC       intestine, liver and uterus.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-IV subfamily. {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; U20257; AAA76735.1; -; mRNA.
DR   EMBL; U76734; AAC53124.1; -; Genomic_DNA.
DR   EMBL; U76728; AAC53124.1; JOINED; Genomic_DNA.
DR   EMBL; U76729; AAC53124.1; JOINED; Genomic_DNA.
DR   EMBL; U76730; AAC53124.1; JOINED; Genomic_DNA.
DR   EMBL; U76727; AAC53124.1; JOINED; Genomic_DNA.
DR   EMBL; U76731; AAC53124.1; JOINED; Genomic_DNA.
DR   EMBL; U76733; AAC53124.1; JOINED; Genomic_DNA.
DR   EMBL; U76732; AAC53124.1; JOINED; Genomic_DNA.
DR   EMBL; AC079682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS38651.1; -.
DR   PIR; A56436; A56436.
DR   RefSeq; NP_033756.2; NM_009626.4.
DR   RefSeq; XP_006500982.1; XM_006500919.3.
DR   AlphaFoldDB; Q64437; -.
DR   SMR; Q64437; -.
DR   STRING; 10090.ENSMUSP00000087633; -.
DR   iPTMnet; Q64437; -.
DR   PhosphoSitePlus; Q64437; -.
DR   SwissPalm; Q64437; -.
DR   jPOST; Q64437; -.
DR   PaxDb; 10090-ENSMUSP00000087633; -.
DR   PeptideAtlas; Q64437; -.
DR   ProteomicsDB; 296183; -.
DR   Pumba; Q64437; -.
DR   Antibodypedia; 25891; 396 antibodies from 31 providers.
DR   DNASU; 11529; -.
DR   Ensembl; ENSMUST00000090171.7; ENSMUSP00000087633.6; ENSMUSG00000055301.9.
DR   GeneID; 11529; -.
DR   KEGG; mmu:11529; -.
DR   UCSC; uc008rnd.2; mouse.
DR   AGR; MGI:87926; -.
DR   CTD; 131; -.
DR   MGI; MGI:87926; Adh7.
DR   VEuPathDB; HostDB:ENSMUSG00000055301; -.
DR   eggNOG; KOG0022; Eukaryota.
DR   GeneTree; ENSGT00940000162708; -.
DR   HOGENOM; CLU_026673_14_0_1; -.
DR   InParanoid; Q64437; -.
DR   OMA; IHATPRM; -.
DR   OrthoDB; 1077476at2759; -.
DR   PhylomeDB; Q64437; -.
DR   TreeFam; TF300429; -.
DR   Reactome; R-MMU-71384; Ethanol oxidation.
DR   BioGRID-ORCS; 11529; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Adh7; mouse.
DR   PRO; PR:Q64437; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q64437; Protein.
DR   Bgee; ENSMUSG00000055301; Expressed in esophagus and 103 other cell types or tissues.
DR   ExpressionAtlas; Q64437; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:MGI.
DR   GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; ISO:MGI.
DR   GO; GO:0004031; F:aldehyde oxidase activity; ISO:MGI.
DR   GO; GO:0035276; F:ethanol binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0051287; F:NAD binding; ISO:MGI.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:MGI.
DR   GO; GO:0050153; F:omega-hydroxydecanoate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; TAS:MGI.
DR   GO; GO:0048019; F:receptor antagonist activity; ISO:MGI.
DR   GO; GO:0019841; F:retinol binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0006068; P:ethanol catabolic process; IMP:MGI.
DR   GO; GO:0006067; P:ethanol metabolic process; ISO:MGI.
DR   GO; GO:0006069; P:ethanol oxidation; ISO:MGI.
DR   GO; GO:0010430; P:fatty acid omega-oxidation; ISO:MGI.
DR   GO; GO:0009617; P:response to bacterium; ISO:MGI.
DR   GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI.
DR   GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; IMP:MGI.
DR   CDD; cd08299; alcohol_DH_class_I_II_IV; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF2; ALL-TRANS-RETINOL DEHYDROGENASE [NAD(+)] ADH7; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
DR   Genevisible; Q64437; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lipid metabolism; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..374
FT                   /note="All-trans-retinol dehydrogenase [NAD(+)] ADH7"
FT                   /id="PRO_0000160692"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         292..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        120
FT                   /note="R -> C (in Ref. 1; AAA76735 and 2; AAC53124)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="I -> V (in Ref. 1; AAA76735 and 2; AAC53124)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  39904 MW;  D615119A23B41843 CRC64;
     MGTAGKVIKC KAAVLWGVNQ PFSIEEIEVA PPKAKEVRVK ILATGICRTD DHIIKGSMVS
     KFPVIVGHEA VGVVESVGEG VTTVRPGDKV IPLFLPQCRE CNACLNPEGN LCIRSDLTGR
     GVLADGTTRF TCKGKPVQHF MNTSTFTEYT VLDESSVAKV DGAAPPEKAC LIGCGFSTGY
     GAAVKTAKVT PGSTCVVFGL GGVGLSVIMG CKAAGASRII GIDINKDKFQ KALAVGATEC
     ISPKDSTKPI SEVLSDMTGN TIQYTFEVIG RLETMVDALS SCHMNYGTSV VVGAPPSAKM
     LTYDPMLLFT GRTWKGCVFG GWKSRDDVPK LVTEFLEKKF DLDQLITHTL PFNNINEGFE
     LLYSGKSIRT VLTF
//