ADHX_MOUSE
ID ADHX_MOUSE Reviewed; 374 AA.
AC P28474; Q3TW83; Q8C662;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Alcohol dehydrogenase class-3 {ECO:0000305};
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P11766};
DE AltName: Full=Alcohol dehydrogenase 2;
DE AltName: Full=Alcohol dehydrogenase 5;
DE AltName: Full=Alcohol dehydrogenase B2;
DE Short=ADH-B2;
DE AltName: Full=Alcohol dehydrogenase class-III;
DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE Short=FALDH;
DE Short=FDH;
DE Short=GSH-FDH;
DE EC=1.1.1.-;
DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE EC=1.1.1.284 {ECO:0000250|UniProtKB:P11766};
GN Name=Adh5 {ECO:0000312|MGI:MGI:87929}; Synonyms=Adh-2, Adh2;
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].
RX PubMed=2053480; DOI=10.1007/978-1-4684-5901-2_27;
RA Edenberg H.J., Brown C.J., Carr L.G., Ho W.H., Hur M.W.;
RT "Alcohol dehydrogenase gene expression and cloning of the mouse chi-like
RT ADH.";
RL Adv. Exp. Med. Biol. 284:253-262(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1472709; DOI=10.3109/10425179209034012;
RA Hur M.W., Ho W.H., Brown C.J., Goldman D., Edenberg H.J.;
RT "Molecular cloning of mouse alcohol dehydrogenase-B2 cDNA: nucleotide
RT sequences of the class III ADH genes evolve slowly even for silent
RT substitutions.";
RL DNA Seq. 3:167-175(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=8647091; DOI=10.1111/j.1432-1033.1996.0496k.x;
RA Foglio M.H., Duester G.;
RT "Characterization of the functional gene encoding mouse class III alcohol
RT dehydrogenase (glutathione-dependent formaldehyde dehydrogenase) and an
RT unexpressed processed pseudogene with an intact open reading frame.";
RL Eur. J. Biochem. 237:496-504(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [6]
RP PROTEIN SEQUENCE OF 234-248, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=FVB/N;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the oxidation of long-chain primary alcohols and
CC the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long
CC chain omega-hydroxy fatty acids, such as 20-HETE, producing both the
CC intermediate aldehyde, 20-oxoarachidonate and the end product, a
CC dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Class-III ADH
CC is remarkably ineffective in oxidizing ethanol.
CC {ECO:0000250|UniProtKB:P11766}.
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:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD(+) =
CC (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:39803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76645,
CC ChEBI:CHEBI:76647; Evidence={ECO:0000250|UniProtKB:P11766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39804;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD(+) = 20-
CC oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:39799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:76624, ChEBI:CHEBI:76645;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39800;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11766}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7738026}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
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DR EMBL; M84147; AAA68896.1; -; mRNA.
DR EMBL; U48970; AAC52763.1; -; Genomic_DNA.
DR EMBL; U48964; AAC52763.1; JOINED; Genomic_DNA.
DR EMBL; U48965; AAC52763.1; JOINED; Genomic_DNA.
DR EMBL; U48966; AAC52763.1; JOINED; Genomic_DNA.
DR EMBL; U48968; AAC52763.1; JOINED; Genomic_DNA.
DR EMBL; U48969; AAC52763.1; JOINED; Genomic_DNA.
DR EMBL; AK076507; BAC36370.1; -; mRNA.
DR EMBL; AK146949; BAE27558.1; -; mRNA.
DR EMBL; AK159803; BAE35383.1; -; mRNA.
DR EMBL; BC090978; AAH90978.1; -; mRNA.
DR CCDS; CCDS17868.1; -.
DR PIR; A56643; A56643.
DR RefSeq; NP_001275507.1; NM_001288578.1.
DR RefSeq; NP_031436.2; NM_007410.3.
DR AlphaFoldDB; P28474; -.
DR SMR; P28474; -.
DR BioGRID; 197986; 5.
DR STRING; 10090.ENSMUSP00000005964; -.
DR BindingDB; P28474; -.
DR ChEMBL; CHEMBL3341; -.
DR iPTMnet; P28474; -.
DR PhosphoSitePlus; P28474; -.
DR SwissPalm; P28474; -.
DR REPRODUCTION-2DPAGE; P28474; -.
DR EPD; P28474; -.
DR jPOST; P28474; -.
DR PaxDb; P28474; -.
DR PeptideAtlas; P28474; -.
DR PRIDE; P28474; -.
DR ProteomicsDB; 296110; -.
DR Antibodypedia; 25845; 450 antibodies from 37 providers.
DR DNASU; 11532; -.
DR Ensembl; ENSMUST00000005964; ENSMUSP00000005964; ENSMUSG00000028138.
DR GeneID; 11532; -.
DR KEGG; mmu:11532; -.
DR UCSC; uc008rnk.2; mouse.
DR CTD; 128; -.
DR MGI; MGI:87929; Adh5.
DR VEuPathDB; HostDB:ENSMUSG00000028138; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155196; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P28474; -.
DR OMA; IHHYMGT; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P28474; -.
DR TreeFam; TF300429; -.
DR Reactome; R-MMU-71384; Ethanol oxidation.
DR BioGRID-ORCS; 11532; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Adh5; mouse.
DR PRO; PR:P28474; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P28474; protein.
DR Bgee; ENSMUSG00000028138; Expressed in floor plate of midbrain and 275 other tissues.
DR ExpressionAtlas; P28474; baseline and differential.
DR Genevisible; P28474; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IMP:MGI.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:MGI.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR GO; GO:0010430; P:fatty acid omega-oxidation; ISS:UniProtKB.
DR GO; GO:0046294; P:formaldehyde catabolic process; IMP:MGI.
DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:MGI.
DR GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0051409; P:response to nitrosative stress; IMP:MGI.
DR GO; GO:0051775; P:response to redox state; ISO:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; IMP:MGI.
DR CDD; cd08300; alcohol_DH_class_III; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014183; ADH_3.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Lipid metabolism;
KW Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT CHAIN 2..374
FT /note="Alcohol dehydrogenase class-3"
FT /id="PRO_0000160760"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
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|UniProtKB:P11766"
FT SITE 115
FT /note="Important for FDH activity and activation by fatty
FT acids"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT MOD_RES 233
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT CONFLICT 55
FT /note="A -> R (in Ref. 1; no nucleotide entry, 2; AAA68896
FT and 3; AAC52763)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> R (in Ref. 4; BAE35383)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="A -> T (in Ref. 4; BAE35383)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="V -> I (in Ref. 4; BAE35383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 39548 MW; 32A3727B5DAB0919 CRC64;
MANQVIRCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIL ATAVCHTDAY TLSGADPEGC
FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK
GLMPDGTSRF TCKGKSVFHF MGTSTFSEYT VVADISVAKI DPSAPLDKVC LLGCGISTGY
GAAVNTAKVE PGSTCAVFGL GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGASEC
ISPQDFSKSI QEVLVEMTDG GVDYSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL SFDQINQAFD
LMHSGDSIRT VLKM
