ARK72_MOUSE
ID ARK72_MOUSE Reviewed; 367 AA.
AC Q8CG76; A2AMV3; Q3UPU2; Q8CG77; Q8JZQ8; Q9D157;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Aflatoxin B1 aldehyde reductase member 2;
DE EC=1.1.1.n11;
DE AltName: Full=Succinic semialdehyde reductase;
DE Short=SSA reductase;
GN Name=Akr7a2 {ECO:0000250|UniProtKB:O43488};
GN Synonyms=Afar {ECO:0000312|MGI:MGI:107796},
GN Akr7a5 {ECO:0000312|MGI:MGI:107796};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [2]
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).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH31857.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-367.
RC STRAIN=FVB/N; TISSUE=Liver {ECO:0000312|EMBL:AAH31857.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:CAC81078.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-367.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:CAC81078.1};
RX PubMed=12879023; DOI=10.1038/sj.onc.1206684;
RA Praml C., Savelyeva L., Schwab M.;
RT "Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a
RT region frequently altered in human tumour cells.";
RL Oncogene 22:4765-4773(2003).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-367, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Liver;
RX PubMed=12123834; DOI=10.1016/s0014-5793(02)02982-4;
RA Hinshelwood A., McGarvie G., Ellis E.;
RT "Characterisation of a novel mouse liver aldo-keto reductase AKR7A5.";
RL FEBS Lett. 523:213-218(2002).
RN [6] {ECO:0000305}
RP SEQUENCE REVISION TO 127 AND 162.
RA Ellis E.M., Hinshelwood A., McGarvie G.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305, ECO:0000312|EMBL:DAA00087.1}
RP GENE STRUCTURE.
RX PubMed=12071861; DOI=10.1042/bj20020342;
RA Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D.;
RT "Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases
RT that associate with the Golgi apparatus define a distinct subclass of aldo-
RT keto reductase 7 family proteins.";
RL Biochem. J. 366:847-861(2002).
RN [8]
RP IDENTIFICATION BY 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-40 AND THR-48, AND
RP IDENTIFICATION BY 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-244, AND IDENTIFICATION BY MASS
RP 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-367 IN COMPLEX WITH NADP AND
RP THE INHIBITOR TARTRATE, ACTIVITY REGULATION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBUNIT.
RX PubMed=16460003; DOI=10.1021/bi051610k;
RA Zhu X., Lapthorn A.J., Ellis E.M.;
RT "Crystal structure of mouse succinic semialdehyde reductase AKR7A5:
RT structural basis for substrate specificity.";
RL Biochemistry 45:1562-1570(2006).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of succinic
CC semialdehyde to gamma-hydroxybutyrate. May have an important role in
CC producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad
CC substrate specificity. Can reduce the dialdehyde protein-binding form
CC of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be
CC involved in protection of liver against the toxic and carcinogenic
CC effects of AFB1, a potent hepatocarcinogen (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:16460003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybutanoate + NADP(+) = H(+) + NADPH + succinate
CC semialdehyde; Xref=Rhea:RHEA:26381, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16724, ChEBI:CHEBI:57706, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.n11;
CC Evidence={ECO:0000269|PubMed:16460003};
CC -!- ACTIVITY REGULATION: Inhibited by citrate, succinate and tartrate.
CC {ECO:0000269|PubMed:16460003}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.8 uM for succinic semialdehyde {ECO:0000269|PubMed:16460003};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16460003}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, testis and brain with
CC low levels in skeletal muscle, spleen, heart and lung.
CC {ECO:0000269|PubMed:12123834}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31857.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC81077.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC81078.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK143203; BAE25302.1; -; mRNA.
DR EMBL; AL807811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031857; AAH31857.1; ALT_INIT; mRNA.
DR EMBL; AJ271800; CAC81077.1; ALT_INIT; mRNA.
DR EMBL; AJ271801; CAC81078.1; ALT_INIT; mRNA.
DR EMBL; AF525358; AAO38437.2; -; mRNA.
DR EMBL; BK000393; DAA00087.1; -; mRNA.
DR CCDS; CCDS18844.1; -.
DR RefSeq; NP_079613.3; NM_025337.3.
DR PDB; 2C91; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J=30-367.
DR PDBsum; 2C91; -.
DR AlphaFoldDB; Q8CG76; -.
DR SMR; Q8CG76; -.
DR BioGRID; 225379; 3.
DR IntAct; Q8CG76; 1.
DR STRING; 10090.ENSMUSP00000073459; -.
DR iPTMnet; Q8CG76; -.
DR PhosphoSitePlus; Q8CG76; -.
DR SwissPalm; Q8CG76; -.
DR REPRODUCTION-2DPAGE; Q8CG76; -.
DR EPD; Q8CG76; -.
DR jPOST; Q8CG76; -.
DR MaxQB; Q8CG76; -.
DR PaxDb; Q8CG76; -.
DR PeptideAtlas; Q8CG76; -.
DR PRIDE; Q8CG76; -.
DR ProteomicsDB; 265100; -.
DR DNASU; 110198; -.
DR Ensembl; ENSMUST00000073787; ENSMUSP00000073459; ENSMUSG00000028743.
DR GeneID; 110198; -.
DR KEGG; mmu:110198; -.
DR UCSC; uc008vmc.2; mouse.
DR CTD; 110198; -.
DR MGI; MGI:107796; Akr7a5.
DR VEuPathDB; HostDB:ENSMUSG00000028743; -.
DR eggNOG; ENOG502QU2T; Eukaryota.
DR GeneTree; ENSGT00940000158496; -.
DR HOGENOM; CLU_023205_1_1_1; -.
DR InParanoid; Q8CG76; -.
DR OMA; TARMYVG; -.
DR OrthoDB; 1226539at2759; -.
DR PhylomeDB; Q8CG76; -.
DR TreeFam; TF329173; -.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR SABIO-RK; Q8CG76; -.
DR BioGRID-ORCS; 110198; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Akr7a5; mouse.
DR EvolutionaryTrace; Q8CG76; -.
DR PRO; PR:Q8CG76; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CG76; protein.
DR Bgee; ENSMUSG00000028743; Expressed in right kidney and 255 other tissues.
DR Genevisible; Q8CG76; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; ISO:MGI.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019119; F:phenanthrene-9,10-epoxide hydrolase activity; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Golgi apparatus; Lipid metabolism;
KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..367
FT /note="Aflatoxin B1 aldehyde reductase member 2"
FT /id="PRO_0000070376"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 179..180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 234..244
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 326..334
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16460003"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16460003"
FT SITE 113
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O43488"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 244
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 5
FT /note="A -> G (in Ref. 1; BAE25302)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="V -> G (in Ref. 1; BAE25302)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; BAE25302)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="A -> G (in Ref. 1; BAE25302)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="I -> V (in Ref. 3; AAH31857 and 4; CAC81078)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="R -> C (in Ref. 5; AAO38437)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="A -> G (in Ref. 3; AAH31857)"
FT /evidence="ECO:0000305"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2C91"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2C91"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:2C91"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 275..292
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2C91"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 345..358
FT /evidence="ECO:0007829|PDB:2C91"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:2C91"
SQ SEQUENCE 367 AA; 40612 MW; 1123BD7028D3FBDF CRC64;
MLRAASRAVG RAAVRSAQRS GTSVGRPLAM SRPPPPRAAS GAPLRPATVL GTMEMGRRMD
ASASAASVRA FLERGHSELD TAFMYCDGQS ENILGGLGLG LGSGDCTVKI ATKANPWEGK
SLKPDSIRSQ LETSLKRLQC PRVDLFYLHA PDHSTPVEET LRACHQLHQE GKFVELGLSN
YASWEVAEIC TLCKSNGWIL PTVYQGMYNA TTRQVEAELL PCLRHFGLRF YAYNPLAGGL
LTGKYKYEDK DGKQPVGRFF GNNWAETYRN RFWKEHHFEA IALVEKALQT TYGTNAPRMT
SAALRWMYHH SQLQGTRGDA VILGMSSLEQ LEQNLAATEE GPLEPAVVEA FDQAWNMVAH
ECPNYFR
