AK1C3_PONAB
ID AK1C3_PONAB Reviewed; 323 AA.
AC Q5R7C9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Aldo-keto reductase family 1 member C3;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P42330};
DE EC=1.1.1.210 {ECO:0000250|UniProtKB:P42330};
DE EC=1.1.1.53 {ECO:0000250|UniProtKB:P42330};
DE EC=1.1.1.62 {ECO:0000250|UniProtKB:P42330};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase type 5;
DE Short=17-beta-HSD 5;
DE AltName: Full=3-alpha-HSD type II, brain;
DE AltName: Full=3-alpha-hydroxysteroid dehydrogenase type 2;
DE Short=3-alpha-HSD type 2;
DE EC=1.1.1.357 {ECO:0000250|UniProtKB:P42330};
DE AltName: Full=Chlordecone reductase homolog HAKRb;
DE AltName: Full=Dihydrodiol dehydrogenase 3;
DE Short=DD-3;
DE Short=DD3;
DE AltName: Full=Dihydrodiol dehydrogenase type I;
DE AltName: Full=HA1753;
DE AltName: Full=Prostaglandin F synthase;
DE Short=PGFS;
DE EC=1.1.1.188 {ECO:0000250|UniProtKB:P42330};
DE AltName: Full=Testosterone 17-beta-dehydrogenase 5;
DE EC=1.1.1.239 {ECO:0000250|UniProtKB:P42330};
DE EC=1.1.1.64 {ECO:0000250|UniProtKB:P42330};
GN Name=AKR1C3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytosolic aldo-keto reductase that catalyzes the NADH and
CC NADPH-dependent reduction of ketosteroids to hydroxysteroids. Acts as a
CC NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid
CC nucleus and side chain and regulates the metabolism of androgens,
CC estrogens and progesterone. Displays the ability to catalyze both
CC oxidation and reduction in vitro, but most probably acts as a reductase
CC in vivo since the oxidase activity measured in vitro is inhibited by
CC physiological concentration of NADPH. Acts preferentially as a 17-
CC ketosteroid reductase and has the highest catalytic efficiency of the
CC AKR1C enzyme for the reduction of delta4-androstenedione to form
CC testosterone. Reduces prostaglandin (PG) D2 to 11beta-prostaglandin F2,
CC progesterone to 20alpha-hydroxyprogesterone and estrone to 17beta-
CC estradiol. Catalyzes the transformation of the potent androgen
CC dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-
CC 3-alpha,17-beta-diol (3-alpha-diol). Also displays retinaldehyde
CC reductase activity toward 9-cis-retinal.
CC {ECO:0000250|UniProtKB:P42330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) +
CC NADPH; Xref=Rhea:RHEA:34783, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.357; Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) +
CC NADH; Xref=Rhea:RHEA:34779, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC ChEBI:CHEBI:47788, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.357; Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC D2; Xref=Rhea:RHEA:10140, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57406, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.188; Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.239; Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14931;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.64;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14982;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14983;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC H2; Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45314;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + prostaglandin D2 = 11beta-prostaglandin F2 +
CC NADP(+); Xref=Rhea:RHEA:45316, ChEBI:CHEBI:15378, ChEBI:CHEBI:57406,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85173;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45317;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45318;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + prostaglandin D2-ethanolamide = 11beta-
CC prostaglandin F2-ethanolamide + NADP(+); Xref=Rhea:RHEA:45308,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:85174, ChEBI:CHEBI:85175;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45309;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24617;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24614;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-hydroxypregn-4-en-3-one + NADP(+) = H(+) + NADPH +
CC progesterone; Xref=Rhea:RHEA:42112, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17026, ChEBI:CHEBI:28453, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42113;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42114;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-hydroxypregn-4-en-3-one + NAD(+) = H(+) + NADH +
CC progesterone; Xref=Rhea:RHEA:42108, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17026, ChEBI:CHEBI:28453, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42109;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42110;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NADP(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:42116,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42118;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha-hydroxy-5alpha-androstan-17-one + H(+) + NADPH =
CC 5alpha-androstane-3alpha,17beta-diol + NADP(+); Xref=Rhea:RHEA:42156,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42157;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42158;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 3alpha-
CC hydroxy-5alpha-androstan-17-one + H(+) + NADH; Xref=Rhea:RHEA:42124,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42125;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:16297,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.210;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16299;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54918;
CC Evidence={ECO:0000250|UniProtKB:P42330};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:P42330}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42330}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {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; CR860189; CAH92331.1; -; mRNA.
DR RefSeq; NP_001127540.1; NM_001134068.1.
DR AlphaFoldDB; Q5R7C9; -.
DR SMR; Q5R7C9; -.
DR GeneID; 100174617; -.
DR KEGG; pon:100174617; -.
DR CTD; 8644; -.
DR InParanoid; Q5R7C9; -.
DR OrthoDB; 1016440at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0047020; F:15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0047787; F:delta4-3-oxosteroid 5beta-reductase activity; ISS:UniProtKB.
DR GO; GO:0035410; F:dihydrotestosterone 17-beta-dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0045550; F:geranylgeranyl reductase activity; ISS:UniProtKB.
DR GO; GO:0045703; F:ketoreductase activity; ISS:UniProtKB.
DR GO; GO:0047086; F:ketosteroid monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; ISS:UniProtKB.
DR GO; GO:0018636; F:phenanthrene 9,10-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0036131; F:prostaglandin D2 11-ketoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; IEA:RHEA.
DR GO; GO:0047017; F:prostaglandin-F synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071384; P:cellular response to corticosteroid stimulus; ISS:UniProtKB.
DR GO; GO:0071395; P:cellular response to jasmonic acid stimulus; ISS:UniProtKB.
DR GO; GO:0071799; P:cellular response to prostaglandin D stimulus; ISS:UniProtKB.
DR GO; GO:0071379; P:cellular response to prostaglandin stimulus; ISS:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISS:UniProtKB.
DR GO; GO:0044597; P:daunorubicin metabolic process; ISS:UniProtKB.
DR GO; GO:0016488; P:farnesol catabolic process; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1900053; P:negative regulation of retinoic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0042448; P:progesterone metabolic process; ISS:UniProtKB.
DR GO; GO:0048385; P:regulation of retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000224; P:regulation of testosterone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; ISS:UniProtKB.
DR GO; GO:0061370; P:testosterone biosynthetic process; ISS:UniProtKB.
DR CDD; cd19108; AKR_AKR1C1-35; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044482; AKR1C.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipid metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..323
FT /note="Aldo-keto reductase family 1 member C3"
FT /id="PRO_0000124639"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 20..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P42330"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P42330"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P42330"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P42330"
FT BINDING 216..221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P42330"
FT BINDING 270..280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P42330"
FT SITE 54
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P14550"
FT SITE 227
FT /note="Involved in ligand recognition and product release"
FT /evidence="ECO:0000250|UniProtKB:P42330"
FT SITE 306
FT /note="Involved in ligand recognition and product release"
FT /evidence="ECO:0000250|UniProtKB:P42330"
SQ SEQUENCE 323 AA; 36848 MW; DCAD6ECA97C204AB CRC64;
MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ
VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM
SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEECKDAGLA KSIGVSNFNR RQLEMILNKP
GLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIREN VQVFEFQLTA EDMRAIDGLN
RNLHYFNSDS LASHPNYPYS DEY
