DHRS4_RABIT
ID DHRS4_RABIT Reviewed; 260 AA.
AC Q9GKX2;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Dehydrogenase/reductase SDR family member 4 {ECO:0000303|PubMed:19056333};
DE EC=1.1.1.184 {ECO:0000305|PubMed:12604222, ECO:0000305|PubMed:19056333, ECO:0000305|PubMed:9880795};
DE EC=1.1.1.300 {ECO:0000305|PubMed:12604222};
DE AltName: Full=NADPH-dependent carbonyl reductase {ECO:0000303|PubMed:12604222};
DE Short=CR {ECO:0000303|PubMed:12604222};
DE Short=RACR {ECO:0000303|PubMed:12604222};
DE AltName: Full=NADPH-dependent retinol dehydrogenase/reductase {ECO:0000303|PubMed:12604222};
DE Short=NDRD {ECO:0000303|PubMed:12604222};
DE AltName: Full=Peroxisomal short-chain alcohol dehydrogenase;
DE Short=PSCD;
DE AltName: Full=Short chain dehydrogenase/reductase family 25C member 2 {ECO:0000250|UniProtKB:Q9BTZ2};
DE Short=Protein SDR25C2 {ECO:0000250|UniProtKB:Q9BTZ2};
DE AltName: Full=rabNRDR;
DE Flags: Fragment;
GN Name=DHRS4;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RA Furukawa A., Ohnishi T., Huang D., Araki N., Ichikawa Y.;
RT "cDNA cloning and characterization of peroxisomal short-chain dehydrogenase
RT / reductase that reduce all-trans retinal to retinol.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 75-83; 108-115; 119-125; 133-149 AND 177-190, FUNCTION,
RP TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC TISSUE=Heart;
RX PubMed=12604222; DOI=10.1016/s0009-2797(02)00210-7;
RA Usami N., Ishikura S., Abe H., Nagano M., Uebuchi M., Kuniyasu A.,
RA Otagiri M., Nakayama H., Imamura Y., Hara A.;
RT "Cloning, expression and tissue distribution of a tetrameric form of pig
RT carbonyl reductase.";
RL Chem. Biol. Interact. 143:353-361(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RX PubMed=9880795; DOI=10.1093/oxfordjournals.jbchem.a022266;
RA Imamura Y., Migita T., Otagiri M., Choshi T., Hibino S.;
RT "Purification and catalytic properties of a tetrameric carbonyl reductase
RT from rabbit heart.";
RL J. Biochem. 125:41-47(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19056333; DOI=10.1016/j.abb.2008.11.014;
RA Endo S., Maeda S., Matsunaga T., Dhagat U., El-Kabbani O., Tanaka N.,
RA Nakamura K.T., Tajima K., Hara A.;
RT "Molecular determinants for the stereospecific reduction of 3-ketosteroids
RT and reactivity towards all-trans-retinal of a short-chain
RT dehydrogenase/reductase (DHRS4).";
RL Arch. Biochem. Biophys. 481:183-190(2009).
CC -!- FUNCTION: NADPH-dependent oxidoreductase which catalyzes the reduction
CC of a variety of compounds bearing carbonyl groups including
CC ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones
CC and quinones (PubMed:12604222, PubMed:9880795, PubMed:19056333).
CC Reduces all-trans-retinal and 9-cis retinal (Probable). Reduces 3-
CC ketosteroids and benzil into 3alpha-hydroxysteroids and S-benzoin,
CC respectively, in contrast to the stereoselectivity of primates DHRS4s
CC which produce 3beta-hydroxysteroids and R-benzoin (By similarity). In
CC the reverse reaction, catalyze the NADP-dependent oxidation of 3alpha-
CC hydroxysteroids and alcohol, but with much lower efficiency (By
CC similarity). Involved in the metabolism of 3alpha-hydroxysteroids,
CC retinoid, isatin and xenobiotic carbonyl compounds (PubMed:12604222,
CC PubMed:19056333). {ECO:0000250|UniProtKB:Q8WNV7,
CC ECO:0000269|PubMed:12604222, ECO:0000269|PubMed:19056333,
CC ECO:0000269|PubMed:9880795, ECO:0000305|PubMed:12604222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH;
CC Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.184; Evidence={ECO:0000305|PubMed:12604222,
CC ECO:0000305|PubMed:19056333, ECO:0000305|PubMed:9880795};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259;
CC Evidence={ECO:0000305|PubMed:12604222, ECO:0000305|PubMed:19056333,
CC ECO:0000305|PubMed:9880795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha-hydroxy-5beta-pregnan-20-one + NADP(+) = 5beta-pregnan-
CC 3,20-dione + H(+) + NADPH; Xref=Rhea:RHEA:69016, ChEBI:CHEBI:1712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30154, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000305|PubMed:19056333};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69017;
CC Evidence={ECO:0000305|PubMed:19056333};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5beta-dihydrotestosterone + H(+) + NADPH = 5beta-androstane-
CC 3alpha,17beta-diol + NADP(+); Xref=Rhea:RHEA:69028, ChEBI:CHEBI:2150,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36714, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:Q8WNV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69029;
CC Evidence={ECO:0000250|UniProtKB:Q8WNV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300; Evidence={ECO:0000269|PubMed:12604222};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25035;
CC Evidence={ECO:0000305|PubMed:12604222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + isatin + NADPH = 3-hydroxyindolin-2-one + NADP(+);
CC Xref=Rhea:RHEA:68608, ChEBI:CHEBI:15378, ChEBI:CHEBI:27539,
CC ChEBI:CHEBI:28536, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000305|PubMed:12604222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68609;
CC Evidence={ECO:0000305|PubMed:12604222};
CC -!- ACTIVITY REGULATION: Inhibited by flavonoids (kaempferol, quercetin,
CC quercitrin, genistein), myristic acid, pyrazole, barbital,
CC phenobarbital and CuSO4. {ECO:0000269|PubMed:9880795,
CC ECO:0000305|PubMed:12604222}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.028 mM for 16-Ketoestrone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.045 mM for 16-Ketoestrone (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.007 mM for all-trans-Retinal (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.079 mM for 9-cis-retinal (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.11 mM for Isatin (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.061 mM for Isatin (at pH7.4) {ECO:0000269|PubMed:12604222};
CC KM=0.89 mM for Propiophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.063 mM for Heptanophenone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.027 mM for Nonanophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.095 mM for 4-Hexanoylpyridine (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.022 mM for Hexanophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.11 mM for Valerophenone (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.18 mM for n-Butyrophenone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.52 mM for 3-Benzoylpyridine (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.69 mM for 4-Benzoylpyridine (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=1.7 mM for 2,3-Hexanedione (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.4 mM for 1-phenyl-1,2-propanedione (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.11 mM for Benzil (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=13 mM for Diacetyl (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=1.8 mM for Pyridine-4-aldehyde (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.006 mM for 1-Phenylisatin (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.001 mM for 9,10-Phenanthrenequinone (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.001 mM for 9,10-Phenanthrenequinone (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.12 mM for Menadione (at pH6) {ECO:0000269|PubMed:12604222};
CC KM=0.27 mM for S-(-)-1-Phenyl-1-butanol (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.034 mM for all-trans-Retinol (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC KM=0.33 mM for 3-Benzoylpyridine (at pH6)
CC {ECO:0000269|PubMed:9880795};
CC KM=0.63 mM for 4-Benzoylpyridine (at pH6)
CC {ECO:0000269|PubMed:9880795};
CC KM=1.55 mM for 4-Acetylpyridine (at pH6)
CC {ECO:0000269|PubMed:9880795};
CC KM=1.8 mM for Pyridine-3-aldehyde (at pH6)
CC {ECO:0000269|PubMed:9880795};
CC KM=0.9 mM for Pyridine-4-aldehyde (at pH6)
CC {ECO:0000269|PubMed:9880795};
CC KM=0.59 mM for 4-Nitroacetophenone (at pH6)
CC {ECO:0000269|PubMed:9880795};
CC KM=0.18 mM for Menadione (at pH6) {ECO:0000269|PubMed:9880795};
CC KM=0.028 mM for 5beta-Pregnane-3,20-dione (at pH7.4)
CC {ECO:0000269|PubMed:19056333};
CC Vmax=48.7 umol/min/mg enzyme with 16-Ketoestrone as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=24.2 umol/min/mg enzyme with 16-Ketoestrone as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=2.54 umol/min/mg enzyme with all-trans-Retinal as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=6.34 umol/min/mg enzyme with 9-cis-retinal as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=83.6 umol/min/mg enzyme with Isatin as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=34.5 umol/min/mg enzyme with Isatin as substrate (at pH7.4)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=1 umol/min/mg enzyme with Propiophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=6.5 umol/min/mg enzyme with Heptanophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=3.5 umol/min/mg enzyme with Nonanophenoneas substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=55.7 umol/min/mg enzyme with 4-Hexanoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=5.8 umol/min/mg enzyme with Hexanophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=5.8 umol/min/mg enzyme with Valerophenone as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=3.3 umol/min/mg enzyme with n-Butyrophenone as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=3.8 umol/min/mg enzyme with 3-benzoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=13.3 umol/min/mg enzyme with 4-Benzoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=115 umol/min/mg enzyme with 2,3-Hexanedione as substrate (at
CC pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=115 umol/min/mg enzyme with 1-phenyl-1,2-propanedione as
CC substrate (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=66.8 umol/min/mg enzyme for the reduction of Benzil into S-
CC benzoin (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=110 umol/min/mg enzyme with Diacetyl as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=98.9 umol/min/mg enzyme with Pyridine-4-aldehyde as substrate
CC (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=152 umol/min/mg enzyme with 1-Phenylisatin as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=121 umol/min/mg enzyme with 9,10-Phenanthrenequinone as
CC substrate (at pH6) {ECO:0000269|PubMed:12604222};
CC Vmax=78 umol/min/mg enzyme with 9,10-Phenanthrenequinone as substrate
CC (at pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=2.6 umol/min/mg enzyme with Menadione as substrate (at pH6)
CC {ECO:0000269|PubMed:12604222};
CC Vmax=1.35 umol/min/mg enzyme with S-(-)-1-Phenyl-1-butanol as
CC substrate (at pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=0.034 umol/min/mg enzyme with all-trans-Retinol as substrate (at
CC pH7.4) {ECO:0000269|PubMed:12604222};
CC Vmax=0.76 umol/min/mg enzyme with 3-Benzoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:9880795};
CC Vmax=2.98 umol/min/mg enzyme with 4-Benzoylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:9880795};
CC Vmax=1.76 umol/min/mg enzyme with 4-Acetylpyridine as substrate (at
CC pH6) {ECO:0000269|PubMed:9880795};
CC Vmax=3.64 umol/min/mg enzyme with Pyridine-3-aldehyde as substrate
CC (at pH6) {ECO:0000269|PubMed:9880795};
CC Vmax=10.5 umol/min/mg enzyme with Pyridine-4-aldehyde as substrate
CC (at pH6) {ECO:0000269|PubMed:9880795};
CC Vmax=1.73 umol/min/mg enzyme with 4-Nitroacetophenone as substrate
CC (at pH6) {ECO:0000269|PubMed:9880795};
CC Vmax=2.47 umol/min/mg enzyme with Menadione as substrate (at pH6)
CC {ECO:0000269|PubMed:9880795};
CC Note=kcat is 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate
CC (at pH7.4). {ECO:0000269|PubMed:19056333};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12604222}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q8WNV7}.
CC -!- TISSUE SPECIFICITY: Detected in liver and kidney. Detected at lower
CC levels in heart, lung, spleen, small intestine, testis, brain and
CC stomach. {ECO:0000269|PubMed:12604222}.
CC -!- DOMAIN: The C-terminus peroxisomal targeting signal tripeptide is
CC important for peroxisomal import. Once in the peroxisome, it is
CC involved in intersubunit interactions. {ECO:0000250|UniProtKB:Q8WNV7}.
CC -!- DOMAIN: Three specific residues, Phe-158, Leu-161 and Asn-177 are
CC conserved between non-primate mammals whereas the respective residues
CC are serine, phenylalanine and threonine in primates (PubMed:19056333).
CC The two residues at positions 158 and 161 are molecular determinants
CC responsible for the stereoselective reduction of 3-ketosteroids and
CC benzil (PubMed:19056333). The presence of an asparagine at position 177
CC is important for the maintenance of the quaternary structure resulting
CC in stability at cold temperature and improved catalytic activity toward
CC retinal (PubMed:19056333). {ECO:0000269|PubMed:19056333}.
CC -!- MISCELLANEOUS: Primate DHRS4s display different stereoselectivity and
CC catalytic efficiency in the oxidoreduction of some substrates as
CC compared to other mammal DHRS4s due to a difference in conserved amino
CC acid residues. {ECO:0000269|PubMed:19056333}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB045133; BAB18777.1; -; mRNA.
DR AlphaFoldDB; Q9GKX2; -.
DR SMR; Q9GKX2; -.
DR STRING; 9986.ENSOCUP00000019647; -.
DR eggNOG; KOG0725; Eukaryota.
DR InParanoid; Q9GKX2; -.
DR BRENDA; 1.1.1.300; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042180; P:cellular ketone metabolic process; IDA:UniProtKB.
DR GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
DR InterPro; IPR029511; DHRS4-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43943:SF8; PTHR43943:SF8; 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; Direct protein sequencing; NADP; Oxidoreductase; Peroxisome;
KW Phosphoprotein; Reference proteome.
FT CHAIN <1..260
FT /note="Dehydrogenase/reductase SDR family member 4"
FT /id="PRO_0000054651"
FT MOTIF 258..260
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 18..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT SITE 158
FT /note="Responsible for the stereoselective reduction of 3-
FT ketosteroids into 3alpha-hydroxysteroids and benzil into S-
FT benzoin"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT SITE 161
FT /note="Responsible for the stereoselective reduction of 3-
FT ketosteroids into 3alpha-hydroxysteroids and benzil into S-
FT benzoin"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT SITE 177
FT /note="Important for the maintenance of the quaternary
FT structure, the catalytic activity and cold stability"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 74
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 198
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 198
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT MOD_RES 209
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LB2"
FT NON_TER 1
SQ SEQUENCE 260 AA; 27430 MW; 5B0585B58911B90C CRC64;
MASSGVTRRD PLANKVAIVT ASTDGIGLAI ARRLAQDGAH VVISSRKQQN VDRAVAALQA
EGLSVTGTVC HVGKAEDRER LVATALNLHG GIDILVSNAA VNPFFGKLMD VTEEVWDKIL
DINVKAMALM TKAVVPEMEK RGGGSVVIVA SIAAFNPFSG LGPYNVSKTA LVGLTKNLAL
ELAAQNIRVN CLAPGLIKTS FSKALWEDKA QEENIIQKLR IRRLGKPEEC AGIVSFLCSE
DASYITGETV VVAGGAPSRL
