DHB4_RAT
ID DHB4_RAT Reviewed; 735 AA.
AC P97852; P70523; P70540;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Peroxisomal multifunctional enzyme type 2 {ECO:0000305};
DE Short=MFE-2;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 4;
DE Short=17-beta-HSD 4;
DE AltName: Full=D-bifunctional protein;
DE Short=DBP;
DE AltName: Full=Multifunctional protein 2;
DE Short=MFP-2;
DE Contains:
DE RecName: Full=(3R)-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.n12 {ECO:0000250|UniProtKB:P51659};
DE Contains:
DE RecName: Full=Enoyl-CoA hydratase 2;
DE EC=4.2.1.107 {ECO:0000250|UniProtKB:P51659};
DE EC=4.2.1.119 {ECO:0000250|UniProtKB:P51659};
DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase;
GN Name=Hsd17b4 {ECO:0000312|RGD:621806}; Synonyms=Edh17b4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-30; 32-44; 110-115;
RP 132-139 AND 270-274, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RC TISSUE=Liver;
RX PubMed=8856068; DOI=10.1111/j.1432-1033.1996.0660h.x;
RA Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T.,
RA Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P.,
RA Mannaerts G.P.;
RT "Further characterization of the peroxisomal 3-hydroxyacyl-CoA
RT dehydrogenases from rat liver. Relationship between the different
RT dehydrogenases and evidence that fatty acids and the C27 bile acids di- and
RT tri-hydroxycoprostanic acids are metabolized by separate multifunctional
RT proteins.";
RL Eur. J. Biochem. 240:660-666(1996).
RN [2]
RP ERRATUM OF PUBMED:8856068.
RX DOI=10.1111/j.1432-1033.1997.537_1a.x;
RA Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T.,
RA Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P.,
RA Mannaerts G.P.;
RL Eur. J. Biochem. 243:537-537(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8913347;
RA Corton J.C., Bocos C., Moreno E.S., Merritt A., Marsman D.S., Sausen P.J.,
RA Cattley R.C., Gustafsson J.-A.;
RT "Rat 17 beta-hydroxysteroid dehydrogenase type IV is a novel peroxisome
RT proliferator-inducible gene.";
RL Mol. Pharmacol. 50:1157-1166(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 318-330; 479-505; 542-554;
RP 562-576 AND 583-587, AND ENZYME CATALYSIS.
RX PubMed=9003397; DOI=10.1042/bj3210021;
RA Qin Y.M., Poutanen M.H., Helander H.M., Kvist A.P., Siivari K.M.,
RA Schmitz W., Conzelmann E., Hellman U., Hiltunen J.K.;
RT "Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-
RT hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and
RT characterization.";
RL Biochem. J. 321:21-28(1997).
RN [5]
RP PROTEIN SEQUENCE OF 312-324, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=9003427; DOI=10.1042/bj3210253;
RA Dieuaide-Noubhani M., Novikov D., Vandekerckhove J., Veldhoven P.P.,
RA Mannaerts G.P.;
RT "Identification and characterization of the 2-enoyl-CoA hydratases involved
RT in peroxisomal beta-oxidation in rat liver.";
RL Biochem. J. 321:253-259(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-319 IN COMPLEX WITH NAD, AND
RP HOMODIMERIZATION.
RX PubMed=12517343; DOI=10.1016/s0969-2126(02)00931-0;
RA Haapalainen A.M., Koski M.K., Qin Y.-M., Hiltunen J.K., Glumoff T.;
RT "Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from
RT rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution.";
RL Structure 11:87-97(2003).
CC -!- FUNCTION: Bifunctional enzyme acting on the peroxisomal beta-oxidation
CC pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA
CC intermediates from straight-chain, 2-methyl-branched-chain fatty acids
CC bile acid intermediates. With EHHADH, catalyzes the hydration of trans-
CC 2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with
CC opposite chiral specificity. {ECO:0000250|UniProtKB:P51659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:32711, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726;
CC EC=1.1.1.n12; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32712;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-
CC cholestan-26-oyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-
CC cholest-24-en-26-oyl-CoA + H2O; Xref=Rhea:RHEA:18933,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:59807, ChEBI:CHEBI:59879;
CC EC=4.2.1.107; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18935;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:58856; EC=4.2.1.119;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26527;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenoyl-CoA + H2O = (3R)-hydroxyoctanoyl-CoA;
CC Xref=Rhea:RHEA:40187, ChEBI:CHEBI:15377, ChEBI:CHEBI:62242,
CC ChEBI:CHEBI:74279; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40188;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:40191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62619, ChEBI:CHEBI:74279;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40192;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC + H(+) + NADH; Xref=Rhea:RHEA:40243, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:74278; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40244;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenedioyl-CoA + H2O = (3R)-hydroxyhexadecanedioyl-
CC CoA; Xref=Rhea:RHEA:40255, ChEBI:CHEBI:15377, ChEBI:CHEBI:77075,
CC ChEBI:CHEBI:77079; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40256;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanedioyl-CoA + NAD(+) = 3-
CC oxohexadecanedioyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:40263,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:77079, ChEBI:CHEBI:77081;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40264;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:74278; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:39161;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:45992, ChEBI:CHEBI:15377, ChEBI:CHEBI:61406,
CC ChEBI:CHEBI:74272; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45994;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+)
CC + NADH; Xref=Rhea:RHEA:45832, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:74272;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45833;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-
CC cholestan-26-oyl-CoA + NAD(+) = 3alpha,7alpha,12alpha-trihydroxy-24-
CC oxo-5beta-cholestan-26-oyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:47088,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58507, ChEBI:CHEBI:59807;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47089;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P51659}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12517343}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:8856068}.
CC -!- MISCELLANEOUS: The protein is found both as a full-length peptide and
CC in a cleaved version.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; S83279; AAB49519.1; -; mRNA.
DR EMBL; U37486; AAB09724.1; -; mRNA.
DR EMBL; X94978; CAA64427.1; -; mRNA.
DR RefSeq; NP_077368.2; NM_024392.2.
DR PDB; 1GZ6; X-ray; 2.38 A; A/B/C/D=1-319.
DR PDBsum; 1GZ6; -.
DR AlphaFoldDB; P97852; -.
DR SMR; P97852; -.
DR BioGRID; 249442; 2.
DR IntAct; P97852; 2.
DR STRING; 10116.ENSRNOP00000021646; -.
DR ChEMBL; CHEMBL1075219; -.
DR iPTMnet; P97852; -.
DR PhosphoSitePlus; P97852; -.
DR jPOST; P97852; -.
DR PaxDb; P97852; -.
DR PRIDE; P97852; -.
DR GeneID; 79244; -.
DR KEGG; rno:79244; -.
DR UCSC; RGD:621806; rat.
DR CTD; 3295; -.
DR RGD; 621806; Hsd17b4.
DR VEuPathDB; HostDB:ENSRNOG00000015840; -.
DR eggNOG; ENOG502QPX4; Eukaryota.
DR HOGENOM; CLU_010194_18_4_1; -.
DR InParanoid; P97852; -.
DR OrthoDB; 1120431at2759; -.
DR BioCyc; MetaCyc:MON-14329; -.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-RNO-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-RNO-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; P97852; -.
DR PRO; PR:P97852; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000015840; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; P97852; baseline and differential.
DR Genevisible; P97852; RN.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0106386; F:(3R)-hydroxyacyl-CoA dehydrogenase (NAD) activity; IEA:RHEA.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IDA:RGD.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0033989; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; ISS:UniProtKB.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; TAS:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0008209; P:androgen metabolic process; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; NAS:RGD.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0036112; P:medium-chain fatty-acyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0060009; P:Sertoli cell development; ISO:RGD.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
DR GO; GO:0036111; P:very long-chain fatty-acyl-CoA metabolic process; ISO:RGD.
DR Gene3D; 3.30.1050.10; -; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR SUPFAM; SSF55718; SSF55718; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; NAD;
KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..735
FT /note="Peroxisomal multifunctional enzyme type 2"
FT /id="PRO_0000054585"
FT CHAIN 1..311
FT /note="(3R)-hydroxyacyl-CoA dehydrogenase"
FT /id="PRO_0000400086"
FT CHAIN 312..735
FT /note="Enoyl-CoA hydratase 2"
FT /id="PRO_0000400087"
FT DOMAIN 483..599
FT /note="MaoC-like"
FT DOMAIN 623..735
FT /note="SCP2"
FT REGION 1..305
FT /note="(3R)-hydroxyacyl-CoA dehydrogenase"
FT REGION 321..621
FT /note="Enoyl-CoA hydratase 2"
FT MOTIF 733..735
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT BINDING 16..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12517343"
FT BINDING 21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT BINDING 164..168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 405..406
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 509..514
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 562
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 705
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 46
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 68
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 275
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 355
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 423
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 564
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 578
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 662
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT MOD_RES 668
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 724
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51660"
FT CONFLICT 1..2
FT /note="MA -> M (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="V -> G (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="A -> G (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="V -> G (in Ref. 4; AAB09724)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="R -> P (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> S (in Ref. 4; AAB09724)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="K -> E (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="A -> P (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="F -> I (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="M -> T (in Ref. 4; AAB09724)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="S -> D (in Ref. 4; AAB09724)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="L -> V (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="S -> G (in Ref. 1; CAA64427)"
FT /evidence="ECO:0000305"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1GZ6"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:1GZ6"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1GZ6"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:1GZ6"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 113..141
FT /evidence="ECO:0007829|PDB:1GZ6"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1GZ6"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:1GZ6"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:1GZ6"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1GZ6"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:1GZ6"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:1GZ6"
SQ SEQUENCE 735 AA; 79428 MW; E14F15FFD35FC7D8 CRC64;
MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSSAADKVVE
EIRRRGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA GILRDRSFSR ISDEDWDIIQ
RVHLRGSFQV TRAAWDHMKK QNYGRIIMTA SASGIYGNFG QANYSAAKLG LLGLANTLVI
EGRKNNIHCN TIAPNAGSRM TETVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG
AGWIGKLRWE RTLGAIVRKR NQPMTPEAVR DNWVKICDFS NASKPKSIQE STGGIIEVLH
KIDSEGISQN HTGQVASADA SGFAGVVGHK LPSFSSSYTE LQCIMYALGV GASVKNPKDL
KFVYEGSADF SCLPTFGVIV AQKSLMSGGL AEVPGLSINF AKVLHGEQYL ELYKPLPRSG
ELKCEAVIAD ILDKGSGIVI VMDVYSYSGK ELICYNQFSV FVVGSGGFGG KRTSEKLKAA
VAVPSRPPDA VLRDTTSLNQ AALYRLSGDS NPLHIDPSFA SIAGFEKPIL HGLCTFGFSA
RHVLQQFADN DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVQ ETGDIVISNA
YVDLVPTSGV SAQTPSEGGA LQSALVFGEI GRRLKDVGRE VVKKVNAVFE WHITKNGNVA
AKWTIDLKNG SGEVYQGPAK GSADTTITIS DEDFMEVVLG KLNPQNAFFS GRLKARGNIM
LSQKLQMILK DYAKL
