CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008409
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisomal multifunctional enzyme type 2 
Protein Synonyms/Alias
 MFE-2; 17-beta-hydroxysteroid dehydrogenase 4; 17-beta-HSD 4; D-bifunctional protein; DBP; Multifunctional protein 2; MPF-2; (3R)-hydroxyacyl-CoA dehydrogenase; Enoyl-CoA hydratase 2; 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase 
Gene Name
 HSD17B4 
Gene Synonyms/Alias
 EDH17B4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46NDLGGDFKGVGKGSLacetylation[1]
46NDLGGDFKGVGKGSLubiquitination[2]
139RAAWEHMKKQKYGRIacetylation[3]
184SLAIEGRKSNIHCNTubiquitination[2]
275AVKANWKKICDFENAubiquitination[2]
565AIKARFAKPVYPGQTacetylation[3]
565AIKARFAKPVYPGQTubiquitination[2]
669AKWTIDLKSGSGKVYacetylation[3]
707LGKLDPQKAFFSGRLacetylation[3]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids. 
Sequence Annotation
 DOMAIN 484 600 MaoC-like.
 DOMAIN 624 736 SCP2.
 NP_BIND 13 37 NAD (By similarity).
 NP_BIND 75 76 NAD.
 NP_BIND 164 168 NAD.
 NP_BIND 196 199 NAD.
 REGION 2 305 (3R)-hydroxyacyl-CoA dehydrogenase.
 REGION 322 622 Enoyl-CoA hydratase 2.
 REGION 406 407 (3R)-3-hydroxydecanoyl-CoA binding (By
 REGION 510 515 (3R)-3-hydroxydecanoyl-CoA binding (By
 MOTIF 734 736 Microbody targeting signal (Potential).
 ACT_SITE 164 164 Proton acceptor (By similarity).
 BINDING 21 21 NAD; via amide nitrogen.
 BINDING 40 40 NAD.
 BINDING 99 99 NAD; via carbonyl oxygen.
 BINDING 151 151 Substrate (By similarity).
 BINDING 435 435 (3R)-3-hydroxydecanoyl-CoA (By
 BINDING 533 533 (3R)-3-hydroxydecanoyl-CoA; via amide
 BINDING 563 563 (3R)-3-hydroxydecanoyl-CoA; via carbonyl
 BINDING 706 706 Substrate.
 BINDING 724 724 Substrate.
 MOD_RES 3 3 Phosphoserine (By similarity).
 MOD_RES 304 304 Phosphoserine.
 MOD_RES 309 309 Phosphoserine.
 MOD_RES 565 565 N6-acetyllysine.
 MOD_RES 663 663 N6-acetyllysine (By similarity).
 MOD_RES 669 669 N6-acetyllysine.
 MOD_RES 707 707 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Deafness; Direct protein sequencing; Disease mutation; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; NAD; Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 736 AA 
Protein Sequence
MGSPLRFDGR VVLVTGAGAG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSLAADKVVE 60
EIRRRGGKAV ANYDSVEEGE KVVKTALDAF GRIDVVVNNA GILRDRSFAR ISDEDWDIIH 120
RVHLRGSFQV TRAAWEHMKK QKYGRIIMTS SASGIYGNFG QANYSAAKLG LLGLANSLAI 180
EGRKSNIHCN TIAPNAGSRM TQTVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG 240
AGWIGKLRWE RTLGAIVRQK NHPMTPEAVK ANWKKICDFE NASKPQSIQE STGSIIEVLS 300
KIDSEGGVSA NHTSRATSTA TSGFAGAIGQ KLPPFSYAYT ELEAIMYALG VGASIKDPKD 360
LKFIYEGSSD FSCLPTFGVI IGQKSMMGGG LAEIPGLSIN FAKVLHGEQY LELYKPLPRA 420
GKLKCEAVVA DVLDKGSGVV IIMDVYSYSE KELICHNQFS LFLVGSGGFG GKRTSDKVKV 480
AVAIPNRPPD AVLTDTTSLN QAALYRLSGD WNPLHIDPNF ASLAGFDKPI LHGLCTFGFS 540
ARRVLQQFAD NDVSRFKAIK ARFAKPVYPG QTLQTEMWKE GNRIHFQTKV QETGDIVISN 600
AYVDLAPTSG TSAKTPSEGG KLQSTFVFEE IGRRLKDIGP EVVKKVNAVF EWHITKGGNI 660
GAKWTIDLKS GSGKVYQGPA KGAADTTIIL SDEDFMEVVL GKLDPQKAFF SGRLKARGNI 720
MLSQKLQMIL KDYAKL 736 
Gene Ontology
 GO:0005782; C:peroxisomal matrix; TAS:Reactome.
 GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
 GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IDA:UniProtKB.
 GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
 GO:0033989; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity; TAS:Reactome.
 GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
 GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0032934; F:sterol binding; IEA:InterPro.
 GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
 GO:0008209; P:androgen metabolic process; IDA:UniProtKB.
 GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
 GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
 GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
 GO:0036112; P:medium-chain fatty-acyl-CoA metabolic process; IDA:UniProtKB.
 GO:0036111; P:very long-chain fatty-acyl-CoA metabolic process; IDA:UniProtKB. 
Interpro
 IPR002198; DH_sc/Rdtase_SDR.
 IPR002347; Glc/ribitol_DH.
 IPR002539; MaoC_dom.
 IPR016040; NAD(P)-bd_dom.
 IPR020904; Sc_DH/Rdtase_CS.
 IPR003033; SCP2_sterol-bd_dom. 
Pfam
 PF00106; adh_short
 PF01575; MaoC_dehydratas
 PF02036; SCP2 
SMART
  
PROSITE
 PS00061; ADH_SHORT 
PRINTS
 PR00081; GDHRDH.
 PR00080; SDRFAMILY.