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Peroxisomal multifunctional enzyme type 2 (MFE-2) (17-beta-hydroxysteroid dehydrogenase 4) (17-beta-HSD 4) (D-bifunctional protein) (DBP) (Multifunctional protein 2) (MPF-2) [Cleaved into: (3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12); Enoyl-CoA hydratase 2 (EC 4.2.1.107) (EC 4.2.1.119) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase)]

 DHB4_RAT                Reviewed;         735 AA.
P97852; P70523; P70540;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 151.
RecName: Full=Peroxisomal multifunctional enzyme type 2;
Short=MFE-2;
AltName: Full=17-beta-hydroxysteroid dehydrogenase 4;
Short=17-beta-HSD 4;
AltName: Full=D-bifunctional protein;
Short=DBP;
AltName: Full=Multifunctional protein 2;
Short=MPF-2;
Contains:
RecName: Full=(3R)-hydroxyacyl-CoA dehydrogenase;
EC=1.1.1.n12;
Contains:
RecName: Full=Enoyl-CoA hydratase 2;
EC=4.2.1.107;
EC=4.2.1.119;
AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase;
Name=Hsd17b4; Synonyms=Edh17b4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-30; 32-44; 110-115;
132-139 AND 270-274, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
TISSUE=Liver;
PubMed=8856068; DOI=10.1111/j.1432-1033.1996.0660h.x;
Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T.,
Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P.,
Mannaerts G.P.;
"Further characterization of the peroxisomal 3-hydroxyacyl-CoA
dehydrogenases from rat liver. Relationship between the different
dehydrogenases and evidence that fatty acids and the C27 bile acids
di- and tri-hydroxycoprostanic acids are metabolized by separate
multifunctional proteins.";
Eur. J. Biochem. 240:660-666(1996).
[2]
ERRATUM.
DOI=10.1111/j.1432-1033.1997.537_1a.x;
Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T.,
Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P.,
Mannaerts G.P.;
Eur. J. Biochem. 243:537-537(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8913347;
Corton J.C., Bocos C., Moreno E.S., Merritt A., Marsman D.S.,
Sausen P.J., Cattley R.C., Gustafsson J.-A.;
"Rat 17 beta-hydroxysteroid dehydrogenase type IV is a novel
peroxisome proliferator-inducible gene.";
Mol. Pharmacol. 50:1157-1166(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 318-330; 479-505;
542-554; 562-576 AND 583-587, AND ENZYME CATALYSIS.
PubMed=9003397; DOI=10.1042/bj3210021;
Qin Y.M., Poutanen M.H., Helander H.M., Kvist A.P., Siivari K.M.,
Schmitz W., Conzelmann E., Hellman U., Hiltunen J.K.;
"Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-
3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression
and characterization.";
Biochem. J. 321:21-28(1997).
[5]
PROTEIN SEQUENCE OF 312-324, AND PROTEOLYTIC CLEAVAGE.
PubMed=9003427; DOI=10.1042/bj3210253;
Dieuaide-Noubhani M., Novikov D., Vandekerckhove J., Veldhoven P.P.,
Mannaerts G.P.;
"Identification and characterization of the 2-enoyl-CoA hydratases
involved in peroxisomal beta-oxidation in rat liver.";
Biochem. J. 321:253-259(1997).
[6]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-319 IN COMPLEX WITH NAD,
AND HOMODIMERIZATION.
PubMed=12517343; DOI=10.1016/S0969-2126(02)00931-0;
Haapalainen A.M., Koski M.K., Qin Y.-M., Hiltunen J.K., Glumoff T.;
"Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase
from rat peroxisomal multifunctional enzyme type 2 at 2.38 A
resolution.";
Structure 11:87-97(2003).
-!- FUNCTION: 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.
-!- CATALYTIC ACTIVITY: (R)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH.
-!- CATALYTIC ACTIVITY: (24R,25R)-3-alpha,7-alpha,12-alpha,24-
tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12-
alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H(2)O.
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA +
H(2)O.
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12517343}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:8856068}.
-!- MISCELLANEOUS: The protein is found both as a full-length peptide
and in a cleaved version.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S83279; AAB49519.1; -; mRNA.
EMBL; U37486; AAB09724.1; -; mRNA.
EMBL; X94978; CAA64427.1; -; mRNA.
RefSeq; NP_077368.2; NM_024392.2.
UniGene; Rn.2082; -.
PDB; 1GZ6; X-ray; 2.38 A; A/B/C/D=1-319.
PDBsum; 1GZ6; -.
ProteinModelPortal; P97852; -.
SMR; P97852; -.
IntAct; P97852; 1.
STRING; 10116.ENSRNOP00000021646; -.
ChEMBL; CHEMBL1075219; -.
iPTMnet; P97852; -.
PhosphoSitePlus; P97852; -.
PaxDb; P97852; -.
PRIDE; P97852; -.
Ensembl; ENSRNOT00000021646; ENSRNOP00000021646; ENSRNOG00000015840.
GeneID; 79244; -.
KEGG; rno:79244; -.
UCSC; RGD:621806; rat.
CTD; 3295; -.
RGD; 621806; Hsd17b4.
eggNOG; KOG1206; Eukaryota.
eggNOG; COG2030; LUCA.
GeneTree; ENSGT00530000062928; -.
HOGENOM; HOG000170895; -.
HOVERGEN; HBG002174; -.
InParanoid; P97852; -.
KO; K12405; -.
BioCyc; MetaCyc:MONOMER-14329; -.
Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-RNO-389887; Beta-oxidation of pristanoyl-CoA.
Reactome; R-RNO-390247; Beta-oxidation of very long chain fatty acids.
Reactome; R-RNO-9033241; Peroxisomal protein import.
UniPathway; UPA00659; -.
EvolutionaryTrace; P97852; -.
PRO; PR:P97852; -.
Proteomes; UP000002494; Chromosome 18.
Bgee; ENSRNOG00000015840; Expressed in 10 organ(s), highest expression level in liver.
ExpressionAtlas; P97852; baseline and differential.
Genevisible; P97852; RN.
GO; GO:0005777; C:peroxisome; IDA:HGNC.
GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IDA:RGD.
GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IDA:RGD.
GO; GO:0033989; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:RGD.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; TAS:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0008203; P:cholesterol metabolic process; NAS:RGD.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
Gene3D; 3.30.1050.10; -; 1.
InterPro; IPR029069; HotDog_dom_sf.
InterPro; IPR002539; MaoC_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR003033; SCP2_sterol-bd_dom.
InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
Pfam; PF01575; MaoC_dehydratas; 1.
Pfam; PF02036; SCP2; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF54637; SSF54637; 2.
SUPFAM; SSF55718; SSF55718; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Fatty acid metabolism; Isomerase;
Lipid metabolism; Lyase; NAD; Oxidoreductase; Peroxisome;
Phosphoprotein; Reference proteome.
CHAIN 1 735 Peroxisomal multifunctional enzyme type
2.
/FTId=PRO_0000054585.
CHAIN 1 311 (3R)-hydroxyacyl-CoA dehydrogenase.
/FTId=PRO_0000400086.
CHAIN 312 735 Enoyl-CoA hydratase 2.
/FTId=PRO_0000400087.
DOMAIN 483 599 MaoC-like.
DOMAIN 623 735 SCP2.
NP_BIND 16 40 NAD. {ECO:0000269|PubMed:12517343}.
NP_BIND 75 76 NAD. {ECO:0000250}.
NP_BIND 164 168 NAD. {ECO:0000250}.
NP_BIND 196 199 NAD. {ECO:0000250}.
REGION 1 305 (3R)-hydroxyacyl-CoA dehydrogenase.
REGION 321 621 Enoyl-CoA hydratase 2.
REGION 405 406 (3R)-3-hydroxydecanoyl-CoA binding.
{ECO:0000250}.
REGION 509 514 (3R)-3-hydroxydecanoyl-CoA binding.
{ECO:0000250}.
MOTIF 733 735 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 164 164 Proton acceptor.
BINDING 21 21 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 40 40 NAD. {ECO:0000250}.
BINDING 99 99 NAD; via carbonyl oxygen. {ECO:0000250}.
BINDING 151 151 Substrate.
BINDING 434 434 (3R)-3-hydroxydecanoyl-CoA.
{ECO:0000250}.
BINDING 532 532 (3R)-3-hydroxydecanoyl-CoA; via amide
nitrogen. {ECO:0000250}.
BINDING 562 562 (3R)-3-hydroxydecanoyl-CoA; via carbonyl
oxygen. {ECO:0000250}.
BINDING 705 705 Substrate. {ECO:0000250}.
BINDING 723 723 Substrate. {ECO:0000250}.
MOD_RES 46 46 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 46 46 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:P51659}.
MOD_RES 57 57 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 68 68 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 84 84 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 265 265 Phosphothreonine.
{ECO:0000250|UniProtKB:P51659}.
MOD_RES 275 275 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:P51659}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000250|UniProtKB:P51659}.
MOD_RES 355 355 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 423 423 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 564 564 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51659}.
MOD_RES 578 578 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 662 662 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 668 668 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51659}.
MOD_RES 724 724 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
CONFLICT 1 2 MA -> M (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 12 12 V -> G (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 26 26 A -> G (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 76 76 V -> G (in Ref. 4; AAB09724).
{ECO:0000305}.
CONFLICT 106 106 R -> P (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 157 157 G -> S (in Ref. 4; AAB09724).
{ECO:0000305}.
CONFLICT 284 284 K -> E (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 368 368 A -> P (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 376 376 F -> I (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 386 386 M -> T (in Ref. 4; AAB09724).
{ECO:0000305}.
CONFLICT 485 485 S -> D (in Ref. 4; AAB09724).
{ECO:0000305}.
CONFLICT 498 498 L -> V (in Ref. 1; CAA64427).
{ECO:0000305}.
CONFLICT 521 521 S -> G (in Ref. 1; CAA64427).
{ECO:0000305}.
STRAND 11 14 {ECO:0000244|PDB:1GZ6}.
TURN 15 18 {ECO:0000244|PDB:1GZ6}.
HELIX 20 31 {ECO:0000244|PDB:1GZ6}.
STRAND 35 39 {ECO:0000244|PDB:1GZ6}.
HELIX 53 64 {ECO:0000244|PDB:1GZ6}.
STRAND 68 72 {ECO:0000244|PDB:1GZ6}.
HELIX 76 78 {ECO:0000244|PDB:1GZ6}.
HELIX 79 89 {ECO:0000244|PDB:1GZ6}.
STRAND 95 98 {ECO:0000244|PDB:1GZ6}.
HELIX 108 110 {ECO:0000244|PDB:1GZ6}.
HELIX 113 141 {ECO:0000244|PDB:1GZ6}.
STRAND 144 149 {ECO:0000244|PDB:1GZ6}.
HELIX 152 156 {ECO:0000244|PDB:1GZ6}.
HELIX 162 181 {ECO:0000244|PDB:1GZ6}.
HELIX 183 185 {ECO:0000244|PDB:1GZ6}.
STRAND 187 195 {ECO:0000244|PDB:1GZ6}.
TURN 199 201 {ECO:0000244|PDB:1GZ6}.
HELIX 202 204 {ECO:0000244|PDB:1GZ6}.
HELIX 207 212 {ECO:0000244|PDB:1GZ6}.
HELIX 215 217 {ECO:0000244|PDB:1GZ6}.
HELIX 219 225 {ECO:0000244|PDB:1GZ6}.
STRAND 236 240 {ECO:0000244|PDB:1GZ6}.
STRAND 243 251 {ECO:0000244|PDB:1GZ6}.
HELIX 266 271 {ECO:0000244|PDB:1GZ6}.
HELIX 273 276 {ECO:0000244|PDB:1GZ6}.
HELIX 288 302 {ECO:0000244|PDB:1GZ6}.
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


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Genprice Inc, Invoices and accounting
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