NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8913347 [NCBI, ExPASy, EBI, Israel, Japan]
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).

[2]

X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-319 IN COMPLEX WITH NAD, AND HOMODIMERIZATION.
DOI=10.1016/S0969-2126(02)00931-0; PubMed=12517343 [NCBI, ExPASy, EBI, Israel, Japan]
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).

Comments

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 (By similarity).
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 + H₂O.
CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH.
PATHWAY: Lipid metabolism; fatty acid beta-oxidation .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Peroxisome (By similarity).
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.
SIMILARITY: Contains 1 SCP2 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S83279; AAB49519.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_077368.2; -.

UniGene

Rn.2082

3D structure databases

PDB

1GZ6; X-ray; 2.38 A; A/B/C/D=1-319.

[ExPASy / RCSB / EBI]

PDBsum

1GZ6; -.

SMR

P97852; 321-603, 322-604, 620-734, 621-735.

ModBase

P97852.

Organism-specific databases

RGD

621806; Hsd17b4.

Gene expression databases

ArrayExpress

P97852; -.

GermOnline

ENSRNOG00000015840; Rattus norvegicus.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from direct assay from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR002539; MaoC_deHydtase.
IPR016040; NAD(P)-bd.
IPR003033; SCP2_sterol_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
PF01575; MaoC_dehydratas; 1.
PF02036; SCP2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; FALSE_NEG.

Genome annotation databases

Ensembl

ENSRNOG00000015840; Rattus norvegicus. [Contig view]

GeneID

79244; -.

KEGG

rno:79244; -.

Phylogenomic databases

HOVERGEN

P97852; -.

Other

NextBio

614694; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; NAD; Oxidoreductase; Peroxisome; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 735`	`734`	`Peroxisomal multifunctional enzyme type 2.`	`PRO_0000054585`
`DOMAIN`	`623 735`	`113`	`SCP2.`
`NP_BIND`	`16 40`	`25`	`NAD.`
`NP_BIND`	`75 76`	`2`	`NAD (By similarity).`
`NP_BIND`	`164 168`	`5`	`NAD (By similarity).`
`NP_BIND`	`196 199`	`4`	`NAD (By similarity).`
`REGION`	`2 305`	`304`	`3-hydroxyacyl-CoA dehydrogenase.`
`REGION`	`321 621`	`301`	`3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase.`
`ACT_SITE`	`164 164`		`Proton acceptor.`
`BINDING`	`21 21`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`40 40`		`NAD (By similarity).`
`BINDING`	`99 99`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`151 151`		`Substrate.`
`BINDING`	`705 705`		`Substrate (By similarity).`
`BINDING`	`723 723`		`Substrate (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`3 3`		`Phosphoserine (By similarity).`
`MOD_RES`	`308 308`		`Phosphoserine (By similarity).`
`MOD_RES`	`662 662`		`N6-acetyllysine (By similarity).`
`STRAND`	`11 14`	`4`
`TURN`	`15 18`	`4`
`HELIX`	`20 31`	`12`
`STRAND`	`35 39`	`5`
`HELIX`	`53 64`	`12`
`STRAND`	`68 72`	`5`
`HELIX`	`76 78`	`3`
`HELIX`	`79 89`	`11`
`STRAND`	`95 98`	`4`
`HELIX`	`108 110`	`3`
`HELIX`	`113 141`	`29`
`STRAND`	`144 149`	`6`
`HELIX`	`152 156`	`5`
`HELIX`	`162 181`	`20`
`HELIX`	`183 185`	`3`
`STRAND`	`187 195`	`9`
`TURN`	`199 201`	`3`
`HELIX`	`202 204`	`3`
`HELIX`	`207 212`	`6`
`HELIX`	`215 217`	`3`
`HELIX`	`219 225`	`7`
`STRAND`	`236 240`	`5`
`STRAND`	`243 251`	`9`
`HELIX`	`266 271`	`6`
`HELIX`	`273 276`	`4`
`HELIX`	`288 302`	`15`

Sequence information

Length: 735 AA [This is the length of the unprocessed precursor]

Molecular weight: 79428 Da [This is the MW of the unprocessed precursor]

CRC64: E14F15FFD35FC7D8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSSAADKVVE 

        70         80         90        100        110        120 
EIRRRGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA GILRDRSFSR ISDEDWDIIQ 

       130        140        150        160        170        180 
RVHLRGSFQV TRAAWDHMKK QNYGRIIMTA SASGIYGNFG QANYSAAKLG LLGLANTLVI 

       190        200        210        220        230        240 
EGRKNNIHCN TIAPNAGSRM TETVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG 

       250        260        270        280        290        300 
AGWIGKLRWE RTLGAIVRKR NQPMTPEAVR DNWVKICDFS NASKPKSIQE STGGIIEVLH 

       310        320        330        340        350        360 
KIDSEGISQN HTGQVASADA SGFAGVVGHK LPSFSSSYTE LQCIMYALGV GASVKNPKDL 

       370        380        390        400        410        420 
KFVYEGSADF SCLPTFGVIV AQKSLMSGGL AEVPGLSINF AKVLHGEQYL ELYKPLPRSG 

       430        440        450        460        470        480 
ELKCEAVIAD ILDKGSGIVI VMDVYSYSGK ELICYNQFSV FVVGSGGFGG KRTSEKLKAA 

       490        500        510        520        530        540 
VAVPSRPPDA VLRDTTSLNQ AALYRLSGDS NPLHIDPSFA SIAGFEKPIL HGLCTFGFSA 

       550        560        570        580        590        600 
RHVLQQFADN DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVQ ETGDIVISNA 

       610        620        630        640        650        660 
YVDLVPTSGV SAQTPSEGGA LQSALVFGEI GRRLKDVGRE VVKKVNAVFE WHITKNGNVA 

       670        680        690        700        710        720 
AKWTIDLKNG SGEVYQGPAK GSADTTITIS DEDFMEVVLG KLNPQNAFFS GRLKARGNIM 

       730 
LSQKLQMILK DYAKL

P97852 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools