P51660
PR
Gene name |
Hsd17b4 |
Protein name |
Peroxisomal multifunctional enzyme type 2 |
Names |
MFE-2, 17-beta-hydroxysteroid dehydrogenase 4, 17-beta-HSD 4, D-bifunctional protein, DBP, Multifunctional protein 2, MFP-2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:15488 |
EC number |
1.1.1.n12: With NAD(+) or NADP(+) as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P51660
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P51660-F1 | Predicted | AlphaFoldDB |
30 variants for P51660
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389517349 | 44 | D>E | No | EVA | |
| rs241022912 | 48 | I>V | No | EVA | |
| rs3389502052 | 63 | R>S | No | EVA | |
| rs3389450925 | 80 | E>* | No | EVA | |
| rs248567975 | 118 | I>L | No | EVA | |
| rs3389495747 | 162 | A>V | No | EVA | |
| rs3389412883 | 178 | L>V | No | EVA | |
| rs584375469 | 205 | L>M | No | EVA | |
| rs260501129 | 311 | R>H | No | EVA | |
| rs212273808 | 315 | A>T | No | EVA | |
| rs3389502953 | 318 | A>V | No | EVA | |
| rs217748587 | 325 | G>D | No | EVA | |
| rs242772089 | 331 | L>F | No | EVA | |
| rs3389460328 | 386 | M>I | No | EVA | |
| rs3389496645 | 389 | G>R | No | EVA | |
| rs3389502043 | 398 | F>L | No | EVA | |
| rs3389498991 | 428 | I>F | No | EVA | |
| rs262885593 | 438 | V>A | No | EVA | |
| rs259231322 | 460 | V>A | No | EVA | |
| rs246689710 | 460 | V>I | No | EVA | |
| rs3389511350 | 465 | S>Y | No | EVA | |
| rs3389495749 | 626 | V>M | No | EVA | |
| rs3389496663 | 646 | N>I | No | EVA | |
| rs3389496631 | 656 | G>R | No | EVA | |
| rs249545083 | 669 | S>N | No | EVA | |
| rs238729582 | 699 | F>L | No | EVA | |
| rs3408367984 | 710 | S>R | No | EVA | |
| rs3406647901 | 716 | R>G | No | EVA | |
| rs3389511396 | 723 | Q>L | No | EVA | |
| rs3389501678 | 733 | A>V | No | EVA |
No associated diseases with P51660
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.n12 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| peroxisomal matrix | The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase. |
| peroxisome | A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. |
11 GO annotations of molecular function
| Name | Definition |
|---|---|
| (3R)-hydroxyacyl-CoA dehydrogenase (NAD) activity | Catalysis of the reaction: 3R-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. |
| 17-beta-hydroxysteroid dehydrogenase (NAD+) activity | Catalysis of the reaction: a 17-beta-hydroxysteroid + NAD+ = a 17-oxosteroid + NADH + H+. |
| 3-hydroxyacyl-CoA dehydratase activity | Catalysis of the reaction: alkene-CoA + H2O = alcohol-CoA. Substrates are crotonoyl-CoA (producing 3-hydroxyacyl-CoA) and 2,3-didehydro-pimeloyl-CoA (producing 3-hydroxypimeloyl-CoA). |
| 3-hydroxyacyl-CoA dehydrogenase activity | Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H(+). |
| 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity | Catalysis of the reaction: (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O. |
| enoyl-CoA hydratase activity | Catalysis of the reaction: (3S)-3-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O. |
| estradiol 17-beta-dehydrogenase activity | Catalysis of the reaction: estradiol-17-beta + NADP+ = estrone + NADPH + H+. |
| identical protein binding | Binding to an identical protein or proteins. |
| isomerase activity | Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. |
| long-chain-enoyl-CoA hydratase activity | Catalysis of the reaction: a long-chain (3S)-3-hydroxyacyl-CoA = a long-chain trans-2-enoyl-CoA + H2O. A long-chain acyl-CoA is an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| androgen metabolic process | The chemical reactions and pathways involving androgens, C19 steroid hormones that can stimulate the development of male sexual characteristics. |
| estrogen metabolic process | The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants. |
| fatty acid beta-oxidation | A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
| medium-chain fatty-acyl-CoA metabolic process | The chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12. |
| Sertoli cell development | The process whose specific outcome is the progression of a Sertoli cell over time, from its formation to the mature structure. Cell development does not include the steps involved in committing a cell to a Sertoli cell fate. |
| very long-chain fatty acid metabolic process | The chemical reactions and pathways involving a fatty acid which has a chain length greater than C22. |
| very long-chain fatty-acyl-CoA metabolic process | The chemical reactions and pathways involving very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASPLRFDGR | VVLVTGAGGG | LGRAYALAFA | ERGALVIVND | LGGDFKGIGK | GSSAADKVVA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EIRRKGGKAV | ANYDSVEAGE | KLVKTALDTF | GRIDVVVNNA | GILRDRSFSR | ISDEDWDIIH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RVHLRGSFQV | TRAAWDHMKK | QNYGRILMTS | SASGIYGNFG | QANYSAAKLG | ILGLCNTLAI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EGRKNNIHCN | TIAPNAGSRM | TETVLPEDLV | EALKPEYVAP | LVLWLCHESC | EENGGLFEVG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AGWIGKLRWE | RTLGAIVRKR | NQPMTPEAVR | DNWEKICDFS | NASKPQTIQE | STGGIVEVLH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KVDSEGISPN | RTSHAAPAAT | SGFVGAVGHK | LPSFSSSYTE | LQSIMYALGV | GASVKNPKDL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KFVYEGSADF | SCLPTFGVIV | AQKSMMNGGL | AEVPGLSFNF | AKALHGEQYL | ELYKPLPRSG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ELKCEAVIAD | ILDKGSGVVI | VMDVYSYSGK | ELICYNQFSV | FVVGSGGFGG | KRTSEKLKAA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VAVPNRPPDA | VLRDATSLNQ | AALYRLSGDW | NPLHIDPDFA | SVAGFEKPIL | HGLCTFGFSA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RHVLQQFADN | DVSRFKAIKV | RFAKPVYPGQ | TLQTEMWKEG | NRIHFQTKVH | ETGDVVISNA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YVDLVPASGV | STQTPSEGGE | LQSALVFGEI | GRRLKSVGRE | VVKKANAVFE | WHITKGGTVA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| AKWTIDLKSG | SGEVYQGPAK | GSADVTIIIS | DEDFMEVVFG | KLDPQKAFFS | GRLKARGNIM |
| 730 | |||||
| LSQKLQMILK | DYAKL |