P16393

PR
Gene name
HMGCR
Protein name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
Names
HMG-CoA reductase
Species
Strongylocentrotus purpuratus (Purple sea urchin)
KEGG Pathway
spu:373355
EC number
1.1.1.34: 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)

199-284 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P16393

Entry ID Method Resolution Chain Position Source
AF-P16393-F1 Predicted AlphaFoldDB

No variants for P16393

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P16393

No associated diseases with P16393

4 regional properties for P16393

Type Name Position InterPro Accession
domain Sterol-sensing domain 62 - 226 IPR000731
conserved_site Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site 662 - 676 IPR023076-1
conserved_site Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site 818 - 825 IPR023076-2
conserved_site Hydroxymethylglutaryl-CoA reductase, class I/II, conserved site 872 - 885 IPR023076-3

Functions

Description
EC Number 1.1.1.34 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Endoplasmic reticulum membrane; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
peroxisomal membrane The lipid bilayer surrounding a peroxisome.

2 GO annotations of molecular function

Name Definition
hydroxymethylglutaryl-CoA reductase (NADPH) activity Catalysis of the reaction: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

4 GO annotations of biological process

Name Definition
cholesterol biosynthetic process The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
coenzyme A metabolic process The chemical reactions and pathways involving coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester.
isoprenoid biosynthetic process The chemical reactions and pathways resulting in the formation of an isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
sterol biosynthetic process The chemical reactions and pathways resulting in the formation of sterols, steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLSRLFLAQG RFCSSHPWEV IVCTLTLTIC MLSMNYFTGL PRICGWNYEC APQVKESSLS
70 80 90 100 110 120
SDVLVMCIMR TLAVAYLYLQ FTKLRTTGSK YILGIAGLFT IFSSFLFSSA VIHLFGLELT
130 140 150 160 170 180
GLNEALPFFL LLIDLTKASA LTKFALSSTT QNEVVDNIAR GMAILGPTIT LDTVVTTLVI
190 200 210 220 230 240
SIGTMSSIRK MEVFCCFGIL SLIANYFVFM TFFPACLSLV LELSNSNKYG RPVWHLGRFA
250 260 270 280 290 300
EVLEEEEDRK PNPVVQRVKM IMRTGLVLVH AHSYWLASND TELMSRDMLY DGNLLTDKKI
310 320 330 340 350 360
DPTMPLWEFY ATRLWPPTLD YILTAILATV LASHYIFFSD LATYPEKRVS IMEGHEVVNP
370 380 390 400 410 420
GSDHEDASEV ETIGTLSSSP STSDVRVIES MTSRTQACQT DPVTASPRNS RSSSPVSSHS
430 440 450 460 470 480
VKPARFTIGS SGSGSEDEEE EVIKEEEVEW VLETELKAPR PMPELLEILN VGKGPNALTD
490 500 510 520 530 540
DEVQLLVGAK HIPAYKLENI LDNPERGVAV RRQIISKLLP ITDALEKLPY ASYDYSFVSG
550 560 570 580 590 600
ACCENVIGYM PVPVGVAGPL LLDGQEFQVP MATTEGCLVA STNRGCRALR SAGGIHSVLI
610 620 630 640 650 660
GDGMTRGPLV RLPSAQEAGA IKQWLEVPEN FAAIKERFES TSRFAKLKSI QTALAGRYMF
670 680 690 700 710 720
LRFKALTGDA MGMNMISKGT EQALHALQTM FPNIEIMSLS GNYCTDKKVA AINWIEGRGK
730 740 750 760 770 780
SVVCEATVPA HIVQQVLKTS ASALVDLNIH KNLVGSAMAG SIGGFNAHAA NIVTAIYIAT
790 800 810 820 830 840
GQDAAQNIAS SNCMTLMETR GPKGGDLYLS CTMPSIELGT VGGGTVLPPQ SACLQMMDVK
850 860 870 880 890 900
GSNIHGSGLN ASQLARIVCA TVMAGELSLM SALAAGHLVK SHMKHNRSAL NIASPLPSID
910 920 930
EVATHRRSKS VDFSALKESS AAAPGTCTAN AS