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 P17177

Entry ID Method Resolution Chain Position Source
AF-P17177-F1 Predicted AlphaFoldDB

No variants for P17177

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P17177

No associated diseases with P17177

1 regional properties for P17177

Type Name Position InterPro Accession
conserved_site Cytochrome P450, conserved site 473 - 482 IPR017972

Functions

Description
EC Number 1.14.15.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein
  • Post-translationally targeted to mitochondria
  • All three of the receptor proteins in the TOM complex, TOMM70, TOMM20 and TOMM22 are required for the translocation across the mitochondrial outer membrane
  • After translocation into the matrix, associates with the inner membrane as a membrane extrinsic protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.

10 GO annotations of molecular function

Name Definition
3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity Catalysis of the reaction: H2O + NAD+ + 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al = NADH + 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate.
cholestanetetraol 26-dehydrogenase activity Catalysis of the reaction: 5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NAD+ = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al + NADH.
cholestanetriol 26-monooxygenase activity Catalysis of the reaction: 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + NADPH + O2 = 5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NADP+ + H2O.
cholesterol 26-hydroxylase activity Catalysis of the hydroxylation of cholesterol at position 26 of the side chain, to produce 26-hydroxycholesterol.
cholesterol 7-alpha-monooxygenase activity Catalysis of the reaction: cholesterol + NADPH + H+ + O2 = 7-alpha-hydroxycholesterol + NADP+ + H2O.
cholesterol monooxygenase (side-chain-cleaving) activity Catalysis of the reaction: cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
Hsp70 protein binding Binding to a Hsp70 protein, heat shock proteins around 70kDa in size.
iron ion binding Binding to an iron (Fe) ion.
vitamin D3 25-hydroxylase activity Catalysis of the reaction: vitamin D3 + NADPH + H+ + O2 = calcidiol + NADP+ + H2O.

4 GO annotations of biological process

Name Definition
bile acid biosynthetic process The chemical reactions and pathways resulting in the formation of bile acids, any of a group of steroid carboxylic acids occurring in bile.
C21-steroid hormone biosynthetic process The chemical reactions and pathways resulting in the formation of C21-steroid hormones, steroid compounds containing 21 carbons which function as hormones.
calcitriol biosynthetic process from calciol Conversion of vitamin D3 from its largely inactive form (calciol, also called cholecalciferol) into a hormonally active form (calcitriol). Conversion requires 25-hydroxylation of calciol in the liver to form calcidiol, and subsequent 1,alpha-hydroxylation of calcidiol in the kidney to form calcitriol.
cholesterol catabolic process The chemical reactions and pathways resulting in the breakdown 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAALGCARLR WALLGPRVAG CGLCPQGARA KAAIPTALPA DEAAQAPGAG PGDRRRRRSL
70 80 90 100 110 120
EELPRLGQLR FFYQAFVQGY LLHLHKLQVL NKARYGPMWV SYLGPQLFVN LASAPLVETV
130 140 150 160 170 180
MRQEGKYPVR NDMQLWKEHR DHQDLAYGVF TTDGHDWYQL RQALNQRLLK PAEAALYTDA
190 200 210 220 230 240
LNEVIDSFVV RLDQLRAESA SGDQVPDMAD LLYHFALEAI CYILFEKRIG CLEASIPKDT
250 260 270 280 290 300
ENFIRSVGLM FQNSVYVTFL PKWTRPLLPF WKRYLDGWDT IFSFGKNLID QKLQEVVAQL
310 320 330 340 350 360
QSAGSDGVQV SGYLHSLLTS GQLSPREALG SLPELLLAGV DTTSNTLTWA LYHLSKNPEI
370 380 390 400 410 420
QAALRKEVVG VVAAGQVPQH KDFAHMPLLK AVLKETLRLY PVIPANSRII VDKEIEVGGF
430 440 450 460 470 480
LFPKNTQFVF CHYVTSRDPS TFSEPDTFWP YRWLRKGQPE TSKTQHPFGS VPFGYGVRAC
490 500 510 520 530
LGRRIAELEM QLLLARLIQR YELMLAPETG EVQSVARIVL VPNKKVGLRF LPTQR