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P04175

- NCPR_PIG

UniProt

P04175 - NCPR_PIG

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Protein

NADPH--cytochrome P450 reductase

Gene

POR

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.

Catalytic activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.

Cofactori

Protein has several cofactor binding sites:

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi170 – 20132FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi314 – 32512FADBy similarityAdd
BLAST
Nucleotide bindingi451 – 46111FADBy similarityAdd
BLAST
Nucleotide bindingi529 – 54719NADPBy similarityAdd
BLAST
Nucleotide bindingi624 – 64017NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. NADPH-hemoprotein reductase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase (EC:1.6.2.4)
Short name:
CPR
Short name:
P450R
Gene namesi
Name:POR
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein
Note: Anchored to the ER membrane by its N-terminal hydrophobic region.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 678677NADPH--cytochrome P450 reductasePRO_0000167598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP04175.

Structurei

3D structure databases

ProteinModelPortaliP04175.
SMRiP04175. Positions 64-678.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 224145Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini279 – 521243FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG000432.
InParanoidiP04175.
KOiK00327.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04175-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDSNVDTGT TTSEMVAEEV SLFSATDMVL FSLIVGLLTY WFIFRKKKDE
60 70 80 90 100
VPEFSKIETT TSSVKDSSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK
110 120 130 140 150
DAHRYGMRGM AADPEEYDLS DLSSLPEIEN ALAVFCMATY GEGDPTDNAQ
160 170 180 190 200
DFYDWLQEAD VDLTGVKYAV FGLGNKTYEH FNAMGKYVDK RLEQLGAQRI
210 220 230 240 250
FDLGLGDDDG NLEEDFITWR EQFWPAVCEH FGVEATGEES SIRQYELVVH
260 270 280 290 300
TDMDTAVVYT GEMGRLKSYE NQKPPFDAKN PFLAVVTTNR KLNQGTERHL
310 320 330 340 350
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQLGEILGT DLDIVMSLNN
360 370 380 390 400
LDEESNKRHP FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE
410 420 430 440 450
QLRKMASSSG EGKELYLSWV VEARRHILAI LQDYPSLRPP IDHLCERLPR
460 470 480 490 500
LQARYYSIAS SSKVHPNSVH ICAVVVEYET KSGRVNKGVA TSWLRAKEPA
510 520 530 540 550
GENGRRALVP MFVRKSQFRL PFKATTPVIM VGPGTGVAPF IGFIQERAWL
560 570 580 590 600
QEQGKEVGET LLYYGCRRSD EDYLYREELA QFHAKGALTR LSVAFSREQP
610 620 630 640 650
QKVYVQHLLK RDKEHLWKLI HDGGAHIYIC GDARNMARDV QNTFCDIVAE
660 670
QGPMEHAQAV DYVKKLMTKG RYSLDVWS
Length:678
Mass (Da):76,833
Last modified:January 23, 2007 - v2
Checksum:i206079E13CA6E0A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551S → T in AAA85368. 1 PublicationCurated
Sequence conflicti164 – 1641T → S in AAA85368. 1 PublicationCurated
Sequence conflicti175 – 1751N → D AA sequence (PubMed:3098240)Curated
Sequence conflicti340 – 3401T → A AA sequence (PubMed:3098240)Curated
Sequence conflicti379 – 3791N → D AA sequence (PubMed:3098240)Curated
Sequence conflicti401 – 4011Q → E AA sequence (PubMed:3098240)Curated
Sequence conflicti447 – 4471R → L in AAA85368. 1 PublicationCurated
Sequence conflicti503 – 5031N → D AA sequence (PubMed:3098240)Curated
Sequence conflicti509 – 5091V → L AA sequence (PubMed:3099837)Curated
Sequence conflicti509 – 5091V → L AA sequence (PubMed:3098240)Curated
Sequence conflicti675 – 6751D → N AA sequence (PubMed:3098240)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33893 mRNA. Translation: AAA85368.1.
PIRiA25584. RDPGO4.
RefSeqiNP_001123431.1. NM_001129959.1.
UniGeneiSsc.50299.

Genome annotation databases

GeneIDi100170114.
KEGGissc:100170114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33893 mRNA. Translation: AAA85368.1 .
PIRi A25584. RDPGO4.
RefSeqi NP_001123431.1. NM_001129959.1.
UniGenei Ssc.50299.

3D structure databases

ProteinModelPortali P04175.
SMRi P04175. Positions 64-678.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P04175.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100170114.
KEGGi ssc:100170114.

Organism-specific databases

CTDi 5447.

Phylogenomic databases

HOVERGENi HBG000432.
InParanoidi P04175.
KOi K00327.

Family and domain databases

Gene3Di 1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000208. P450R. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Amborn J., Preiss B., Stender B., Viale M., Repp R.Z., Lampert F., Kroger M., Lumper L.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete amino acid sequence of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes."
    Haniu M., Iyanagi T., Miller P., Lee T.D., Shively J.E.
    Biochemistry 25:7906-7911(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-678, ACETYLATION AT GLY-2.
  3. "Complete structure of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase."
    Vogel F., Lumper L.
    Biochem. J. 236:871-878(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-678.

Entry informationi

Entry nameiNCPR_PIG
AccessioniPrimary (citable) accession number: P04175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3