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Q7Z1V1 (CP51_TRYCC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sterol 14-alpha demethylase

Short name=Tc14DM
EC=1.14.13.70
Alternative name(s):
Cytochrome P450 51
Lanosterol 14-alpha demethylase
Gene names
Name:CYP51
ORF Names:Tc00.1047053506297.260, Tc00.1047053510101.50
OrganismTrypanosoma cruzi (strain CL Brener) [Complete proteome]
Taxonomic identifier353153 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol By similarity. Favors C4 dimethylated substrates, the substrate preference order is 24-methylenedihydrolanosterol > 24,25-dihydrolanosterol > lanosterol > obtusifoliol > norlanosterol. Ref.2 UniProtKB P0A512

Catalytic activity

A 14-alpha-methylsteroid + 3 O2 + 3 NADPH = a Delta(14)-steroid + formate + 3 NADP+ + 4 H2O. Ref.2

Cofactor

Heme group By similarity. UniProtKB P0A512

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6. UniProtKB P0A512

Subcellular location

Membrane; Single-pass membrane protein Potential.

Developmental stage

Expressed in both the insect and mammalian life-cycle stages. Ref.1

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Sterol 14-alpha demethylase
PRO_0000389527

Regions

Transmembrane1 – 2121Helical; Potential

Sites

Metal binding4221Iron (heme axial ligand) By similarity UniProtKB P0A512

Natural variations

Natural variant621D → E in allele 2. Ref.1 Ref.3
Natural variant1171A → S in allele 2. Ref.1 Ref.3
Natural variant1601E → K in allele 2. Ref.1 Ref.3

Experimental info

Mutagenesis1051I → F: Increases activity on norlanosterol and obtusifoliol. Ref.2
Sequence conflict91A → G in AAW47718. Ref.2
Sequence conflict91A → G in EAN98359. Ref.3

Secondary structure

.................................................................................. 481
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7Z1V1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: C83BA5243C959151

FASTA48154,683
        10         20         30         40         50         60 
MFIEAIVLAL TALILYSVYS VKSFNTTRPT DPPVYPVTVP FLGHIVQFGK NPLEFMQRCK 

        70         80         90        100        110        120 
RDLKSGVFTI SIGGQRVTIV GDPHEHSRFF SPRNEILSPR EVYTIMTPVF GEGVAYAAPY 

       130        140        150        160        170        180 
PRMREQLNFL AEELTIAKFQ NFVPAIQHEV RKFMAENWKE DEGVINLLED CGAMIINTAC 

       190        200        210        220        230        240 
QCLFGEDLRK RLNARHFAQL LSKMESSLIP AAVFMPWLLR LPLPQSARCR EARAELQKIL 

       250        260        270        280        290        300 
GEIIVAREKE EASKDNNTSD LLGGLLKAVY RDGTRMSLHE VCGMIVAAMF AGQHTSTITT 

       310        320        330        340        350        360 
SWSMLHLMHP KNKKWLDKLH KEIDEFPAQL NYDNVMDEMP FAERCVRESI RRDPPLLMVM 

       370        380        390        400        410        420 
RMVKAEVKVG SYVVPKGDII ACSPLLSHHD EEAFPNPRLW DPERDEKVDG AFIGFGAGVH 

       430        440        450        460        470        480 
KCIGQKFALL QVKTILATAF REYDFQLLRD EVPDPDYHTM VVGPTLNQCL VKYTRKKKLP 


S 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and analysis of Trypanosoma cruzi lanosterol 14alpha-demethylase."
Buckner F.S., Joubert B.M., Boyle S.M., Eastman R.T., Verlinde C.L.M.J., Matsuda S.P.T.
Mol. Biochem. Parasitol. 132:75-81(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 1 AND 2), DEVELOPMENTAL STAGE.
Strain: Tulahuen.
[2]"CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B' helix defines substrate preferences of sterol 14alpha-demethylase."
Lepesheva G.I., Zaitseva N.G., Nes W.D., Zhou W., Arase M., Liu J., Hill G.C., Waterman M.R.
J. Biol. Chem. 281:3577-3585(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE 1), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-105.
[3]"The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease."
El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., Anupama A., Arner E., Aslund L. expand/collapse author list , Attipoe P., Bontempi E., Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., Andersson B.
Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES 1 AND 2).
Strain: CL Brener.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY283022 Genomic DNA. Translation: AAP33131.1.
AY283023 Genomic DNA. Translation: AAP33132.1.
AY856083 Genomic DNA. Translation: AAW47718.1.
AAHK01000021 Genomic DNA. Translation: EAN99368.1.
AAHK01000058 Genomic DNA. Translation: EAN98359.1.
RefSeqXP_820210.1. XM_815117.1.
XP_821219.1. XM_816126.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WUZX-ray2.35A/B22-481[»]
2WX2X-ray2.27A/B22-481[»]
3K1OX-ray2.89A32-481[»]
3KHMX-ray2.85A32-481[»]
3KSWX-ray3.05A32-481[»]
3ZG2X-ray2.80A28-481[»]
3ZG3X-ray2.90A29-481[»]
4BY0X-ray3.10A/B32-481[»]
4H6OX-ray2.80A32-481[»]
ProteinModelPortalQ7Z1V1.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ7Z1V1.
ChEMBLCHEMBL1075110.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3552837.
3554116.
KEGGtcr:506297.260.
tcr:510101.50.

Phylogenomic databases

KOK05917.
ProtClustDBCLSZ2443033.

Enzyme and pathway databases

UniPathwayUPA00770; UER00754.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7Z1V1.

Entry information

Entry nameCP51_TRYCC
AccessionPrimary (citable) accession number: Q7Z1V1
Secondary accession number(s): Q5I4E1, Q7Z1V0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways