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Q9HBI6

- CP4FB_HUMAN

UniProt

Q9HBI6 - CP4FB_HUMAN

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Protein

Phylloquinone omega-hydroxylase CYP4F11

Gene

CYP4F11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Omega-hydroxylase that oxidizes a variety of structurally unrelated compounds, including fatty acids and xenobiotics. Plays a key role in vitamin K catabolism by mediating omega-hydroxylation of vitamin K1 (phylloquinone), and menaquinone-4 (MK-4), a form of vitamin K2. Hydroxylation of phylloquinone and MK-4 probably regulates blood coagulation (PubMed:24138531). Catalyzes omega-hydroxylation of 3-hydroxy fatty acids, such as 3-hydroxypalmitate, 3-hydroxyoleate, 3-hydroxyarachidonate, and 3-hydroxystearate (PubMed:18065749, PubMed:19932081). Oxidizes drugs such as erythromycin, benzphetamine, ethylmorphine, chlorpromazine and imipramine (PubMed:15364545).4 Publications

Catalytic activityi

Phylloquinone + NADPH + O2 = omega-hydroxyphylloquinone + NADP+ + H2O.1 Publication

Cofactori

hemeBy similarity

Kineticsi

kcat is 0.088 min(-1) with menaquinone-4 (MK-4) as substrate1 Publication

  1. KM=53.5 mM for 3-hydroxystearate1 Publication
  2. KM=105.8 mM for 3-hydroxypalmitate1 Publication
  3. KM=2.4 µM for menaquinone-4 (MK-4)1 Publication
  4. KM=125 µM for erythromycin1 Publication

Vmax=830 pmol/min/ng enzyme with erythromycin as substrate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei328 – 3281Heme (covalent; via 1 link)By similarity
Metal bindingi468 – 4681Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. aromatase activity Source: UniProtKB-EC
  2. heme binding Source: UniProtKB
  3. iron ion binding Source: InterPro
  4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: UniProtKB
  2. inflammatory response Source: UniProtKB
  3. menaquinone catabolic process Source: UniProtKB
  4. oxidation-reduction process Source: UniProtKB
  5. phylloquinone catabolic process Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  7. vitamin K catabolic process Source: UniProtKB
  8. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiREACT_13425. Miscellaneous substrates.
REACT_13645. Eicosanoids.
REACT_13814. Fatty acids.
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
UniPathwayiUPA01054.

Names & Taxonomyi

Protein namesi
Recommended name:
Phylloquinone omega-hydroxylase CYP4F11Curated (EC:1.14.13.1941 Publication)
Alternative name(s):
3-hydroxy fatty acids omega-hydroxylase CYP4F11Curated (EC:1.14.13.-Curated)
Cytochrome P450 4F11
Short name:
CYPIVF11
Gene namesi
Name:CYP4F11Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:13265. CYP4F11.

Subcellular locationi

Microsome membrane 1 Publication; Single-pass membrane protein Curated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei15 – 3723HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27120.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Phylloquinone omega-hydroxylase CYP4F11PRO_0000051856Add
BLAST

Proteomic databases

MaxQBiQ9HBI6.
PaxDbiQ9HBI6.
PRIDEiQ9HBI6.

PTM databases

PhosphoSiteiQ9HBI6.

Expressioni

Tissue specificityi

Expressed mainly in human liver, followed by kidney, heart, and skeletal muscle.2 Publications

Gene expression databases

BgeeiQ9HBI6.
CleanExiHS_CYP4F11.
ExpressionAtlasiQ9HBI6. baseline and differential.
GenevestigatoriQ9HBI6.

Organism-specific databases

HPAiHPA017265.

Interactioni

Protein-protein interaction databases

BioGridi121790. 2 interactions.
IntActiQ9HBI6. 1 interaction.
STRINGi9606.ENSP00000248041.

Structurei

3D structure databases

ProteinModelPortaliQ9HBI6.
SMRiQ9HBI6. Positions 97-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118816.
HOGENOMiHOG000233833.
HOVERGENiHBG000182.
InParanoidiQ9HBI6.
KOiK17729.
OMAiEPLGANS.
PhylomeDBiQ9HBI6.
TreeFamiTF105088.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HBI6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPQLSLSWLG LGPVAASPWL LLLLVGGSWL LARVLAWTYT FYDNCRRLQC
60 70 80 90 100
FPQPPKQNWF WGHQGLVTPT EEGMKTLTQL VTTYPQGFKL WLGPTFPLLI
110 120 130 140 150
LCHPDIIRPI TSASAAVAPK DMIFYGFLKP WLGDGLLLSG GDKWSRHRRM
160 170 180 190 200
LTPAFHFNIL KPYMKIFNKS VNIMHDKWQR LASEGSARLD MFEHISLMTL
210 220 230 240 250
DSLQKCVFSF ESNCQEKPSE YIAAILELSA FVEKRNQQIL LHTDFLYYLT
260 270 280 290 300
PDGQRFRRAC HLVHDFTDAV IQERRCTLPT QGIDDFLKNK AKSKTLDFID
310 320 330 340 350
VLLLSKDEDG KELSDEDIRA EADTFMFEGH DTTASGLSWV LYHLAKHPEY
360 370 380 390 400
QEQCRQEVQE LLKDREPIEI EWDDLAQLPF LTMCIKESLR LHPPVPVISR
410 420 430 440 450
CCTQDFVLPD GRVIPKGIVC LINIIGIHYN PTVWPDPEVY DPFRFDQENI
460 470 480 490 500
KERSPLAFIP FSAGPRNCIG QAFAMAEMKV VLALTLLHFR ILPTHTEPRR
510 520
KPELILRAEG GLWLRVEPLG ANSQ
Length:524
Mass (Da):60,146
Last modified:May 18, 2010 - v3
Checksum:i8B0F14C52E657CB2
GO

Sequence cautioni

The sequence AAC27731.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti458 – 4581F → L in BAF82113. (PubMed:14702039)Curated
Sequence conflicti496 – 4961T → I in AAG15889. (PubMed:10964514)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461R → C.
Corresponds to variant rs57519667 [ dbSNP | Ensembl ].
VAR_060265
Natural varianti276 – 2761C → R.2 Publications
Corresponds to variant rs8104361 [ dbSNP | Ensembl ].
VAR_060266
Natural varianti446 – 4461D → N Common polymorphism; does not affect enzyme activity. 4 Publications
Corresponds to variant rs1060463 [ dbSNP | Ensembl ].
VAR_071198

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236085 mRNA. Translation: AAG15889.1.
AK289424 mRNA. Translation: BAF82113.1.
AC005336 Genomic DNA. Translation: AAC27731.1. Sequence problems.
AC020950 Genomic DNA. No translation available.
AC011517 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84512.1.
CH471106 Genomic DNA. Translation: EAW84513.1.
BC016853 mRNA. Translation: AAH16853.1.
CCDSiCCDS12337.1.
RefSeqiNP_001122404.1. NM_001128932.1.
NP_067010.3. NM_021187.3.
UniGeneiHs.187393.

Genome annotation databases

EnsembliENST00000248041; ENSP00000248041; ENSG00000171903.
ENST00000402119; ENSP00000384588; ENSG00000171903.
GeneIDi57834.
KEGGihsa:57834.
UCSCiuc002nbt.2. human.

Polymorphism databases

DMDMi296439388.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236085 mRNA. Translation: AAG15889.1 .
AK289424 mRNA. Translation: BAF82113.1 .
AC005336 Genomic DNA. Translation: AAC27731.1 . Sequence problems.
AC020950 Genomic DNA. No translation available.
AC011517 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84512.1 .
CH471106 Genomic DNA. Translation: EAW84513.1 .
BC016853 mRNA. Translation: AAH16853.1 .
CCDSi CCDS12337.1.
RefSeqi NP_001122404.1. NM_001128932.1.
NP_067010.3. NM_021187.3.
UniGenei Hs.187393.

3D structure databases

ProteinModelPortali Q9HBI6.
SMRi Q9HBI6. Positions 97-510.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121790. 2 interactions.
IntActi Q9HBI6. 1 interaction.
STRINGi 9606.ENSP00000248041.

PTM databases

PhosphoSitei Q9HBI6.

Polymorphism databases

DMDMi 296439388.

Proteomic databases

MaxQBi Q9HBI6.
PaxDbi Q9HBI6.
PRIDEi Q9HBI6.

Protocols and materials databases

DNASUi 57834.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248041 ; ENSP00000248041 ; ENSG00000171903 .
ENST00000402119 ; ENSP00000384588 ; ENSG00000171903 .
GeneIDi 57834.
KEGGi hsa:57834.
UCSCi uc002nbt.2. human.

Organism-specific databases

CTDi 57834.
GeneCardsi GC19M016023.
H-InvDB HIX0014857.
HGNCi HGNC:13265. CYP4F11.
HPAi HPA017265.
MIMi 611517. gene.
neXtProti NX_Q9HBI6.
PharmGKBi PA27120.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000118816.
HOGENOMi HOG000233833.
HOVERGENi HBG000182.
InParanoidi Q9HBI6.
KOi K17729.
OMAi EPLGANS.
PhylomeDBi Q9HBI6.
TreeFami TF105088.

Enzyme and pathway databases

UniPathwayi UPA01054 .
Reactomei REACT_13425. Miscellaneous substrates.
REACT_13645. Eicosanoids.
REACT_13814. Fatty acids.
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Miscellaneous databases

GeneWikii CYP4F11.
GenomeRNAii 57834.
NextBioi 64827.
PROi Q9HBI6.
SOURCEi Search...

Gene expression databases

Bgeei Q9HBI6.
CleanExi HS_CYP4F11.
ExpressionAtlasi Q9HBI6. baseline and differential.
Genevestigatori Q9HBI6.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human cytochrome P450 4F isoform (CYP4F11): cDNA cloning, expression, and genomic structural characterization."
    Cui X., Nelson D.R., Strobel H.W.
    Genomics 68:161-166(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-276 AND ASN-446.
    Tissue: Brain and Liver.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-276 AND ASN-446.
    Tissue: Mammary glandImported.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-276.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-276 AND ASN-446.
    Tissue: Colon.
  6. "Expression and characterization of human cytochrome P450 4F11: Putative role in the metabolism of therapeutic drugs and eicosanoids."
    Kalsotra A., Turman C.M., Kikuta Y., Strobel H.W.
    Toxicol. Appl. Pharmacol. 199:295-304(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Omega oxidation of 3-hydroxy fatty acids by the human CYP4F gene subfamily enzyme CYP4F11."
    Dhar M., Sepkovic D.W., Hirani V., Magnusson R.P., Lasker J.M.
    J. Lipid Res. 49:612-624(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
  8. "Human cytochrome P450 4F11: heterologous expression in bacteria, purification, and characterization of catalytic function."
    Tang Z., Salamanca-Pinzon S.G., Wu Z.L., Xiao Y., Guengerich F.P.
    Arch. Biochem. Biophys. 494:86-93(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Cytochrome P450-dependent catabolism of vitamin K: omega-hydroxylation catalyzed by human CYP4F2 and CYP4F11."
    Edson K.Z., Prasad B., Unadkat J.D., Suhara Y., Okano T., Guengerich F.P., Rettie A.E.
    Biochemistry 52:8276-8285(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, PATHWAY, CHARACTERIZATION OF VARIANT ASN-446.

Entry informationi

Entry nameiCP4FB_HUMAN
AccessioniPrimary (citable) accession number: Q9HBI6
Secondary accession number(s): A0A024R7G0
, A8K059, O75254, Q96AQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3