SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16469

- LOX15_PIG

UniProt

P16469 - LOX15_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Arachidonate 15-lipoxygenase

Gene
ALOX15
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. Beside its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.1 Publication

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.1 Publication
Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.1 Publication

Cofactori

Binds 1 iron ion per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi361 – 3611Iron; catalytic
Metal bindingi366 – 3661Iron; catalytic
Metal bindingi541 – 5411Iron; catalytic
Metal bindingi545 – 5451Iron; catalytic
Metal bindingi663 – 6631Iron; via carboxylate; catalytic By similarity

GO - Molecular functioni

  1. arachidonate 12-lipoxygenase activity Source: UniProtKB
  2. arachidonate 15-lipoxygenase activity Source: UniProtKB
  3. iron ion binding Source: UniProtKB
  4. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB

GO - Biological processi

  1. apoptotic cell clearance Source: UniProtKB
  2. arachidonic acid metabolic process Source: UniProtKB
  3. bone mineralization Source: UniProtKB
  4. cellular response to calcium ion Source: UniProtKB
  5. cellular response to interleukin-13 Source: UniProtKB
  6. linoleic acid metabolic process Source: UniProtKB
  7. lipoxin A4 biosynthetic process Source: UniProtKB
  8. lipoxygenase pathway Source: UniProtKB
  9. negative regulation of adaptive immune response Source: UniProtKB
  10. ossification Source: UniProtKB
  11. phosphatidylethanolamine biosynthetic process Source: UniProtKB
  12. positive regulation of actin filament polymerization Source: UniProtKB
  13. positive regulation of cell-substrate adhesion Source: UniProtKB
  14. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  15. regulation of engulfment of apoptotic cell Source: UniProtKB
  16. regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  17. response to endoplasmic reticulum stress Source: UniProtKB
  18. wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_208437. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_215820. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_226186. Synthesis of 12-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase (EC:1.13.11.33)
Short name:
15-LOX
Alternative name(s):
12/15-lipoxygenase
Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.31)
Short name:
12-LOX
Arachidonate omega-6 lipoxygenase
Erythroid cell-specific 15-lipoxygenase
Gene namesi
Name:ALOX15
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 12

Subcellular locationi

Cytoplasmcytosol By similarity. Cell membrane; Peripheral membrane protein By similarity. Lipid droplet By similarity
Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells By similarity.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  3. lipid particle Source: UniProtKB
  4. membrane Source: UniProtKB
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Lipid droplet, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061I → V: No effect on the stereoselectivity of the oxygenation reaction. 1 Publication
Mutagenesisi128 – 1281H → L: No specific effect on enzymatic activity and iron-binding. 1 Publication
Mutagenesisi356 – 3561H → L: No specific effect on enzymatic activity and iron-binding. 1 Publication
Mutagenesisi361 – 3611H → L or Q: Loss of enzymatic activity and iron-binding. 1 Publication
Mutagenesisi366 – 3661H → L: Loss of enzymatic activity and iron-binding. 1 Publication
Mutagenesisi384 – 3841H → L: Labile enzyme with normal enzymatic activity. 1 Publication
Mutagenesisi393 – 3931H → L: Labile enzyme with loss of enzymatic activity. 1 Publication
Mutagenesisi398 – 3981M → L: No effect on the stereoselectivity of the oxygenation reaction. 1 Publication
Mutagenesisi418 – 4181V → I: Alters the stereoselectivity of the oxygenation reaction. Changes the stereoselectivity of the oxygenation toward the production of (15S)-HPETE; when associated with M-419. 1 Publication
Mutagenesisi419 – 4191V → M: Alters the stereoselectivity of the oxygenation reaction. Changes the stereoselectivity of the oxygenation toward the production of (15S)-HPETE; when associated with I-418. 1 Publication
Mutagenesisi426 – 4261H → L: Decreased enzymatic activity without effect on iron-binding. 1 Publication
Mutagenesisi533 – 5331C → S: No specific effect on enzymatic activity and iron-binding. 1 Publication
Mutagenesisi541 – 5411H → L: Loss of enzymatic activity and iron-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 663662Arachidonate 15-lipoxygenasePRO_0000220684Add
BLAST

Proteomic databases

PaxDbiP16469.

Expressioni

Tissue specificityi

Leukocytes, pituitary gland, lung and in very small amount in jejunum and spleen.

Interactioni

Subunit structurei

Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade By similarity.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000018988.

Structurei

Secondary structure

1
663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi126 – 13914
Helixi158 – 1603
Helixi163 – 1653
Helixi169 – 19325
Helixi201 – 2077
Helixi214 – 2229
Helixi226 – 23510
Helixi259 – 27012
Beta strandi274 – 2785
Helixi280 – 2823
Beta strandi301 – 3066
Beta strandi312 – 3187
Helixi338 – 35821
Helixi359 – 3657
Helixi366 – 37914
Helixi385 – 3906
Helixi391 – 3944
Helixi397 – 40711
Helixi414 – 4185
Turni420 – 4245
Helixi425 – 43612
Helixi440 – 4423
Helixi444 – 4507
Helixi460 – 48324
Helixi487 – 4915
Helixi494 – 50512
Turni506 – 5094
Helixi512 – 5143
Helixi523 – 53715
Helixi539 – 5457
Helixi548 – 5514
Beta strandi552 – 5543
Helixi555 – 5573
Beta strandi568 – 5703
Helixi574 – 5807
Helixi584 – 59815
Helixi618 – 64326
Beta strandi645 – 6473
Turni654 – 6563
Beta strandi657 – 6604

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RDEX-ray1.89A/B/C/D112-663[»]

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 115114PLATAdd
BLAST
Domaini116 – 663548LipoxygenaseAdd
BLAST

Domaini

The PLAT domain can bind calcium ions; this promotes association with membranes By similarity.

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Phylogenomic databases

eggNOGiNOG133298.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
KOiK00460.
OMAiLTCWKDL.
OrthoDBiEOG7B05CG.
TreeFamiTF105320.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16469-1 [UniParc]FASTAAdd to Basket

« Hide

MGLYRVRVST GSSFYAGSQN QVQLWLVGQH GEAALGWCLR PARGKETEFS    50
VDVSEYLGPL LFVKLRKRHL LQDDAWFCNW ISVQGPGANG DEFRFPCYRW 100
VEGDRILSLP EGTARTVVDD PQGLFKKHRE EELAERRKLY RWGNWKDGLI 150
LNIASTGIHD LPVDERFLED KRIDFEASLA KGLADLAVKD SLNVLMSWNS 200
LDSFNRIFWC GQSKLAERVR DSWKEDALFG YQFLNGTNPM LLRHSVELPA 250
RLKFPPGMEE LQAQLEKELQ GGTLFEADFS LLDGIKANVI LCSQQYLAVP 300
LVMLKLQPDG KLLPMVIQLQ LPHEGSPLPP LFLPTDPPMV WLLAKCWVRS 350
SDFQLHELHS HLLRGHLMAE VIAVATMRCL PSIHPIFKLL IPHFRYTMEI 400
NVRARNGLVS DLGIFDQVVS TGGGGHVELL RRAAALLTYS SFCPPDDLAD 450
RGLLGVESSF YAQDALRLWE VISRYVEGIV SLHYKTDESV KEDLELQAWC 500
REFTEIGLLG AQDRGFPVSL QSKEQLCHFV TMCIFTCTGQ HSSNHLGQLD 550
WYSWVPNAPC TMRLPPPTTK DATLETVMAT LPNFHQASLQ MSITWQLGRC 600
QPTMVALGQH EEEYFSGPGP KAVLTKFREE LAALDKDIEV RNAKLALPYE 650
YLRPSRVENS VAI 663
Length:663
Mass (Da):75,004
Last modified:October 16, 2013 - v3
Checksum:i5E3864A7A3FDEF71
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti218 – 2181R → Q in AAA31068. 1 Publication
Sequence conflicti218 – 2181R → Q in BAA01471. 1 Publication
Sequence conflicti323 – 3231H → R in AAA31068. 1 Publication
Sequence conflicti323 – 3231H → R in BAA01471. 1 Publication
Sequence conflicti494 – 4941L → F in AAA31068. 1 Publication
Sequence conflicti494 – 4941L → F in BAA01471. 1 Publication
Sequence conflicti553 – 5531S → T in AAA31068. 1 Publication
Sequence conflicti553 – 5531S → T in BAA01471. 1 Publication
Sequence conflicti623 – 6231V → G in BAA01471. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31417 mRNA. Translation: AAA31068.1.
D10621 Genomic DNA. Translation: BAA01471.1.
CU972403 Genomic DNA. No translation available.
PIRiA35087.
RefSeqiNP_999096.1. NM_213931.1.
UniGeneiSsc.10974.

Genome annotation databases

EnsembliENSSSCT00000019506; ENSSSCP00000018988; ENSSSCG00000017923.
GeneIDi396971.
KEGGissc:396971.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31417 mRNA. Translation: AAA31068.1 .
D10621 Genomic DNA. Translation: BAA01471.1 .
CU972403 Genomic DNA. No translation available.
PIRi A35087.
RefSeqi NP_999096.1. NM_213931.1.
UniGenei Ssc.10974.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3RDE X-ray 1.89 A/B/C/D 112-663 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000018988.

Chemistry

BindingDBi P16469.
ChEMBLi CHEMBL2381.

Proteomic databases

PaxDbi P16469.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000019506 ; ENSSSCP00000018988 ; ENSSSCG00000017923 .
GeneIDi 396971.
KEGGi ssc:396971.

Organism-specific databases

CTDi 239.

Phylogenomic databases

eggNOGi NOG133298.
GeneTreei ENSGT00550000074415.
HOGENOMi HOG000234358.
HOVERGENi HBG005150.
KOi K00460.
OMAi LTCWKDL.
OrthoDBi EOG7B05CG.
TreeFami TF105320.

Enzyme and pathway databases

UniPathwayi UPA00881 .
Reactomei REACT_208437. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_215820. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_226186. Synthesis of 12-eicosatetraenoic acid derivatives.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
InterProi IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11771. PTHR11771. 1 hit.
Pfami PF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view ]
PRINTSi PR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes."
    Yoshimoto T., Suzuki H., Yamamoto S., Takai T., Yokoyama C., Tanabe T.
    Proc. Natl. Acad. Sci. U.S.A. 87:2142-2146(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Leukocyte.
  2. "Molecular structure and function of the porcine arachidonate 12-lipoxygenase gene."
    Arakawa T., Oshima T., Kishimoto K., Yoshimoto T., Yamamoto S.
    J. Biol. Chem. 267:12188-12191(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Porcine genome sequencing project
    Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase."
    Suzuki H., Kishimoto K., Yoshimoto T., Yamamoto S., Kanai F., Ebina Y., Miyatake A., Tanabe T.
    Biochim. Biophys. Acta 1210:308-316(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, IRON-BINDING, MUTAGENESIS OF ILE-106; HIS-128; HIS-356; HIS-361; HIS-366; HIS-384; HIS-393; MET-398; VAL-418; VAL-419; HIS-426; CYS-533 AND HIS-541.
  5. "Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis."
    Xu S., Mueser T.C., Marnett L.J., Funk M.O. Jr.
    Structure 20:1490-1497(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 112-663 IN COMPLEX WITH INHIBITOR, IRON-BINDING.

Entry informationi

Entry nameiLOX15_PIG
AccessioniPrimary (citable) accession number: P16469
Secondary accession number(s): F1RFT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 16, 2013
Last modified: September 3, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi