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Protein

Arachidonate 5-lipoxygenase

Gene

Alox5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes.1 Publication

Catalytic activityi

Arachidonate + O2 = leukotriene A4 + H2O.

Cofactori

Protein has several cofactor binding sites:
  • Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation
  • Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171Calcium 1; via carbonyl oxygen; structuralBy similarity
Metal bindingi18 – 181Calcium 2; via carbonyl oxygen; structuralBy similarity
Metal bindingi19 – 191Calcium 2; structuralBy similarity
Metal bindingi44 – 441Calcium 2; structuralBy similarity
Metal bindingi45 – 451Calcium 2; via carbonyl oxygen; structuralBy similarity
Metal bindingi47 – 471Calcium 2; structuralBy similarity
Metal bindingi79 – 791Calcium 1; via carbonyl oxygen; structuralBy similarity
Metal bindingi80 – 801Calcium 1; via carbonyl oxygen; structuralBy similarity
Sitei103 – 1031Essential for stabilizing binding to COTL1By similarity
Metal bindingi368 – 3681Iron; catalyticPROSITE-ProRule annotation
Metal bindingi373 – 3731Iron; catalyticPROSITE-ProRule annotation
Metal bindingi551 – 5511Iron; catalyticPROSITE-ProRule annotation
Metal bindingi555 – 5551Iron; catalyticPROSITE-ProRule annotation
Metal bindingi674 – 6741Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. arachidonate 5-lipoxygenase activity Source: MGI
  2. iron ion binding Source: UniProtKB

GO - Biological processi

  1. inflammatory response Source: MGI
  2. leukotriene biosynthetic process Source: MGI
  3. leukotriene metabolic process Source: MGI
  4. leukotriene production involved in inflammatory response Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Leukotriene biosynthesis

Keywords - Ligandi

Calcium, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.34. 3474.
ReactomeiREACT_280918. Synthesis of Lipoxins (LX).
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_327774. Synthesis of 5-eicosatetraenoic acids.
UniPathwayiUPA00877.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 5-lipoxygenase (EC:1.13.11.34)
Short name:
5-LO
Short name:
5-lipoxygenase
Gene namesi
Name:Alox5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:87999. Alox5.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation1 Publication. Nucleus matrix 1 Publication. Nucleus membrane By similarity; Peripheral membrane protein By similarity
Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. extracellular space Source: MGI
  4. nuclear envelope Source: MGI
  5. nuclear envelope lumen Source: UniProtKB
  6. nuclear matrix Source: MGI
  7. nuclear membrane Source: UniProtKB
  8. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi672 – 6721V → M: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 674674Arachidonate 5-lipoxygenasePRO_0000220695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei524 – 5241PhosphoserineBy similarity

Post-translational modificationi

Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-524 by PKA has an inhibitory effect. Phosphorylation on Ser-272 prevents export from the nucleus (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP48999.
PaxDbiP48999.
PRIDEiP48999.

PTM databases

PhosphoSiteiP48999.

Expressioni

Gene expression databases

BgeeiP48999.
CleanExiMM_ALOX5.
ExpressionAtlasiP48999. baseline and differential.
GenevestigatoriP48999.

Interactioni

Subunit structurei

Interacts with ALOX5AP and LTC4S. Interacts with COTL1, the interaction is required for stability and efficient catalytic activity (By similarity).By similarity

Protein-protein interaction databases

BioGridi198076. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP48999.
SMRiP48999. Positions 2-674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 118117PLATPROSITE-ProRule annotationAdd
BLAST
Domaini119 – 674556LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG69653.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP48999.
KOiK00461.
OMAiNYSKAME.
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.

P48999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA
60 70 80 90 100
VDSYDVTVDE ELGEIYLVKI EKRKYWLHDD WYLKYITLKT PHGDYIEFPC
110 120 130 140 150
YRWITGEGEI VLRDGRAKLA RDDQIHILKQ HRRKELEARQ KQYRWMEWNP
160 170 180 190 200
GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS
210 220 230 240 250
SWHDFADFEK IFVKISNTIS ERVKNHWQED LMFGYQFLNG CNPVLIKRCT
260 270 280 290 300
ALPPKLPVTT EMVECSLERQ LSLEQEVQEG NIFIVDYELL DGIDANKTDP
310 320 330 340 350
CTHQFLAAPI CLLYKNLANK IVPIAIQLNQ TPGESNPIFL PTDSKYDWLL
360 370 380 390 400
AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPLFKLLVAH
410 420 430 440 450
VRFTIAINTK AREQLICEYG LFDKANATGG GGHVQMVQRA VQDLTYSSLC
460 470 480 490 500
FPEAIKARGM DSTEDIPFYF YRDDGLLVWE AIQSFTMEVV SIYYENDQVV
510 520 530 540 550
EEDQELQDFV KDVYVYGMRG KKASGFPKSI KSREKLSEYL TVVIFTASAQ
560 570 580 590 600
HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW
610 620 630 640 650
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMIRFRK NLEAIVSVIA
660 670
ERNKNKKLPY YYLSPDRIPN SVAI
Length:674
Mass (Da):77,967
Last modified:July 27, 2011 - v3
Checksum:i130F27F9A77A3D88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti466 – 4661I → M in AAC37673 (PubMed:7629107).Curated
Sequence conflicti646 – 6461V → I in AAC37673 (PubMed:7629107).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42198 mRNA. Translation: AAC37673.1.
AK137481 mRNA. Translation: BAE23373.1.
AK171413 mRNA. Translation: BAE42439.1.
BC139102 mRNA. Translation: AAI39103.1.
BC141213 mRNA. Translation: AAI41214.1.
CCDSiCCDS20452.1.
PIRiI49479.
RefSeqiNP_033792.1. NM_009662.2.
UniGeneiMm.41072.

Genome annotation databases

EnsembliENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701.
GeneIDi11689.
KEGGimmu:11689.
UCSCiuc009dkd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42198 mRNA. Translation: AAC37673.1.
AK137481 mRNA. Translation: BAE23373.1.
AK171413 mRNA. Translation: BAE42439.1.
BC139102 mRNA. Translation: AAI39103.1.
BC141213 mRNA. Translation: AAI41214.1.
CCDSiCCDS20452.1.
PIRiI49479.
RefSeqiNP_033792.1. NM_009662.2.
UniGeneiMm.41072.

3D structure databases

ProteinModelPortaliP48999.
SMRiP48999. Positions 2-674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198076. 1 interaction.

Chemistry

BindingDBiP48999.
ChEMBLiCHEMBL5211.

PTM databases

PhosphoSiteiP48999.

Proteomic databases

MaxQBiP48999.
PaxDbiP48999.
PRIDEiP48999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701.
GeneIDi11689.
KEGGimmu:11689.
UCSCiuc009dkd.1. mouse.

Organism-specific databases

CTDi240.
MGIiMGI:87999. Alox5.

Phylogenomic databases

eggNOGiNOG69653.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP48999.
KOiK00461.
OMAiNYSKAME.
OrthoDBiEOG7B05CG.
TreeFamiTF105320.

Enzyme and pathway databases

UniPathwayiUPA00877.
BRENDAi1.13.11.34. 3474.
ReactomeiREACT_280918. Synthesis of Lipoxins (LX).
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_327774. Synthesis of 5-eicosatetraenoic acids.

Miscellaneous databases

NextBioi279339.
PROiP48999.
SOURCEiSearch...

Gene expression databases

BgeeiP48999.
CleanExiMM_ALOX5.
ExpressionAtlasiP48999. baseline and differential.
GenevestigatoriP48999.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, expression, mutagenesis, intracellular localization, and gene chromosomal assignment of mouse 5-lipoxygenase."
    Chen X.-S., Naumann T.A., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.
    J. Biol. Chem. 270:17993-17999(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-672.
    Strain: C57BL/6 X 129/Sv.
    Tissue: Peritoneal cavity.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiLOX5_MOUSE
AccessioniPrimary (citable) accession number: P48999
Secondary accession number(s): Q3TB75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.