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P48999

- LOX5_MOUSE

UniProt

P48999 - LOX5_MOUSE

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Protein
Arachidonate 5-lipoxygenase
Gene
Alox5
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Binds 1 iron ion per subunit By similarity.
Binds 2 calcium ions per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171Calcium 1; via carbonyl oxygen; structural By similarity
Metal bindingi18 – 181Calcium 2; via carbonyl oxygen; structural By similarity
Metal bindingi19 – 191Calcium 2; structural By similarity
Metal bindingi44 – 441Calcium 2; structural By similarity
Metal bindingi45 – 451Calcium 2; via carbonyl oxygen; structural By similarity
Metal bindingi47 – 471Calcium 2; structural By similarity
Metal bindingi79 – 791Calcium 1; via carbonyl oxygen; structural By similarity
Metal bindingi80 – 801Calcium 1; via carbonyl oxygen; structural By similarity
Sitei103 – 1031Essential for stabilizing binding to COTL1 By similarity
Metal bindingi368 – 3681Iron; catalytic By similarity
Metal bindingi373 – 3731Iron; catalytic By similarity
Metal bindingi551 – 5511Iron; catalytic By similarity
Metal bindingi555 – 5551Iron; catalytic By similarity
Metal bindingi674 – 6741Iron; via carboxylate; catalytic By similarity

GO - Molecular functioni

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

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

ReactomeiREACT_196544. Synthesis of Lipoxins (LX).
REACT_206751. Synthesis of 5-eicosatetraenoic acids.
REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).
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: Chromosome 6

Organism-specific databases

MGIiMGI:87999. Alox5.

Subcellular locationi

Cytoplasm. Nucleus matrix. Nucleus membrane; 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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. nuclear envelope lumen Source: UniProtKB
  4. nuclear matrix Source: UniProtKB-SubCell
  5. nuclear membrane Source: UniProtKB
  6. 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-lipoxygenase
PRO_0000220695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721Phosphoserine By similarity
Modified residuei524 – 5241Phosphoserine By 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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP48999.
PaxDbiP48999.
PRIDEiP48999.

PTM databases

PhosphoSiteiP48999.

Expressioni

Gene expression databases

BgeeiP48999.
CleanExiMM_ALOX5.
GenevestigatoriP48999.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi198076. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP48999.
SMRiP48999. Positions 2-674.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 118117PLAT
Add
BLAST
Domaini119 – 674556Lipoxygenase
Add
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Phylogenomic databases

eggNOGiNOG69653.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiQ3TB75.
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

MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA    50
VDSYDVTVDE ELGEIYLVKI EKRKYWLHDD WYLKYITLKT PHGDYIEFPC 100
YRWITGEGEI VLRDGRAKLA RDDQIHILKQ HRRKELEARQ KQYRWMEWNP 150
GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS 200
SWHDFADFEK IFVKISNTIS ERVKNHWQED LMFGYQFLNG CNPVLIKRCT 250
ALPPKLPVTT EMVECSLERQ LSLEQEVQEG NIFIVDYELL DGIDANKTDP 300
CTHQFLAAPI CLLYKNLANK IVPIAIQLNQ TPGESNPIFL PTDSKYDWLL 350
AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPLFKLLVAH 400
VRFTIAINTK AREQLICEYG LFDKANATGG GGHVQMVQRA VQDLTYSSLC 450
FPEAIKARGM DSTEDIPFYF YRDDGLLVWE AIQSFTMEVV SIYYENDQVV 500
EEDQELQDFV KDVYVYGMRG KKASGFPKSI KSREKLSEYL TVVIFTASAQ 550
HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 600
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMIRFRK NLEAIVSVIA 650
ERNKNKKLPY YYLSPDRIPN SVAI 674
Length:674
Mass (Da):77,967
Last modified:July 27, 2011 - v3
Checksum:i130F27F9A77A3D88
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti466 – 4661I → M in AAC37673. 1 Publication
Sequence conflicti646 – 6461V → I in AAC37673. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS20452.1.
PIRi I49479.
RefSeqi NP_033792.1. NM_009662.2.
UniGenei Mm.41072.

3D structure databases

ProteinModelPortali P48999.
SMRi P48999. Positions 2-674.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198076. 1 interaction.

Chemistry

BindingDBi P48999.
ChEMBLi CHEMBL5211.

PTM databases

PhosphoSitei P48999.

Proteomic databases

MaxQBi P48999.
PaxDbi P48999.
PRIDEi P48999.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026795 ; ENSMUSP00000026795 ; ENSMUSG00000025701 .
GeneIDi 11689.
KEGGi mmu:11689.
UCSCi uc009dkd.1. mouse.

Organism-specific databases

CTDi 240.
MGIi MGI:87999. Alox5.

Phylogenomic databases

eggNOGi NOG69653.
GeneTreei ENSGT00550000074415.
HOGENOMi HOG000234358.
HOVERGENi HBG005150.
InParanoidi Q3TB75.
KOi K00461.
OMAi NYSKAME.
OrthoDBi EOG7B05CG.
TreeFami TF105320.

Enzyme and pathway databases

UniPathwayi UPA00877 .
Reactomei REACT_196544. Synthesis of Lipoxins (LX).
REACT_206751. Synthesis of 5-eicosatetraenoic acids.
REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Miscellaneous databases

NextBioi 279339.
PROi P48999.
SOURCEi Search...

Gene expression databases

Bgeei P48999.
CleanExi MM_ALOX5.
Genevestigatori P48999.

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. "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(1995) [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(2005) [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(2004) [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: September 3, 2014
This is version 121 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

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