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P48999 (LOX5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. 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:
Arachidonate 5-lipoxygenase

Short name=5-LO
Short name=5-lipoxygenase
EC=1.13.11.34
Gene names
Name:Alox5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Arachidonate + O2 = leukotriene A4 + H2O.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 2 calcium ions per subunit By similarity.

Pathway

Lipid metabolism; leukotriene A4 biosynthesis.

Subunit structure

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

Subcellular location

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. Ref.1

Post-translational modification

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.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 674674Arachidonate 5-lipoxygenase
PRO_0000220695

Regions

Domain2 – 118117PLAT
Domain119 – 674556Lipoxygenase

Sites

Metal binding171Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding181Calcium 2; via carbonyl oxygen; structural By similarity
Metal binding191Calcium 2; structural By similarity
Metal binding441Calcium 2; structural By similarity
Metal binding451Calcium 2; via carbonyl oxygen; structural By similarity
Metal binding471Calcium 2; structural By similarity
Metal binding791Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding801Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding3681Iron; catalytic By similarity
Metal binding3731Iron; catalytic By similarity
Metal binding5511Iron; catalytic By similarity
Metal binding5551Iron; catalytic By similarity
Metal binding6741Iron; via carboxylate; catalytic By similarity
Site1031Essential for stabilizing binding to COTL1 By similarity

Amino acid modifications

Modified residue2721Phosphoserine By similarity
Modified residue5241Phosphoserine By similarity

Experimental info

Mutagenesis6721V → M: Loss of activity. Ref.1
Sequence conflict4661I → M in AAC37673. Ref.1
Sequence conflict6461V → I in AAC37673. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48999 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 130F27F9A77A3D88

FASTA67477,967
        10         20         30         40         50         60 
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA VDSYDVTVDE 

        70         80         90        100        110        120 
ELGEIYLVKI EKRKYWLHDD WYLKYITLKT PHGDYIEFPC YRWITGEGEI VLRDGRAKLA 

       130        140        150        160        170        180 
RDDQIHILKQ HRRKELEARQ KQYRWMEWNP GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL 

       190        200        210        220        230        240 
NYSKAMENLF INRFMHMFQS SWHDFADFEK IFVKISNTIS ERVKNHWQED LMFGYQFLNG 

       250        260        270        280        290        300 
CNPVLIKRCT ALPPKLPVTT EMVECSLERQ LSLEQEVQEG NIFIVDYELL DGIDANKTDP 

       310        320        330        340        350        360 
CTHQFLAAPI CLLYKNLANK IVPIAIQLNQ TPGESNPIFL PTDSKYDWLL AKIWVRSSDF 

       370        380        390        400        410        420 
HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPLFKLLVAH VRFTIAINTK AREQLICEYG 

       430        440        450        460        470        480 
LFDKANATGG GGHVQMVQRA VQDLTYSSLC FPEAIKARGM DSTEDIPFYF YRDDGLLVWE 

       490        500        510        520        530        540 
AIQSFTMEVV SIYYENDQVV EEDQELQDFV KDVYVYGMRG KKASGFPKSI KSREKLSEYL 

       550        560        570        580        590        600 
TVVIFTASAQ HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 

       610        620        630        640        650        660 
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMIRFRK NLEAIVSVIA ERNKNKKLPY 

       670 
YYLSPDRIPN SVAI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI49479.
RefSeqNP_033792.1. NM_009662.2.
UniGeneMm.41072.

3D structure databases

ProteinModelPortalP48999.
SMRP48999. Positions 2-674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198076. 1 interaction.

Chemistry

BindingDBP48999.
ChEMBLCHEMBL5211.

PTM databases

PhosphoSiteP48999.

Proteomic databases

PaxDbP48999.
PRIDEP48999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026795; ENSMUSP00000026795; ENSMUSG00000025701.
GeneID11689.
KEGGmmu:11689.
UCSCuc009dkd.1. mouse.

Organism-specific databases

CTD240.
MGIMGI:87999. Alox5.

Phylogenomic databases

eggNOGNOG69653.
GeneTreeENSGT00550000074415.
HOGENOMHOG000234358.
HOVERGENHBG005150.
InParanoidQ3TB75.
KOK00461.
OMAGIDANKT.
OrthoDBEOG7B05CG.
TreeFamTF105320.

Enzyme and pathway databases

UniPathwayUPA00877.

Gene expression databases

BgeeP48999.
CleanExMM_ALOX5.
GenevestigatorP48999.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279339.
PROP48999.
SOURCESearch...

Entry information

Entry nameLOX5_MOUSE
AccessionPrimary (citable) accession number: P48999
Secondary accession number(s): Q3TB75
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot