Skip Header

Contribute Send feedback
Read comments (?) or add your own

P51399 (LOX5_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

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 By similarity. Nucleus matrix By similarity. Nucleus membrane; Peripheral membrane protein By similarity. Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-271. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association By similarity.

Post-translational modification

Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-523 by PKA has an inhibitory effect. Phosphorylation on Ser-271 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

Initiator methionine11Removed By similarity
Chain2 – 673672Arachidonate 5-lipoxygenase
PRO_0000220694

Regions

Domain2 – 117116PLAT
Domain118 – 673556Lipoxygenase

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 binding3671Iron; catalytic By similarity
Metal binding3721Iron; catalytic By similarity
Metal binding5501Iron; catalytic By similarity
Metal binding5541Iron; catalytic By similarity
Metal binding6731Iron; via carboxylate; catalytic By similarity
Site1031Essential for stabilizing binding to COTL1 By similarity

Amino acid modifications

Modified residue2711Phosphoserine By similarity
Modified residue5231Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P51399 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A7AF63B11CDC7972

FASTA67377,873
        10         20         30         40         50         60 
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGA VDSYDVTVDE 

        70         80         90        100        110        120 
ELGEIQLVRI EKRKYWLHDD WYLKYITLKT PTDYIEFPCY RWITGEGEIV LRDGRAKLAR 

       130        140        150        160        170        180 
DDQIHILKQH RRKELEARQK QYRWMEWNPG FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN 

       190        200        210        220        230        240 
YSKAMENLFI NRFMHMFQSS WNDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC 

       250        260        270        280        290        300 
NPVLIKRCRE LPQKLPVTTE MVECSLERHL SLEQEVQEGN IFIVDYELLD GIDANKTDPC 

       310        320        330        340        350        360 
THQFLAAPIC LLYKNLANKI VPIAIQLNQA PGEKNPIFLP SDAKYDWLLA KIWVRSSDFH 

       370        380        390        400        410        420 
VHQTITHLLC THLVSEVFGI AMYRQLPAVH PIFKLLVAHV RFTIAINTKA REQLICEYGL 

       430        440        450        460        470        480 
FDKANATGGG GHVQMVQRAV QDLTYSSLCF PEAIKARGMD STEDIPYYFY RDDGLLVWEA 

       490        500        510        520        530        540 
IQSFTSEVVS IYYEDDQVVM EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT 

       550        560        570        580        590        600 
VVIFTASAQH AAVNFGQYDW CSWIPNAPPT MRAPPATAKG VVTIEQIVAT LPDRGRSCWH 

       610        620        630        640        650        660 
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMTRFRKN LEAIVNVIAE RNKNKKLPYY 

       670 
YLSPDRIPNS VAI

« Hide

References

[1]"Cloning, sequencing and expression of a 5-lipoxygenase from Syrian hamster embryo fibroblasts."
Kitzler J.W., Eling T.E.
Prostaglandins Leukot. Essent. Fatty Acids 55:269-277(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Syrian.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U43333 mRNA. Translation: AAA85257.1.

3D structure databases

ProteinModelPortalP51399.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005150.

Enzyme and pathway databases

UniPathwayUPA00877.

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.
IPR001024. LipOase_LH2.
IPR001885. LipOase_mml.
[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]
SUPFAMSSF49723. Lipase_LipOase. 1 hit.
SSF48484. Lipoxygenase. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLOX5_MESAU
AccessionPrimary (citable) accession number: P51399
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents