Arachidonate 5-lipoxygenase - Rattus norvegicus (Rat)

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P12527 (LOX5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Arachidonate 5-lipoxygenase
Short name=5-LO
Short name=5-lipoxygenase
EC=1.13.11.34

Gene names

Name:

Alox5

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. Nucleus matrix. Nucleus membrane; Peripheral membrane protein. 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.
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 caution	The sequence AAA41538.1 differs from that shown. Reason: Frameshift at position 667.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm Membrane Nucleus
Ligand	Calcium Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute inflammatory response Inferred from mutant phenotype PubMed 20204486. Source: RGD arachidonic acid metabolic process Inferred from mutant phenotype PubMed 15107407. Source: RGD leukotriene biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB lipoxygenase pathway Inferred from mutant phenotype PubMed 15107407. Source: RGD positive regulation of vasoconstriction Inferred from mutant phenotype PubMed 16331105. Source: RGD response to hyperoxia Inferred from expression pattern PubMed 12490039. Source: RGD response to nutrient Inferred from expression pattern PubMed 16956363. Source: RGD sensory perception of pain Inferred from mutant phenotype PubMed 19580807. Source: RGD
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from direct assay PubMed 16606359. Source: RGD nuclear envelope lumen Inferred from sequence or structural similarity. Source: UniProtKB nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear membrane Inferred from sequence or structural similarity. Source: UniProtKB sarcolemma Inferred from direct assay PubMed 15107407. Source: RGD
Molecular_function	arachidonate 5-lipoxygenase activity Inferred from mutant phenotype PubMed 15107407. Source: RGD iron ion binding Inferred from sequence or structural similarity. Source: UniProtKB lipoxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 673

672

Arachidonate 5-lipoxygenase

PRO_0000220696

Regions

Domain

2 – 117

116

PLAT

Domain

118 – 673

556

Lipoxygenase

Sites

Metal binding

Calcium 1; via carbonyl oxygen; structural By similarity

Metal binding

Calcium 2; via carbonyl oxygen; structural By similarity

Metal binding

Calcium 2; structural By similarity

Metal binding

Calcium 2; structural By similarity

Metal binding

Calcium 2; via carbonyl oxygen; structural By similarity

Metal binding

Calcium 2; structural By similarity

Metal binding

Calcium 1; via carbonyl oxygen; structural By similarity

Metal binding

Calcium 1; via carbonyl oxygen; structural By similarity

Metal binding

367

Iron; catalytic By similarity

Metal binding

372

Iron; catalytic By similarity

Metal binding

550

Iron; catalytic By similarity

Metal binding

554

Iron; catalytic By similarity

Metal binding

673

Iron; via carboxylate; catalytic By similarity

Site

103

Essential for stabilizing binding to COTL1 By similarity

Amino acid modifications

Modified residue

271

Phosphoserine By similarity

Modified residue

523

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P12527 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 536B0BC27CB0A608
Show »

FASTA

673

78,087

        10         20         30         40         50         60 
MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGG RDSYDVTVDE 

        70         80         90        100        110        120 
ELGEIYLVKI EKRKYRLHDD WYLKYITLKT PHDYIEFPCY RWITGEGEIV LRDGCAKLAR 

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

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

       250        260        270        280        290        300 
NPVLIKRCTE LPKKLPVTTE MVECSLERQL SLEQEVQEGN IFIVDYELLD GIDANKTDPC 

       310        320        330        340        350        360 
THQFLAAPIC LLYKNLANKI VPIAIQLNQT PGEKNPIFLP TDSKYDWLLA KIWVRSSDFH 

       370        380        390        400        410        420 
IHQTITHLLR THLVSEVFGI AMYRQLPAVH PLFKLLVAHV RFTIAINTKA REQLNCEYGL 

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

       490        500        510        520        530        540 
IQSFTTEVVS IYYEDDQVVE EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT 

       550        560        570        580        590        600 
VVIFTASAQH AAVNFGQYDW CSWIPNAPPT MRAPPPTAKG VVTIEQIVDT LPDRGRSCWH 

       610        620        630        640        650        660 
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMIRFRKN LEAIVSVIAE RNKNKKLPYY 

       670 
YLSPDRIPNS VAI

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References

[1]	"Isolation and characterization of a cDNA clone encoding rat 5-lipoxygenase." Balcarek J.M., Theisen T.W., Cook M.N., Varrichio A., Hwang S.-M., Strohsacker M.W., Crooke S.T. J. Biol. Chem. 263:13937-13941(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1." Minor W., Steczko J., Bolin J.T., Otwinowski Z., Axelrod B. Biochemistry 32:6320-6323(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 667-670.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03960 mRNA. Translation: AAA41538.1. Frameshift.
IPI	IPI00194785.
PIR	A30882.
RefSeq	NP_036954.1. NM_012822.1.
UniGene	Rn.9662.
3D structure databases
ProteinModelPortal	P12527.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48659N.
STRING	10116.ENSRNOP00000017633.
PTM databases
PhosphoSite	P12527.
Proteomic databases
PRIDE	P12527.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25290.
KEGG	rno:25290.
UCSC	RGD:2096. rat.
Organism-specific databases
CTD	240.
RGD	2096. Alox5.
Phylogenomic databases
eggNOG	NOG69653.
HOGENOM	HOG000234358.
HOVERGEN	HBG005150.
InParanoid	P12527.
KO	K00461.
OrthoDB	EOG46Q6S3.
Enzyme and pathway databases
UniPathway	UPA00877.
Gene expression databases
ArrayExpress	P12527.
Genevestigator	P12527.
GermOnline	ENSRNOG00000012972. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. IPR001024. LipOase_LH2. IPR001885. LipOase_mml. [Graphical view]
PANTHER	PTHR11771. PTHR11771. 1 hit.
Pfam	PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PRINTS	PR00087. LIPOXYGENASE. PR00467. MAMLPOXGNASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
SUPFAM	SSF49723. Lipase_LipOase. 1 hit. SSF48484. Lipoxygenase. 1 hit.
PROSITE	PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P12527.
ChEMBL	CHEMBL312.
NextBio	606033.

Entry information

Entry name

LOX5_RAT

Accession

Primary (citable) accession number: P12527

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents