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P12527

- LOX5_RAT

UniProt

P12527 - LOX5_RAT

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Protein

Arachidonate 5-lipoxygenase

Gene
Alox5
Organism
Rattus norvegicus (Rat)
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.

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 bindingi367 – 3671Iron; catalytic By similarity
Metal bindingi372 – 3721Iron; catalytic By similarity
Metal bindingi550 – 5501Iron; catalytic By similarity
Metal bindingi554 – 5541Iron; catalytic By similarity
Metal bindingi673 – 6731Iron; via carboxylate; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. acute inflammatory response Source: RGD
  2. arachidonic acid metabolic process Source: RGD
  3. leukotriene biosynthetic process Source: UniProtKB
  4. lipoxygenase pathway Source: RGD
  5. positive regulation of vasoconstriction Source: RGD
  6. response to hyperoxia Source: RGD
  7. response to nutrient Source: RGD
  8. sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Leukotriene biosynthesis

Keywords - Ligandi

Calcium, Iron, Metal-binding

Enzyme and pathway databases

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2096. Alox5.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. dendrite Source: RGD
  3. nuclear envelope Source: RGD
  4. nuclear envelope lumen Source: UniProtKB
  5. nuclear matrix Source: UniProtKB-SubCell
  6. nuclear membrane Source: UniProtKB
  7. nucleus Source: RGD
  8. sarcolemma Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Arachidonate 5-lipoxygenasePRO_0000220696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711Phosphoserine By similarity
Modified residuei523 – 5231Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP12527.

PTM databases

PhosphoSiteiP12527.

Expressioni

Gene expression databases

GenevestigatoriP12527.

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

DIPiDIP-48659N.
STRINGi10116.ENSRNOP00000017633.

Structurei

3D structure databases

ProteinModelPortaliP12527.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 117116PLATAdd
BLAST
Domaini118 – 673556LipoxygenaseAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Phylogenomic databases

eggNOGiNOG69653.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP12527.
KOiK00461.
PhylomeDBiP12527.

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. 1 hit.
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.

P12527-1 [UniParc]FASTAAdd to Basket

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MPSYTVTVAT GSQWFAGTDD YIYLSLIGSA GCSEKHLLDK AFYNDFERGG    50
RDSYDVTVDE ELGEIYLVKI EKRKYRLHDD WYLKYITLKT PHDYIEFPCY 100
RWITGEGEIV LRDGCAKLAR DDQIHILKQH RRKELETRQK QYRWMEWNPG 150
FPLSIDAKCH KDLPRDIQFD SEKGVDFVLN YSKAMENLFI NRFMHMFQSS 200
WHDFADFEKI FVKISNTISE RVKNHWQEDL MFGYQFLNGC NPVLIKRCTE 250
LPKKLPVTTE MVECSLERQL SLEQEVQEGN IFIVDYELLD GIDANKTDPC 300
THQFLAAPIC LLYKNLANKI VPIAIQLNQT PGEKNPIFLP TDSKYDWLLA 350
KIWVRSSDFH IHQTITHLLR THLVSEVFGI AMYRQLPAVH PLFKLLVAHV 400
RFTIAINTKA REQLNCEYGL FDKANATGGG GHVQMVQRAV QDLTYSSLCF 450
PEAIKARGMD NTEDIPYYFY RDDGLLVWEA IQSFTTEVVS IYYEDDQVVE 500
EDQELQDFVK DVYVYGMRGR KASGFPKSIK SREKLSEYLT VVIFTASAQH 550
AAVNFGQYDW CSWIPNAPPT MRAPPPTAKG VVTIEQIVDT LPDRGRSCWH 600
LGAVWALSQF QENELFLGMY PEEHFIEKPV KEAMIRFRKN LEAIVSVIAE 650
RNKNKKLPYY YLSPDRIPNS VAI 673
Length:673
Mass (Da):78,087
Last modified:January 23, 2007 - v3
Checksum:i536B0BC27CB0A608
GO

Sequence cautioni

The sequence AAA41538.1 differs from that shown. Reason: Frameshift at position 667.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03960 mRNA. Translation: AAA41538.1. Frameshift.
PIRiA30882.
RefSeqiNP_036954.1. NM_012822.1.
UniGeneiRn.9662.

Genome annotation databases

GeneIDi25290.
KEGGirno:25290.
UCSCiRGD:2096. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03960 mRNA. Translation: AAA41538.1 . Frameshift.
PIRi A30882.
RefSeqi NP_036954.1. NM_012822.1.
UniGenei Rn.9662.

3D structure databases

ProteinModelPortali P12527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48659N.
STRINGi 10116.ENSRNOP00000017633.

Chemistry

BindingDBi P12527.
ChEMBLi CHEMBL312.

PTM databases

PhosphoSitei P12527.

Proteomic databases

PRIDEi P12527.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25290.
KEGGi rno:25290.
UCSCi RGD:2096. rat.

Organism-specific databases

CTDi 240.
RGDi 2096. Alox5.

Phylogenomic databases

eggNOGi NOG69653.
HOGENOMi HOG000234358.
HOVERGENi HBG005150.
InParanoidi P12527.
KOi K00461.
PhylomeDBi P12527.

Enzyme and pathway databases

UniPathwayi UPA00877 .

Miscellaneous databases

NextBioi 606033.
PROi P12527.

Gene expression databases

Genevestigatori P12527.

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. 1 hit.
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

  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.

Entry informationi

Entry nameiLOX5_RAT
AccessioniPrimary (citable) accession number: P12527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 127 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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