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Protein

Arachidonate 5-lipoxygenase-activating protein

Gene

Alox5ap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). unstructured (By similarity).By similarity

GO - Molecular functioni

  1. arachidonate 5-lipoxygenase activity Source: Ensembl
  2. arachidonic acid binding Source: UniProtKB
  3. enzyme activator activity Source: InterPro
  4. protein N-terminus binding Source: MGI

GO - Biological processi

  1. cellular response to calcium ion Source: MGI
  2. leukotriene biosynthetic process Source: MGI
  3. leukotriene production involved in inflammatory response Source: MGI
  4. positive regulation of acute inflammatory response Source: Ensembl
  5. protein homotrimerization Source: MGI
Complete GO annotation...

Keywords - Biological processi

Leukotriene biosynthesis

Enzyme and pathway databases

ReactomeiREACT_280918. Synthesis of Lipoxins (LX).
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_327774. Synthesis of 5-eicosatetraenoic acids.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 5-lipoxygenase-activating protein
Alternative name(s):
FLAP
MK-886-binding protein
Gene namesi
Name:Alox5ap
Synonyms:Flap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:107505. Alox5ap.

Subcellular locationi

  1. Nucleus membrane 1 Publication; Multi-pass membrane protein 1 Publication
  2. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88LumenalBy similarity
Transmembranei9 – 3022HelicalBy similarityAdd
BLAST
Topological domaini31 – 5222CytoplasmicBy similarityAdd
BLAST
Transmembranei53 – 7725HelicalBy similarityAdd
BLAST
Topological domaini78 – 803LumenalBy similarity
Transmembranei81 – 10222HelicalBy similarityAdd
BLAST
Topological domaini103 – 1075CytoplasmicBy similarity
Intramembranei108 – 1158By similarity
Transmembranei116 – 12813HelicalBy similarityAdd
BLAST
Topological domaini129 – 16133LumenalBy similarityAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum Source: MGI
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane Source: MGI
  6. nuclear envelope Source: UniProtKB
  7. nuclear membrane Source: UniProtKB
  8. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Arachidonate 5-lipoxygenase-activating proteinPRO_0000217753Add
BLAST

Proteomic databases

MaxQBiP30355.
PaxDbiP30355.
PRIDEiP30355.

PTM databases

PhosphoSiteiP30355.

Expressioni

Gene expression databases

BgeeiP30355.
CleanExiMM_ALOX5AP.
ExpressionAtlasiP30355. baseline and differential.
GenevestigatoriP30355.

Interactioni

Subunit structurei

Homotrimer. Interacts with LTC4S and ALOX5.1 Publication

Protein-protein interaction databases

BioGridi198077. 1 interaction.
STRINGi10090.ENSMUSP00000071130.

Structurei

3D structure databases

ProteinModelPortaliP30355.
SMRiP30355. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 278Inhibitor bindingBy similarity
Regioni112 – 12312Inhibitor bindingBy similarityAdd
BLAST

Domaini

The C-terminal part after residue 140 is mostly disordered.By similarity

Sequence similaritiesi

Belongs to the MAPEG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG79474.
GeneTreeiENSGT00430000030964.
HOGENOMiHOG000116372.
HOVERGENiHBG107295.
InParanoidiP30355.
OMAiNCMDAYP.
PhylomeDBiP30355.
TreeFamiTF105328.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR001446. 5_LipOase_AP.
IPR018295. FLAP/GST2/LTC4S_CS.
IPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]
PRINTSiPR00488. 5LPOXGNASEAP.
PROSITEiPS01297. FLAP_GST2_LTC4S. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30355-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQEAVGNVV LLALVTLISV VQNAFFAHKV EHESKAHNGR SFQRTGTLAF
60 70 80 90 100
ERVYTANQNC VDAYPTFLVV LWTAGLLCSQ VPAAFAGLMY LFVRQKYFVG
110 120 130 140 150
YLGERTQSTP GYIFGKRIIL FLFLMSFAGI LNHYLIFFFG SDFENYIRTV
160
STTISPLLLI P
Length:161
Mass (Da):18,136
Last modified:October 11, 2005 - v2
Checksum:i28DA042AA18D17C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421D → Y in AAA37632 (PubMed:1480129).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004002 mRNA. Translation: BAB23117.1.
BC026209 mRNA. Translation: AAH26209.1.
M96554 mRNA. Translation: AAA37632.1.
CCDSiCCDS39407.1.
RefSeqiNP_033793.1. NM_009663.1.
UniGeneiMm.19844.

Genome annotation databases

EnsembliENSMUST00000071130; ENSMUSP00000071130; ENSMUSG00000060063.
GeneIDi11690.
KEGGimmu:11690.
UCSCiuc009app.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004002 mRNA. Translation: BAB23117.1.
BC026209 mRNA. Translation: AAH26209.1.
M96554 mRNA. Translation: AAA37632.1.
CCDSiCCDS39407.1.
RefSeqiNP_033793.1. NM_009663.1.
UniGeneiMm.19844.

3D structure databases

ProteinModelPortaliP30355.
SMRiP30355. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198077. 1 interaction.
STRINGi10090.ENSMUSP00000071130.

PTM databases

PhosphoSiteiP30355.

Proteomic databases

MaxQBiP30355.
PaxDbiP30355.
PRIDEiP30355.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071130; ENSMUSP00000071130; ENSMUSG00000060063.
GeneIDi11690.
KEGGimmu:11690.
UCSCiuc009app.1. mouse.

Organism-specific databases

CTDi241.
MGIiMGI:107505. Alox5ap.

Phylogenomic databases

eggNOGiNOG79474.
GeneTreeiENSGT00430000030964.
HOGENOMiHOG000116372.
HOVERGENiHBG107295.
InParanoidiP30355.
OMAiNCMDAYP.
PhylomeDBiP30355.
TreeFamiTF105328.

Enzyme and pathway databases

ReactomeiREACT_280918. Synthesis of Lipoxins (LX).
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_327774. Synthesis of 5-eicosatetraenoic acids.

Miscellaneous databases

NextBioi279343.
PROiP30355.
SOURCEiSearch...

Gene expression databases

BgeeiP30355.
CleanExiMM_ALOX5AP.
ExpressionAtlasiP30355. baseline and differential.
GenevestigatoriP30355.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR001446. 5_LipOase_AP.
IPR018295. FLAP/GST2/LTC4S_CS.
IPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]
PRINTSiPR00488. 5LPOXGNASEAP.
PROSITEiPS01297. FLAP_GST2_LTC4S. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Embryo.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. "Cross-species comparison of 5-lipoxygenase-activating protein."
    Vickers P.J., O'Neill G.P., Mancini J.A., Charleson S., Abramovitz M.
    Mol. Pharmacol. 42:1014-1019(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
  4. Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ALOX5.

Entry informationi

Entry nameiAL5AP_MOUSE
AccessioniPrimary (citable) accession number: P30355
Secondary accession number(s): Q9D138
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 11, 2005
Last modified: April 1, 2015
This is version 105 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.