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P30355

- AL5AP_MOUSE

UniProt

P30355 - AL5AP_MOUSE

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Protein

Arachidonate 5-lipoxygenase-activating protein

Gene

Alox5ap

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. arachidonic acid binding Source: UniProtKB
  2. enzyme activator activity Source: InterPro

GO - Biological processi

  1. cellular response to calcium ion Source: Ensembl
  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: Ensembl
Complete GO annotation...

Keywords - Biological processi

Leukotriene biosynthesis

Enzyme and pathway databases

ReactomeiREACT_196544. Synthesis of Lipoxins (LX).
REACT_206751. Synthesis of 5-eicosatetraenoic acids.
REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).

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: Chromosome 5

Organism-specific databases

MGIiMGI:107505. Alox5ap.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum Source: RefGenome
  3. integral component of membrane Source: UniProtKB-KW
  4. nuclear envelope Source: UniProtKB
  5. nuclear membrane Source: UniProtKB
  6. 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

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...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88LumenalBy similarity
Topological domaini31 – 5222CytoplasmicBy similarityAdd
BLAST
Topological domaini78 – 803LumenalBy similarity
Topological domaini103 – 1075CytoplasmicBy similarity
Topological domaini129 – 16133LumenalBy similarityAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei108 – 1158By similarity

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 3022HelicalBy similarityAdd
BLAST
Transmembranei53 – 7725HelicalBy similarityAdd
BLAST
Transmembranei81 – 10222HelicalBy similarityAdd
BLAST
Transmembranei116 – 12813HelicalBy similarityAdd
BLAST

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK004002 mRNA. Translation: BAB23117.1 .
BC026209 mRNA. Translation: AAH26209.1 .
M96554 mRNA. Translation: AAA37632.1 .
CCDSi CCDS39407.1.
RefSeqi NP_033793.1. NM_009663.1.
UniGenei Mm.19844.

3D structure databases

ProteinModelPortali P30355.
SMRi P30355. Positions 1-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198077. 1 interaction.
STRINGi 10090.ENSMUSP00000071130.

PTM databases

PhosphoSitei P30355.

Proteomic databases

PaxDbi P30355.
PRIDEi P30355.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071130 ; ENSMUSP00000071130 ; ENSMUSG00000060063 .
GeneIDi 11690.
KEGGi mmu:11690.
UCSCi uc009app.1. mouse.

Organism-specific databases

CTDi 241.
MGIi MGI:107505. Alox5ap.

Phylogenomic databases

eggNOGi NOG79474.
GeneTreei ENSGT00430000030964.
HOGENOMi HOG000116372.
HOVERGENi HBG107295.
InParanoidi P30355.
OMAi NCMDAYP.
PhylomeDBi P30355.
TreeFami TF105328.

Enzyme and pathway databases

Reactomei REACT_196544. Synthesis of Lipoxins (LX).
REACT_206751. Synthesis of 5-eicosatetraenoic acids.
REACT_215561. Synthesis of Leukotrienes (LT) and Eoxins (EX).

Miscellaneous databases

NextBioi 279343.
PROi P30355.
SOURCEi Search...

Gene expression databases

Bgeei P30355.
CleanExi MM_ALOX5AP.
ExpressionAtlasi P30355. baseline and differential.
Genevestigatori P30355.

Family and domain databases

Gene3Di 1.20.120.550. 1 hit.
InterProi IPR001446. 5_LipOase_AP.
IPR018295. FLAP/GST2/LTC4S_CS.
IPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view ]
Pfami PF01124. MAPEG. 1 hit.
[Graphical view ]
PRINTSi PR00488. 5LPOXGNASEAP.
PROSITEi PS01297. FLAP_GST2_LTC4S. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 101 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