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Arachidonate 5-lipoxygenase-activating protein (FLAP) (MK-886-binding protein)

 AL5AP_MOUSE             Reviewed;         161 AA.
P30355; Q9D138;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
20-JUN-2018, entry version 124.
RecName: Full=Arachidonate 5-lipoxygenase-activating protein;
AltName: Full=FLAP;
AltName: Full=MK-886-binding protein;
Name=Alox5ap; Synonyms=Flap;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
PubMed=1480129;
Vickers P.J., O'Neill G.P., Mancini J.A., Charleson S., Abramovitz M.;
"Cross-species comparison of 5-lipoxygenase-activating protein.";
Mol. Pharmacol. 42:1014-1019(1992).
[4]
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH ALOX5.
PubMed=19075240; DOI=10.1073/pnas.0808211106;
Mandal A.K., Jones P.B., Bair A.M., Christmas P., Miller D.,
Yamin T.-T., Wisniewski D., Menke J., Evans J.F., Hyman B.T.,
Bacskai B., Chen M., Lee D.M., Nikolic B., Soberman R.J.;
"The nuclear membrane organization of leukotriene synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 105:20434-20439(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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). {ECO:0000250,
ECO:0000269|PubMed:19075240}.
-!- SUBUNIT: Homotrimer. Interacts with LTC4S and ALOX5.
{ECO:0000269|PubMed:19075240}.
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000269|PubMed:19075240}; Multi-pass membrane protein
{ECO:0000269|PubMed:19075240}. Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- DOMAIN: The C-terminal part after residue 140 is mostly
disordered. {ECO:0000250}.
-!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK004002; BAB23117.1; -; mRNA.
EMBL; BC026209; AAH26209.1; -; mRNA.
EMBL; M96554; AAA37632.1; -; mRNA.
CCDS; CCDS39407.1; -.
RefSeq; NP_033793.1; NM_009663.2.
UniGene; Mm.19844; -.
ProteinModelPortal; P30355; -.
BioGrid; 198077; 1.
STRING; 10090.ENSMUSP00000071130; -.
BindingDB; P30355; -.
ChEMBL; CHEMBL3414408; -.
PhosphoSitePlus; P30355; -.
MaxQB; P30355; -.
PaxDb; P30355; -.
PeptideAtlas; P30355; -.
PRIDE; P30355; -.
Ensembl; ENSMUST00000071130; ENSMUSP00000071130; ENSMUSG00000060063.
GeneID; 11690; -.
KEGG; mmu:11690; -.
UCSC; uc009app.1; mouse.
CTD; 241; -.
MGI; MGI:107505; Alox5ap.
eggNOG; ENOG410IHE0; Eukaryota.
eggNOG; ENOG4111T4I; LUCA.
GeneTree; ENSGT00430000030964; -.
HOGENOM; HOG000116372; -.
HOVERGEN; HBG107295; -.
InParanoid; P30355; -.
KO; K20735; -.
OMA; NCMDAYP; -.
OrthoDB; EOG091G12NW; -.
PhylomeDB; P30355; -.
TreeFam; TF105328; -.
Reactome; R-MMU-2142688; Synthesis of 5-eicosatetraenoic acids.
Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-MMU-2142700; Synthesis of Lipoxins (LX).
PRO; PR:P30355; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000060063; -.
CleanEx; MM_ALOX5AP; -.
ExpressionAtlas; P30355; baseline and differential.
Genevisible; P30355; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0004051; F:arachidonate 5-lipoxygenase activity; IEA:Ensembl.
GO; GO:0050544; F:arachidonic acid binding; ISS:UniProtKB.
GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
GO; GO:0019370; P:leukotriene biosynthetic process; IDA:MGI.
GO; GO:0002540; P:leukotriene production involved in inflammatory response; IMP:MGI.
GO; GO:0019372; P:lipoxygenase pathway; ISO:MGI.
GO; GO:0002675; P:positive regulation of acute inflammatory response; ISO:MGI.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
Gene3D; 1.20.120.550; -; 1.
InterPro; IPR001446; 5_LipOase_AP.
InterPro; IPR018295; FLAP/GST2/LTC4S_CS.
InterPro; IPR023352; MAPEG-like_dom_sf.
InterPro; IPR001129; Membr-assoc_MAPEG.
Pfam; PF01124; MAPEG; 1.
PRINTS; PR00488; 5LPOXGNASEAP.
SUPFAM; SSF161084; SSF161084; 1.
PROSITE; PS01297; FLAP_GST2_LTC4S; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Leukotriene biosynthesis;
Membrane; Nucleus; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 161 Arachidonate 5-lipoxygenase-activating
protein.
/FTId=PRO_0000217753.
TOPO_DOM 1 8 Lumenal. {ECO:0000250}.
TRANSMEM 9 30 Helical. {ECO:0000250}.
TOPO_DOM 31 52 Cytoplasmic. {ECO:0000250}.
TRANSMEM 53 77 Helical. {ECO:0000250}.
TOPO_DOM 78 80 Lumenal. {ECO:0000250}.
TRANSMEM 81 102 Helical. {ECO:0000250}.
TOPO_DOM 103 107 Cytoplasmic. {ECO:0000250}.
INTRAMEM 108 115 {ECO:0000250}.
TRANSMEM 116 128 Helical. {ECO:0000250}.
TOPO_DOM 129 161 Lumenal. {ECO:0000250}.
REGION 20 27 Inhibitor binding. {ECO:0000250}.
REGION 112 123 Inhibitor binding. {ECO:0000250}.
CONFLICT 142 142 D -> Y (in Ref. 3; AAA37632).
{ECO:0000305}.
SEQUENCE 161 AA; 18136 MW; 28DA042AA18D17C8 CRC64;
MDQEAVGNVV LLALVTLISV VQNAFFAHKV EHESKAHNGR SFQRTGTLAF ERVYTANQNC
VDAYPTFLVV LWTAGLLCSQ VPAAFAGLMY LFVRQKYFVG YLGERTQSTP GYIFGKRIIL
FLFLMSFAGI LNHYLIFFFG SDFENYIRTV STTISPLLLI P


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