ID AL5AP_RAT Reviewed; 161 AA. AC P20291; Q5RJL3; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 24-JAN-2024, entry version 148. DE RecName: Full=Arachidonate 5-lipoxygenase-activating protein; DE AltName: Full=FLAP; DE AltName: Full=MK-886-binding protein; GN Name=Alox5ap; Synonyms=Flap; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2300173; DOI=10.1038/343282a0; RA Dixon R.A.F., Diehl R.E., Opas E., Rands E., Vickers P.J., Evans J.F., RA Gillard J.W., Miller D.K.; RT "Requirement of a 5-lipoxygenase-activating protein for leukotriene RT synthesis."; RL Nature 343:282-284(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 1-39; 90-121 AND 126-146. RX PubMed=2300172; DOI=10.1038/343278a0; RA Miller D.K., Gillard J.W., Vickers P.J., Sadowski S., Leveille C., RA Mancini J.A., Charleson P., Dixon R.A.F., Ford-Hutchinson A.W., Fortin R., RA Gauthier J.Y., Rodkey J., Rosen R., Rouzer C., Sigal I.S., Strader C.D., RA Evans J.F.; RT "Identification and isolation of a membrane protein necessary for RT leukotriene production."; RL Nature 343:278-281(1990). CC -!- FUNCTION: Required for leukotriene biosynthesis by ALOX5 (5- CC lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, CC and could play an essential role in the transfer of arachidonic acid to CC ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of CC leukotrienes (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homotrimer. Interacts with LTC4S and ALOX5 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- DOMAIN: The C-terminal part after residue 140 is mostly disordered. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X52196; CAA36442.1; -; mRNA. DR EMBL; BC086593; AAH86593.1; -; mRNA. DR PIR; S08206; S08206. DR RefSeq; NP_058956.1; NM_017260.2. DR AlphaFoldDB; P20291; -. DR SMR; P20291; -. DR DIP; DIP-48660N; -. DR IntAct; P20291; 1. DR STRING; 10116.ENSRNOP00000001207; -. DR BindingDB; P20291; -. DR ChEMBL; CHEMBL1921661; -. DR PhosphoSitePlus; P20291; -. DR PaxDb; 10116-ENSRNOP00000001207; -. DR Ensembl; ENSRNOT00000001207.7; ENSRNOP00000001207.3; ENSRNOG00000000907.7. DR Ensembl; ENSRNOT00055005320; ENSRNOP00055003946; ENSRNOG00055003427. DR Ensembl; ENSRNOT00060003776; ENSRNOP00060002634; ENSRNOG00060002388. DR Ensembl; ENSRNOT00065009709; ENSRNOP00065007016; ENSRNOG00065006327. DR GeneID; 29624; -. DR KEGG; rno:29624; -. DR UCSC; RGD:2097; rat. DR AGR; RGD:2097; -. DR CTD; 241; -. DR RGD; 2097; Alox5ap. DR eggNOG; ENOG502RZJB; Eukaryota. DR GeneTree; ENSGT00940000158706; -. DR HOGENOM; CLU_110291_0_0_1; -. DR InParanoid; P20291; -. DR OMA; QNVFFAQ; -. DR OrthoDB; 5343039at2759; -. DR PhylomeDB; P20291; -. DR TreeFam; TF105328; -. DR Reactome; R-RNO-2142688; Synthesis of 5-eicosatetraenoic acids. DR Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX). DR Reactome; R-RNO-2142700; Synthesis of Lipoxins (LX). DR PRO; PR:P20291; -. DR Proteomes; UP000002494; Chromosome 12. DR Bgee; ENSRNOG00000000907; Expressed in lung and 19 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005635; C:nuclear envelope; IDA:RGD. DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0050544; F:arachidonic acid binding; ISS:UniProtKB. DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro. DR GO; GO:0019899; F:enzyme binding; IPI:RGD. DR GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IBA:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD. DR GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD. DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:RGD. DR GO; GO:0002540; P:leukotriene production involved in inflammatory response; ISO:RGD. DR GO; GO:0019372; P:lipoxygenase pathway; IDA:RGD. DR GO; GO:0002675; P:positive regulation of acute inflammatory response; IMP:RGD. DR GO; GO:0070207; P:protein homotrimerization; ISO:RGD. DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1. DR InterPro; IPR001446; 5_LipOase_AP. DR InterPro; IPR018295; FLAP/GST2/LTC4S_CS. DR InterPro; IPR023352; MAPEG-like_dom_sf. DR InterPro; IPR001129; Membr-assoc_MAPEG. DR PANTHER; PTHR10250:SF2; ARACHIDONATE 5-LIPOXYGENASE-ACTIVATING PROTEIN; 1. DR PANTHER; PTHR10250; MICROSOMAL GLUTATHIONE S-TRANSFERASE; 1. DR Pfam; PF01124; MAPEG; 1. DR PRINTS; PR00488; 5LPOXGNASEAP. DR SUPFAM; SSF161084; MAPEG domain-like; 1. DR PROSITE; PS01297; FLAP_GST2_LTC4S; 1. DR Genevisible; P20291; RN. PE 1: Evidence at protein level; KW Direct protein sequencing; Endoplasmic reticulum; Leukotriene biosynthesis; KW Membrane; Nucleus; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..161 FT /note="Arachidonate 5-lipoxygenase-activating protein" FT /id="PRO_0000217756" FT TOPO_DOM 1..8 FT /note="Lumenal" FT /evidence="ECO:0000250" FT TRANSMEM 9..30 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 31..52 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 53..77 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 78..80 FT /note="Lumenal" FT /evidence="ECO:0000250" FT TRANSMEM 81..102 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 103..107 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT INTRAMEM 108..115 FT /evidence="ECO:0000250" FT TRANSMEM 116..128 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 129..161 FT /note="Lumenal" FT /evidence="ECO:0000250" FT CONFLICT 32 FT /note="L -> I (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="L -> I (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 161 AA; 18070 MW; 9CCD6F8B3AA3B87E CRC64; MDQEAVGNVV LLAIVTLISV VQNAFFAHKV ELESKAQSGR SFQRTGTLAF ERVYTANQNC VDAYPTFLVV LWTAGLLCSQ VPAAFAGLMY LFVRQKYFVG YLGERTQSTP GYIFGKRIIL FLFLMSLAGI LNHYLIFFFG SDFENYIRTI TTTISPLLLI P //