AL5AP_RAT
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 03-AUG-2022, entry version 140.
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}.
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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; P20291; -.
DR PRIDE; P20291; -.
DR Ensembl; ENSRNOT00000001207; ENSRNOP00000001207; ENSRNOG00000000907.
DR GeneID; 29624; -.
DR KEGG; rno:29624; -.
DR UCSC; RGD:2097; rat.
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; 1609516at2759; -.
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 tissues.
DR Genevisible; P20291; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:RGD.
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:0047485; F:protein N-terminus binding; ISO:RGD.
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; -; 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 Pfam; PF01124; MAPEG; 1.
DR PRINTS; PR00488; 5LPOXGNASEAP.
DR SUPFAM; SSF161084; SSF161084; 1.
DR PROSITE; PS01297; FLAP_GST2_LTC4S; 1.
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
