ID   AL5AP_PIG               Reviewed;         153 AA.
AC   P30356;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Arachidonate 5-lipoxygenase-activating protein;
DE   AltName: Full=FLAP;
DE   AltName: Full=MK-886-binding protein;
DE   Flags: Fragment;
GN   Name=ALOX5AP; Synonyms=FLAP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1480129;
RA   Vickers P.J., O'Neill G.P., Mancini J.A., Charleson S., Abramovitz M.;
RT   "Cross-species comparison of 5-lipoxygenase-activating protein.";
RL   Mol. Pharmacol. 42:1014-1019(1992).
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; M96555; AAA31032.1; -; mRNA.
DR   AlphaFoldDB; P30356; -.
DR   SMR; P30356; -.
DR   STRING; 9823.ENSSSCP00000009958; -.
DR   PaxDb; P30356; -.
DR   PeptideAtlas; P30356; -.
DR   eggNOG; ENOG502RZJB; Eukaryota.
DR   HOGENOM; CLU_110291_0_0_1; -.
DR   InParanoid; P30356; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P30356; SS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR   GO; GO:0050544; F:arachidonic acid binding; ISS:UniProtKB.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
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:0004464; F:leukotriene-C4 synthase activity; IBA:GO_Central.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Leukotriene biosynthesis; Membrane; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..>153
FT                   /note="Arachidonate 5-lipoxygenase-activating protein"
FT                   /id="PRO_0000217754"
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..153
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   NON_TER         153
SQ   SEQUENCE   153 AA;  17345 MW;  16AF19D7914DAF99 CRC64;
     MDQEAMGNIV LLAIVTLISV VQNAFFAHKV EHESKTHNGR SFQRTGTPAF ERVYTANQNC
     VDAYPTFLVV LWSAGLFCSQ VPAAFAGLMY LFVRQKYFVG YLGERTQSTP GYIFGKRIIL
     FLFLMSLAGI FNYFLILFFG SDFENYIKTI TTT