ID   AL5AP_MACFA             Reviewed;         161 AA.
AC   Q2PG08;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Arachidonate 5-lipoxygenase-activating protein;
GN   Name=ALOX5AP; ORFNames=QccE-16217;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT   oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; AB220429; BAE72962.1; -; mRNA.
DR   RefSeq; XP_005585645.1; XM_005585588.2.
DR   AlphaFoldDB; Q2PG08; -.
DR   SMR; Q2PG08; -.
DR   STRING; 9541.XP_005585644.1; -.
DR   Ensembl; ENSMFAT00000069687; ENSMFAP00000019139; ENSMFAG00000032586.
DR   GeneID; 102132235; -.
DR   KEGG; mcf:102132235; -.
DR   eggNOG; ENOG502RZJB; Eukaryota.
DR   GeneTree; ENSGT00940000158706; -.
DR   OrthoDB; 1609516at2759; -.
DR   Proteomes; UP000233100; Chromosome 17.
DR   Bgee; ENSMFAG00000032586; Expressed in bone marrow and 11 other tissues.
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:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0002540; P:leukotriene production involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
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..161
FT                   /note="Arachidonate 5-lipoxygenase-activating protein"
FT                   /id="PRO_0000260254"
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"
SQ   SEQUENCE   161 AA;  18123 MW;  2E8F5CCBB890F54A CRC64;
     MDQETVGNVV LLAIVTLISV VQNGFFAHKV EHESRTQNGR SFQRTGTLAF ERVYTANQNC
     VDAYPTFLAV LWSAGLLCSQ VPAAFAGLMY LLVRQKYFVG YLGERTQSTP GYIFGKRIIL
     FLFLMSVAGI FNYYLIFFFG SDFENYIKTV TTTISPLLLI P