ID   AL5AP_BOVIN             Reviewed;         161 AA.
AC   Q148F2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Arachidonate 5-lipoxygenase-activating protein;
GN   Name=ALOX5AP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) 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}.
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; BC118389; AAI18390.1; -; mRNA.
DR   RefSeq; NP_001069761.1; NM_001076293.2.
DR   AlphaFoldDB; Q148F2; -.
DR   SMR; Q148F2; -.
DR   STRING; 9913.ENSBTAP00000017570; -.
DR   PaxDb; Q148F2; -.
DR   PRIDE; Q148F2; -.
DR   Ensembl; ENSBTAT00000080933; ENSBTAP00000070351; ENSBTAG00000013201.
DR   GeneID; 613869; -.
DR   KEGG; bta:613869; -.
DR   CTD; 241; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013201; -.
DR   VGNC; VGNC:25845; ALOX5AP.
DR   eggNOG; ENOG502RZJB; Eukaryota.
DR   GeneTree; ENSGT00940000158706; -.
DR   HOGENOM; CLU_110291_0_0_1; -.
DR   InParanoid; Q148F2; -.
DR   OMA; QNVFFAQ; -.
DR   OrthoDB; 1609516at2759; -.
DR   TreeFam; TF105328; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000013201; Expressed in neutrophil and 98 other tissues.
DR   ExpressionAtlas; Q148F2; baseline and differential.
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..161
FT                   /note="Arachidonate 5-lipoxygenase-activating protein"
FT                   /id="PRO_0000260253"
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;  18028 MW;  B989F92731716A98 CRC64;
     MDQEAVGNIV LLAIVTLISV VQNGFFAHKV EHESKTHNGR SFQRTGTLAF ERVYTANQNC
     VDAYPTFLVM LWSAGLLCSQ VPAAFAGLMY LFVRQKYFVG YLGERTQSTP GYIFGKRIIL
     FLFAMSLAGI LNYFFIALFG SDFENYIKTV TTTISPLLLI P