AL5AP_RABIT
ID AL5AP_RABIT Reviewed; 153 AA.
AC P30357;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
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}.
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; M96556; AAA31253.1; -; mRNA.
DR AlphaFoldDB; P30357; -.
DR SMR; P30357; -.
DR STRING; 9986.ENSOCUP00000007090; -.
DR PRIDE; P30357; -.
DR eggNOG; ENOG502RZJB; Eukaryota.
DR InParanoid; P30357; -.
DR Proteomes; UP000001811; Unplaced.
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:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
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_0000217755"
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; 17159 MW; 360E34F13AEAF0EA CRC64;
MDQEAVGNVV LLAIVTLISV VQNGFFAHKV EHESRNQNGR SFQRTGTLAF ERVYTANQNC
VDAYPTFLAV LWTAGLLCSQ VPAAFAGLMY LFVRQKYFVG YLGERTQSTP GYIFGKRIIL
FLFLMSLAGI LNYCLILLFG SDFENYIKTI STT
