ID A0A093I5X0_STRCA Unreviewed; 142 AA.
AC A0A093I5X0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Arachidonate 5-lipoxygenase-activating protein {ECO:0000256|ARBA:ARBA00040386};
DE Flags: Fragment;
GN ORFNames=N308_01834 {ECO:0000313|EMBL:KFV87260.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV87260.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV87260.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV87260.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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. {ECO:0000256|ARBA:ARBA00037558}.
CC -!- SUBUNIT: Homotrimer. Interacts with LTC4S and ALOX5.
CC {ECO:0000256|ARBA:ARBA00038708}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004232}.
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DR EMBL; KL206936; KFV87260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093I5X0; -.
DR STRING; 441894.ENSSCUP00000020189; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
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; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR InterPro; IPR001446; 5_LipOase_AP.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR PANTHER; PTHR10250:SF2; ARACHIDONATE 5-LIPOXYGENASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10250; MICROSOMAL GLUTATHIONE S-TRANSFERASE; 1.
DR Pfam; PF01124; MAPEG; 1.
DR PRINTS; PR00488; 5LPOXGNASEAP.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV87260.1"
FT NON_TER 142
FT /evidence="ECO:0000313|EMBL:KFV87260.1"
SQ SEQUENCE 142 AA; 15923 MW; 9EE36DC123FD6F68 CRC64;
LFQTAFFASK VEHESKHCNG KGFQRPGSSA FDRVYTANQN CGHTYPTFLA VLWCAGLLCS
QAPAAFAGLM YLFVRQKYFV GYLGERTQST PGYLFGKRIL LFLFLMSAAG ILNYYLVFFF
GSDFEMHIKT ITSAISPLLL IP
//
