ID I3MBL9_ICTTR Unreviewed; 417 AA.
AC I3MBL9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Membrane bound O-acyltransferase domain containing 1 {ECO:0000313|Ensembl:ENSSTOP00000007554.3};
GN Name=MBOAT1 {ECO:0000313|Ensembl:ENSSTOP00000007554.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000007554.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000007554.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AGTP01056568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01056569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MBL9; -.
DR STRING; 43179.ENSSTOP00000007554; -.
DR Ensembl; ENSSTOT00000008429.3; ENSSTOP00000007554.3; ENSSTOG00000008425.3.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; I3MBL9; -.
DR TreeFam; TF314906; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13906:SF6; LYSOPHOSPHOLIPID ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR13906; PORCUPINE; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012429461"
FT TRANSMEM 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 417 AA; 47592 MW; 648D1EF9F6056789 CRC64;
VNFVACQLFA LLAALWFRLY LHPAKSSPAV RHAFATILGT YFVIFCFGWY SVHLFVLVLM
CYGILVTASV SSIHRYTFFV AMGYLTICHI SRIYIFHYGV LTTDFSGPLM IITQKITTLA
FQVHDGLGRR AEDLSAEQHR LAIKVKPSFL EYLSYLLNFM SVIAGPCNHF KDYVAFIEGR
HTHMKLLEVN GKHKDFHSLP EPSPTGAVMR KLCVTLVSLL LFLTLTKTFP VTCLAEDWFV
QKADFPTRLC YLYVVMQASK PKYYFAWTLA DAVNNAAGFG FSGVDKDGRC CWDLLSNLNI
WKIETATSFR MYLENWNIQT AAWLKVRNNC RHHFLSSKAL KCAYDLVTWA VTQLAVSYTV
APFVMLAAEP ALSLYRSMYF YLHIISLLII LFLPIKPQAH LQRQPQTANS VNKKKTD
//
