ID G1P0F2_MYOLU Unreviewed; 505 AA.
AC G1P0F2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Membrane bound O-acyltransferase domain containing 2 {ECO:0000313|Ensembl:ENSMLUP00000003230.2};
GN Name=MBOAT2 {ECO:0000313|Ensembl:ENSMLUP00000003230.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000003230.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000003230.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000003230.2}
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; AAPE02053740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02053741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02053742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02053743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P0F2; -.
DR STRING; 59463.ENSMLUP00000003230; -.
DR Ensembl; ENSMLUT00000003548.2; ENSMLUP00000003230.2; ENSMLUG00000003545.2.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; G1P0F2; -.
DR OMA; ASFTARC; -.
DR TreeFam; TF314906; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; 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:0036151; P:phosphatidylcholine acyl-chain remodeling; 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 InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13906:SF7; LYSOPHOSPHOLIPID ACYLTRANSFERASE 2; 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:UP000001074};
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 TRANSMEM 12..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 458..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 56450 MW; EE47E0ED85A89D36 CRC64;
LSTEGSRPGR SALRVANVTC AFSSQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA
TLLGLYLAVF CFGWYALHFL VQSGVSYCIM IIIGMEHMHK YCFVFALGYL IVCQITRVYI
FDYGQYSADF SGPMMIMTQK ITSLAYEIHD GMFRKDEDLT PSQRDLAVRR MPSLLEYLSY
NCNFMGILAG PLCSYKDYIT FIEGRSYHVP RSGEDGRKAP PCGGAEPSPN IRMFSSLGIC
CGGFLIIIHL LSSSQDRGSL RREGSSWETL HEGLEAGGWS QPTPVGVPGG ANVPGAGRGG
CRRSAGQEKR RSVFQGSTSF KMFLDNWNIQ TALWLKRVCY ERTTWSPTVQ TFVLSAIWHG
VYPGYYLTFL TGVLMTLAAR AMRSNFRHYF LKSPQLKLLY DVVTWGATQV AVSYTVVPFV
LLSVKPSFAF YSSWSYCLHI AGLLVLLFLP VKKTQRGQDP HEHRRLSRSK KSDENSWGQN
SFPTTTNNVC NQGPAGAARH PSGTE
//
