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Database: UniProt
Entry: G4UD00_NEUT9
LinkDB: G4UD00_NEUT9
Original site: G4UD00_NEUT9 
ID   G4UD00_NEUT9            Unreviewed;       580 AA.
AC   G4UD00;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=MBOAT-domain-containing protein {ECO:0000313|EMBL:EGZ75613.1};
DE   Flags: Fragment;
GN   ORFNames=NEUTE2DRAFT_148711 {ECO:0000313|EMBL:EGZ75613.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ75613.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ75613.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
CC   -!- FUNCTION: Sterol O-acyltransferase that catalyzes the formation of
CC       stery esters. {ECO:0000256|ARBA:ARBA00023568}.
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}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00009010}.
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DR   EMBL; GL891107; EGZ75613.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4UD00; -.
DR   STRING; 510952.G4UD00; -.
DR   eggNOG; KOG0380; Eukaryota.
DR   HOGENOM; CLU_018190_2_0_1; -.
DR   OMA; FICQMLQ; -.
DR   Proteomes; UP000008513; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   InterPro; IPR004299; MBOAT_fam.
DR   InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR   PANTHER; PTHR10408:SF26; O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1.
DR   Pfam; PF03062; MBOAT; 1.
DR   PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        426..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        560..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        517
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGZ75613.1"
SQ   SEQUENCE   580 AA;  64984 MW;  1587E3E0DB2C035F CRC64;
     MTSTSTSADA FAGQGDNILR PRPRKPLHTQ VSQLSHDANG DSDHANGTGA TSVTGVSSGR
     STPIPSDAPP SIQSLSTARK QVRAEQRRRI FPTIEFASRV SHFDPNSDYR DFHGFFNLFW
     IGLAIMAITT CLRNIKDTGY PLRVQIWGLF TVKLWHLAIA DFLMVATTAV SLPLHKVFRA
     APAGGVLTWA KGGMAIQSIY QAIWLAVWIV IPFWLEWTWT AQVFLLLHTM VLLMKMHSYS
     FYMGHLSETE KRLRALDDPA TASKAPAYLY PTPENPLGTV ASPKQRAVEA AAEASSKETK
     EISTPNEDEE ITQLREDLAR ELTSPMGNIT YPANLTWANY LDYLCCPTLC YEIEYPRTAA
     IDWQNLLSKV LAVFGCIFLL TVISEEFILP ALTDASIRLD PTLRAAAGDS GPLTALEGLL
     VLAETISWLL FPFMLTFLLV FLVIFEYVLG AFAEITHFAD RHFYSDWWNS TDWMEFSREW
     NVPVYNFLRR HVYSASRPHV GKANATVITF LISAVGHEIV MACITKKLRG YGFICQMLQL
     PIVMLQKTEL VRGKKTLNNV CFWCSMILGL SLICSLYVLV
//
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