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Database: UniProt
Entry: H0ZDT5_TAEGU
LinkDB: H0ZDT5_TAEGU
Original site: H0ZDT5_TAEGU 
ID   H0ZDT5_TAEGU            Unreviewed;       527 AA.
AC   H0ZDT5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Lysophosphatidylcholine acyltransferase 1 {ECO:0000313|Ensembl:ENSTGUP00000008747.2};
GN   Name=LPCAT1 {ECO:0000313|Ensembl:ENSTGUP00000008747.2};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000008747.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000008747.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000008747.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005074}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   AlphaFoldDB; H0ZDT5; -.
DR   STRING; 59729.ENSTGUP00000008747; -.
DR   Ensembl; ENSTGUT00000008840.2; ENSTGUP00000008747.2; ENSTGUG00000008465.2.
DR   GeneTree; ENSGT01030000234574; -.
DR   HOGENOM; CLU_025017_0_1_1; -.
DR   InParanoid; H0ZDT5; -.
DR   OMA; RLDTITW; -.
DR   OrthoDB; 5471865at2759; -.
DR   TreeFam; TF323244; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000007754; Chromosome 2.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR   GO; GO:0047159; F:1-alkenylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR   GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0047191; F:1-alkylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:2001246; P:negative regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:Ensembl.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR   CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR045252; LPCAT1-like.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR23063:SF57; LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007754};
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        40..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          373..408
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          444..479
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  59659 MW;  54263C2ED326A663 CRC64;
     MKLSSRGRGC CTGGSRERGP PPRSPFVHQL RFSPLQKAKI AFMTLTLFPI RLFFAAFMML
     LAWPFAFIAS MGSDEQELEK PLSWWRKIVD ILLKAIMRMM WLAGGFHWIN VKGRRALPAE
     AAILTVAPHS SYFDAIPVTM TFASIVMKAE SKDIPVWGTL IKYIRPVFVS RSDQDSRRKT
     VEEIKRRAQS DGKWPQIMIF PEGTCTNRSC LITFKPGAFI PGVPVQPVVL RYPNKLDTIT
     WTWQGPGAFE ILWLTLCQFH NSVEIEFLPV YIPSEEERKN PVLYANNVRR VMAEALGVPV
     TDYTFEDCQL ALAEGQLRLP SDTCLLEFAK LVRSLGLKPE TLEDDLDKYT ASAMEMKKEK
     VDLKEFSAYL EFPVSQTLES MFALFDENED GVIDIREFII ALSVVCKPSK TLETIQLAFQ
     LYQSEGGTVT EEDLGNILKT AMGVSQIDVT HLFRAVDEEE KGKITYDDFY TFAVLHPHFA
     EEYLYTDQMG AESGLETSSL SAPNGICTDF SPDNSADRRK PLQKKLN
//
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