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Database: UniProt
Entry: A0A094L9W7_ANTCR
LinkDB: A0A094L9W7_ANTCR
Original site: A0A094L9W7_ANTCR 
ID   A0A094L9W7_ANTCR        Unreviewed;       487 AA.
AC   A0A094L9W7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Lysophosphatidylcholine acyltransferase 2 {ECO:0000313|EMBL:KFZ66237.1};
DE   Flags: Fragment;
GN   ORFNames=N321_11813 {ECO:0000313|EMBL:KFZ66237.1};
OS   Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC   Caprimulgidae; Antrostomus.
OX   NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ66237.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ66237.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ66237.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL362289; KFZ66237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094L9W7; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000053620; Unassembled WGS sequence.
DR   GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00051; EFh; 2.
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:SF21; LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
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; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:KFZ66237.1}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..487
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001901872"
FT   DOMAIN          316..351
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          353..388
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          396..423
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          441..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFZ66237.1"
FT   NON_TER         487
FT                   /evidence="ECO:0000313|EMBL:KFZ66237.1"
SQ   SEQUENCE   487 AA;  54890 MW;  08569270CBD0F280 CRC64;
     IAFIVLLAWL VASIATFRHP GKGSVPLKGW RRRMIQTALS RLTRTLFFVM GFHVKVKGKI
     ANLLEAPILV VAPHSSFFDA IVSALTGMPS IVSRAENLST PVFGTILSSV QPVSVSRQDP
     DSRKNTVTEI TKRALSKGQW PQILIFPEGT CTNRSCLITF KQGAFVPQVP VQPVLIRYPN
     KLDTVTWTWQ GYSLKELCVM TLCQLFTRVE VEFLPVHVPT EEEKNDPILF ANRVRQIMAT
     YVISHGYILA IKYNLVKSQL TLPMEAGLVE FTKISKKLNL KWNHIREQLD TFAAIASASK
     GGRIGIEEFA EYLKLPISDV LRELFLLFDR NGDGTIDFRE YVIGLSILCN PANTEETIRM
     AFKLFDMDED GTITEDEFAC IIQSALGVPD LDVSMLFKEI DADETGKLSY DEFKDFALKH
     PEYATLFTTY LELQRYQMDM SEEDDIQPPE VRKSTVPVSE TTPIARNKVC PEGNEEDNSS
     ISDKKDD
//
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