ID U3JZN1_FICAL Unreviewed; 534 AA.
AC U3JZN1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Lysophosphatidylcholine acyltransferase 2 {ECO:0000313|Ensembl:ENSFALP00000008235.2};
GN Name=LPCAT2 {ECO:0000313|Ensembl:ENSFALP00000008235.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000008235.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000008235.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000008235.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_005052692.1; XM_005052635.1.
DR AlphaFoldDB; U3JZN1; -.
DR STRING; 59894.ENSFALP00000008235; -.
DR Ensembl; ENSFALT00000008268.2; ENSFALP00000008235.2; ENSFALG00000007864.2.
DR GeneID; 101811593; -.
DR KEGG; fab:101811593; -.
DR CTD; 54947; -.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_0_1; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000016665; Chromosome 11.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:Ensembl.
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 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:UP000016665};
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 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 363..398
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 400..435
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 443..470
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 489..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 59765 MW; F10250F61EF0B927 CRC64;
MPIISQDVSL PRGTEEKFLS SCLVLQPAQT VLQGIILLPL RAICITFILL LAWLSASIAT
FHQPGRGFLP LKGWRRRMIQ STLSSLTRTA FFVMGFQVKV KGKVAGLAEA PIFVAAPHSS
FFDAIICALT GMPSIVSRAE NLSTPVFGTI LRSLQPVAVS RQDPDSRKNT VAEITRRALS
RGQWPQILIF PEGTCTNRSC LITFKQGAFV PQVPVQPVLL RYPNKLDTVT WTWQGYSFKE
LCIMTACQIF TRLEVEFLPI HVPTEEEKND PILFANRVRQ TMANALNVPV TDHTFEDCRL
MISAGQLTLP MEAGLVEFTK ISKKLNLKWN HVREQLDTFA AIASASKGGR IGIEEFAEYL
KLPISDVLRE LFLLFDRNGD GTIDFREYVI GLSILCNPAN TEETIRMAFK LFDMDEDGTI
TEDEFASIIQ SALGLPDLDV SVLFKEIDAD ETGKLSYEEF KEFALKHPAY ATLFTTYLDL
QRHQLSMFEE HDTEPPKGKH SSVRSTETTP LGRNKVCPEG NEEDSSSTSD KKDD
//
