ID A0A2U4CNM8_TURTR Unreviewed; 835 AA.
AC A0A2U4CNM8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase delta {ECO:0000256|ARBA:ARBA00040981};
DE EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 4 {ECO:0000256|ARBA:ARBA00041272};
DE AltName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000256|ARBA:ARBA00029536};
DE AltName: Full=Lysophosphatidic acid acyltransferase delta {ECO:0000256|ARBA:ARBA00042940};
GN Name=AGPAT4 {ECO:0000313|RefSeq:XP_019807053.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019807053.1};
RN [1] {ECO:0000313|RefSeq:XP_019807053.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019807053.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z-octadecenoyl)-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:55312, ChEBI:CHEBI:57287, ChEBI:CHEBI:74298,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:138723;
CC Evidence={ECO:0000256|ARBA:ARBA00036892};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55313;
CC Evidence={ECO:0000256|ARBA:ARBA00036892};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-hexadecanoyl-
CC sn-glycero-3-phosphate = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55300,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57518, ChEBI:CHEBI:74298,
CC ChEBI:CHEBI:82928; Evidence={ECO:0000256|ARBA:ARBA00035935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55301;
CC Evidence={ECO:0000256|ARBA:ARBA00035935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-octadecanoyl-
CC sn-glycero-3-phosphate = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55308,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:74565,
CC ChEBI:CHEBI:77130; Evidence={ECO:0000256|ARBA:ARBA00036865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55309;
CC Evidence={ECO:0000256|ARBA:ARBA00036865};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphate = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:55304, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74565, ChEBI:CHEBI:77098;
CC Evidence={ECO:0000256|ARBA:ARBA00036903};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55305;
CC Evidence={ECO:0000256|ARBA:ARBA00036903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00000300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000256|ARBA:ARBA00000300};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004728}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily.
CC {ECO:0000256|ARBA:ARBA00029442}.
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DR RefSeq; XP_019807053.1; XM_019951494.2.
DR AlphaFoldDB; A0A2U4CNM8; -.
DR STRING; 9739.ENSTTRP00000011415; -.
DR GeneID; 101328244; -.
DR InParanoid; A0A2U4CNM8; -.
DR OrthoDB; 3084186at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000245320; Chromosome 12.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd20340; BRcat_RBR_parkin; 1.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR CDD; cd16627; RING-HC_RBR_parkin; 1.
DR CDD; cd21382; RING0_parkin; 1.
DR CDD; cd01798; Ubl_parkin; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR047534; BRcat_RBR_parkin.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR003977; Parkin.
DR InterPro; IPR041565; Parkin_Znf-RING.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR047535; RING-HC_RBR_parkin.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR041170; Znf-RING_14.
DR PANTHER; PTHR10983:SF8; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE DELTA; 1.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF17976; zf-RING_12; 1.
DR Pfam; PF17978; zf-RING_14; 1.
DR PRINTS; PR01475; PARKIN.
DR SMART; SM00647; IBR; 1.
DR SMART; SM00563; PlsC; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|RefSeq:XP_019807053.1};
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 471..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..72
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 234..479
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 77..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 93985 MW; 993FFA13266C3ABE CRC64;
MIVFVRFNSS HGFPVEVDSD TSIFQLKEVV AKQQGVPADQ LRVIFAGKEL RNDLTVRSCD
LDQQSIVHIV LRPQRKVPER STAGRDSPQN TAGGSEREPE SLTRVDLSSS VLPADSVGLA
VILKDDNENG GPPAGRPAGR PTYNSFFVYC KGPCQGVQPG KLRVRCSTCQ QATLTLAQGP
SRWEDVLIPN QMSGECQSPN CPGTRAEFFF KCGAHPTSDK ETSVALNLIT TNSRDITCIT
CMDIRSPVLV FQCNYRHVIC LDCFHLYCVT RLNDRQFVHD PQLGYSLPCV AGCPNSLIKE
LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPSPGCGAG LLPEPSQRKV TCEAGSGLGC
GFVFCRECKE PYHEGECSAL FEASGTVTQA YQVDEKTAER ARWEHASKET IKKTSKPCPR
CHVPVEKHGV FLSPGRPVLW TCSTVGVCGL AEERPPSMDL IALLKSQFLC HLIFCYVFIA
SGLIINTIQL FTLLLWPINK QLFRKINCRL SYCISSQLVM LLEWWSGTEC IIHTDPRAYP
KYGKENAIVV LNHKFEIDFL CGWSLAERFG VLGGSKVLAK KELAYVPIIG WMWYFTEMVF
CTRKWEQDRK TVSESLLHLR DYPEKYFFLI HCEGTRFTEK KHQISMQVAQ AKGLPSLKHH
LLPRTKGFAI TVRSLRNVVS AVYDCTLNFR NNENPTLLGV LNGKKYHADL YVRRIPLGEV
PEDEDRCAAW LHKLYQEKDA LQEEYSRTGT FPGTPMVPPR RPWTLVNWLF WASLLLYPFF
RFLVNMVRSG SSLTLASFVL VFFVASVGVR WMIGVTEIDK GSAYGNMDSK QKHGD
//
