Q924S1 (PLCD_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase delta
EC=2.3.1.51

Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 4
Short name=1-AGP acyltransferase 4
Short name=1-AGPAT 4
Lysophosphatidic acid acyltransferase delta
Short name=LPAAT-delta

Gene names

Name:

Agpat4

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone By similarity.
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 378	378	1-acyl-sn-glycerol-3-phosphate acyltransferase delta		PRO_0000208199
Regions
	Transmembrane	11 – 31	21	Helical; Potential
	Transmembrane	125 – 145	21	Helical; Potential
	Transmembrane	311 – 331	21	Helical; Potential
	Transmembrane	338 – 358	21	Helical; Potential
	Motif	96 – 101	6	HXXXXD motif

Sequences

	Sequence		Length	Mass (Da)
	Q924S1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 389AA01B7327AE2B	FASTA	378	43,794
	10 20 30 40 50 60 MDLIGLLKSQ FLCHLVFCYV FIASGLIVNA IQLCTLVIWP INKQLFRKIN ARLCYCVSSQ 70 80 90 100 110 120 LVMLLEWWSG TECTIYTDPK ASPHYGKENA IVVLNHKFEI DFLCGWSLAE RLGILGNSKV 130 140 150 160 170 180 LAKKELAYVP IIGWMWYFVE MIFCTRKWEQ DRQTVAKSLL HLRDYPEKYL FLIHCEGTRF 190 200 210 220 230 240 TEKKHQISMQ VAQAKGLPSL KHHLLPRTKG FAITVKCLRD VVPAVYDCTL NFRNNENPTL 250 260 270 280 290 300 LGVLNGKKYH ADCYVRRIPM EDIPEDEDKC SAWLHKLYQE KDAFQEEYYR TGVFPETPWV 310 320 330 340 350 360 PPRRPWSLVN WLFWASLLLY PFFQFLVSMV SSGSSVTLAS LVLIFCMASM GVRWMIGVTE 370 IDKGSAYGNI DNKRKQTD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rattus norvegicus mRNA for lysophosphatidic acid acyltransferase-delta, complete cds." Li W., Suzuki T. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB067572 mRNA. Translation: BAB62290.1. BC086992 mRNA. Translation: AAH86992.1.
IPI	IPI00205071.
RefSeq	NP_596897.1. NM_133406.1.
UniGene	Rn.41595.
3D structure databases
ProteinModelPortal	Q924S1.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000024213.
Proteomic databases
PRIDE	Q924S1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024213; ENSRNOP00000024213; ENSRNOG00000017731.
GeneID	170919.
KEGG	rno:170919.
Organism-specific databases
CTD	56895.
RGD	619916. Agpat4.
Phylogenomic databases
eggNOG	COG0204.
GeneTree	ENSGT00530000062943.
HOGENOM	HOG000006110.
HOVERGEN	HBG008205.
InParanoid	Q924S1.
KO	K13523.
OMA	FFLIHCE.
OrthoDB	EOG4W9J46.
Enzyme and pathway databases
UniPathway	UPA00557; UER00613.
Gene expression databases
Genevestigator	Q924S1.
GermOnline	ENSRNOG00000017731. Rattus norvegicus.
Family and domain databases
InterPro	IPR002123. Plipid/glycerol_acylTrfase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	621403.

Entry information

Entry name

PLCD_RAT

Accession

Primary (citable) accession number: Q924S1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program