Q9NRZ7 (PLCC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	AGPAT3
ORF Names:	UNQ759/PRO1490

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.9.
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	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Non-traceable author statement. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NRZ7-1)

Also known as: Gamma-1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NRZ7-2)

Also known as: Gamma-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.

Isoform 3 (identifier: Q9NRZ7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MGLLAFLKTQ...CRLAYSLWSQ → MQSGGSLPFC...SANALPLSAE

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	1-acyl-sn-glycerol-3-phosphate acyltransferase gamma		PRO_0000208194
Regions
	Topological domain	1 – 124	124	Cytoplasmic Potential
	Transmembrane	125 – 145	21	Helical; Potential
	Topological domain	146 – 316	171	Lumenal Potential
	Transmembrane	317 – 339	23	Helical; Potential
	Topological domain	340 – 376	37	Cytoplasmic Potential
	Motif	96 – 101	6	HXXXXD motif
Natural variations
	Alternative sequence	1 – 62	62	Missing in isoform 2.		VSP_005072
	Alternative sequence	1 – 60	60	MGLLA…SLWSQ → MQSGGSLPFCCYLPSVSSQL LLRESYCNFIKRTQCKSSKL MFSRDFLSGQKYCRCLLWAL PDHPRRRGPTSANALPLSAE in isoform 3.		VSP_013144
Experimental info
	Sequence conflict	74	1	T → P in CAD38635. Ref.7
	Sequence conflict	358 – 376	19	VTEIE…FKKKE → ESLEPGRWRLQ in AAQ89067. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Gamma-1) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C12CDBB7CC363852	FASTA	376	43,381
	10 20 30 40 50 60 MGLLAFLKTQ FVLHLLVGFV FVVSGLVINF VQLCTLALWP VSKQLYRRLN CRLAYSLWSQ 70 80 90 100 110 120 LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI DFLCGWTMCE RFGVLGSSKV 130 140 150 160 170 180 LAKKELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVVEGLR RLSDYPEYMW FLLYCEGTRF 190 200 210 220 230 240 TETKHRVSME VAAAKGLPVL KYHLLPRTKG FTTAVKCLRG TVAAVYDVTL NFRGNKNPSL 250 260 270 280 290 300 LGILYGKKYE ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE KDALQEIYNQ KGMFPGEQFK 310 320 330 340 350 360 PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE 370 IEKGSSYGNQ EFKKKE
	Isoform 2 (Gamma-2) [UniParc]. Checksum: FFB9EA98F4F5C204	FASTA	314	36,271
	10 20 30 40 50 60 MLLEWWSCTE CTLFTDQATV ERFGKEHAVI ILNHNFEIDF LCGWTMCERF GVLGSSKVLA 70 80 90 100 110 120 KKELLYVPLI GWTWYFLEIV FCKRKWEEDR DTVVEGLRRL SDYPEYMWFL LYCEGTRFTE 130 140 150 160 170 180 TKHRVSMEVA AAKGLPVLKY HLLPRTKGFT TAVKCLRGTV AAVYDVTLNF RGNKNPSLLG 190 200 210 220 230 240 ILYGKKYEAD MCVRRFPLED IPLDEKEAAQ WLHKLYQEKD ALQEIYNQKG MFPGEQFKPA 250 260 270 280 290 300 RRPWTLLNFL SWATILLSPL FSFVLGVFAS GSPLLILTFL GFVGAASFGV RRLIGVTEIE 310 KGSSYGNQEF KKKE
	Isoform 3 [UniParc]. Checksum: 9729B3AE9FB5E518	FASTA	396	45,514
	10 20 30 40 50 60 MQSGGSLPFC CYLPSVSSQL LLRESYCNFI KRTQCKSSKL MFSRDFLSGQ KYCRCLLWAL 70 80 90 100 110 120 PDHPRRRGPT SANALPLSAE LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI 130 140 150 160 170 180 DFLCGWTMCE RFGVLGSSKV LAKKELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVVEGLR 190 200 210 220 230 240 RLSDYPEYMW FLLYCEGTRF TETKHRVSME VAAAKGLPVL KYHLLPRTKG FTTAVKCLRG 250 260 270 280 290 300 TVAAVYDVTL NFRGNKNPSL LGILYGKKYE ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE 310 320 330 340 350 360 KDALQEIYNQ KGMFPGEQFK PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT 370 380 390 FLGFVGAASF GVRRLIGVTE IEKGSSYGNQ EFKKKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The structure and functions of human lysophosphatidic acid acyltransferases." Leung D.W. Front. Biosci. 6:D944-D953(2001) [PubMed: 11487472] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	"Isolation of a novel gene encoding 1-acylglycerol-3-phosphate O-acyltransferase 3 (AGPAT3) from the human chromosome 21q22.3." Nagamine K., Kudoh J., Minoshima S., Kawasaki K., Hase T., Shimizu N. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal liver.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed: 10830953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain, Skin and Testis.
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372 (ISOFORM 3).
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-376. Tissue: Melanoma.
[9]	"Membrane topology of human AGPAT3 (LPAAT3)." Schmidt J.A., Yvone G.M., Brown W.J. Biochem. Biophys. Res. Commun. 397:661-667(2010) [PubMed: 20537980] [Abstract] Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF156774 mRNA. Translation: AAF80336.1. AF156775 mRNA. Translation: AAF80337.1. AB040138 mRNA. Translation: BAB18943.1. AY358704 mRNA. Translation: AAQ89067.1. AP001054 Genomic DNA. No translation available. CH471079 Genomic DNA. Translation: EAX09461.1. CH471079 Genomic DNA. Translation: EAX09463.1. CH471079 Genomic DNA. Translation: EAX09464.1. CH471079 Genomic DNA. Translation: EAX09465.1. BC011971 mRNA. Translation: AAH11971.1. BC040603 mRNA. Translation: AAH40603.1. BC063552 mRNA. Translation: AAH63552.1. AK125804 mRNA. Translation: BAC86299.1. AL832919 mRNA. Translation: CAD38635.2.
IPI	IPI00217814. IPI00445527. IPI00749011.
RefSeq	NP_001032642.1. NM_001037553.1. NP_064517.1. NM_020132.4.
UniGene	Hs.248785.
3D structure databases
ProteinModelPortal	Q9NRZ7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRZ7. 1 interaction.
STRING	Q9NRZ7.
PTM databases
PhosphoSite	Q9NRZ7.
Polymorphism databases
DMDM	12643817.
Proteomic databases
PRIDE	Q9NRZ7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000291572; ENSP00000291572; ENSG00000160216. ENST00000327505; ENSP00000332989; ENSG00000160216. ENST00000398058; ENSP00000381135; ENSG00000160216. ENST00000398061; ENSP00000381138; ENSG00000160216. ENST00000398063; ENSP00000381140; ENSG00000160216.
GeneID	56894.
KEGG	hsa:56894.
UCSC	uc002zdv.1. human. uc002zdx.1. human.
Organism-specific databases
CTD	56894.
GeneCards	GC21P045285.
H-InvDB	HIX0016159.
HGNC	HGNC:326. AGPAT3.
neXtProt	NX_Q9NRZ7.
PharmGKB	PA24623.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04596.
GeneTree	ENSGT00530000062943.
HOGENOM	HBG714204.
HOVERGEN	HBG008205.
InParanoid	Q9NRZ7.
OMA	INFIQLC.
OrthoDB	EOG4W6NW5.
PhylomeDB	Q9NRZ7.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000160216-MONOMER.
Reactome	REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	Q9NRZ7.
Bgee	Q9NRZ7.
CleanEx	HS_AGPAT3.
Genevestigator	Q9NRZ7.
GermOnline	ENSG00000160216. Homo sapiens.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
KO	K13523.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	62319.

Entry information

Entry name

PLCC_HUMAN

Accession

Primary (citable) accession number: Q9NRZ7
Secondary accession number(s): D3DSL2 , Q3ZCU2, Q6UWP6, Q6ZUC6, Q8N3Q7, Q9NRZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.