Q6P1A2 (MBOA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysophospholipid acyltransferase 5
Short name=LPLAT 5
EC=2.3.1.-

Alternative name(s):
1-acylglycerophosphocholine O-acyltransferase
EC=2.3.1.23
1-acylglycerophosphoserine O-acyltransferase
EC=2.3.1.n6
Lysophosphatidylcholine acyltransferase
Short name=LPCAT
Short name=Lyso-PC acyltransferase
Lysophosphatidylcholine acyltransferase 3
Short name=Lyso-PC acyltransferase 3
Lysophosphatidylserine acyltransferase
Short name=LPSAT
Short name=Lyso-PS acyltransferase
Membrane-bound O-acyltransferase domain-containing protein 5
Short name=O-acyltransferase domain-containing protein 5

Gene names

Name:	LPCAT3
Synonyms:	MBOAT5, OACT5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Ref.7 Ref.8
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. Acyl-CoA + 1-acyl-sn-glycero-3-phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-phosphatidylserine.
Enzyme regulation	Activity is inhibited by thimerosal.
Pathway	Lipid metabolism; phospholipid metabolism.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.7.
Tissue specificity	Highly expressed in liver, pancreas and adipose tissue. Very low expression in skeletal muscle and heart. Detected in neutrophils. Ref.7 Ref.8
Domain	The di-lysine motif confers endoplasmic reticulum localization.
Sequence similarities	Belongs to the membrane-bound acyltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=41.29 µM for palmitoyl-CoA Ref.7 KM=36.65 µM for stearoyl-CoA KM=72.68 µM for oleoyl-CoA KM=201.4 µM for linoleoyl-CoA KM=71.56 µM for arachidonoyl-CoA KM=72.19 µM for 1-palmitoyl-lysophosphatidylcholine Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates
Sequence caution	The sequence AAB51326.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAC51640.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAG37917.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycerophospholipid biosynthetic process Traceable author statement. Source: Reactome phosphatidylcholine acyl-chain remodeling Traceable author statement. Source: Reactome phosphatidylethanolamine acyl-chain remodeling Traceable author statement. Source: Reactome phosphatidylserine acyl-chain remodeling Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	1-acylglycerophosphocholine 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 – 487	487	Lysophospholipid acyltransferase 5		PRO_0000233382
Regions
	Transmembrane	44 – 64	21	Helical; Potential
	Transmembrane	84 – 104	21	Helical; Potential
	Transmembrane	111 – 131	21	Helical; Potential
	Transmembrane	180 – 200	21	Helical; Potential
	Transmembrane	227 – 247	21	Helical; Potential
	Transmembrane	285 – 305	21	Helical; Potential
	Transmembrane	364 – 384	21	Helical; Potential
	Transmembrane	422 – 442	21	Helical; Potential
	Transmembrane	453 – 473	21	Helical; Potential
	Motif	484 – 487	4	Di-lysine motif
Sites
	Active site	428	1	Potential
Natural variations
	Natural variant	63	1	F → L. Corresponds to variant rs34196984 [ dbSNP | Ensembl ].		VAR_050027
	Natural variant	217	1	I → T. Corresponds to variant rs1984564 [ dbSNP | Ensembl ].		VAR_050028
Experimental info
	Sequence conflict	387	1	E → K in AAH00664. Ref.3
	Sequence conflict	387	1	E → K in AAP35646. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q6P1A2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 429258B54585B4A7	FASTA	487	56,035
	10 20 30 40 50 60 MASSAEGDEG TVVALAGVLQ SGFQELSLNK LATSLGASEQ ALRLIISIFL GYPFALFYRH 70 80 90 100 110 120 YLFYKETYLI HLFHTFTGLS IAYFNFGNQL YHSLLCIVLQ FLILRLMGRT ITAVLTTFCF 130 140 150 160 170 180 QMAYLLAGYY YTATGNYDIK WTMPHCVLTL KLIGLAVDYF DGGKDQNSLS SEQQKYAIRG 190 200 210 220 230 240 VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVQGELIDIP GKIPNSIIPA LKRLSLGLFY 250 260 270 280 290 300 LVGYTLLSPH ITEDYLLTED YDNHPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILTGL 310 320 330 340 350 360 GFNGFEEKGK AKWDACANMK VWLFETNPRF TGTIASFNIN TNAWVARYIF KRLKFLGNKE 370 380 390 400 410 420 LSQGLSLLFL ALWHGLHSGY LVCFQMEFLI VIVERQAARL IQESPTLSKL AAITVLQPFY 430 440 450 460 470 480 YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YKSIYFLGHI FFLSLLFILP YIHKAMVPRK EKLKKME

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Endometrium.
[2]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: Colon and Pancreas.
[4]	"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination." Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A. Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-487.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-487.
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-487.
[7]	"Identification and characterization of a major liver lysophosphatidylcholine acyltransferase." Zhao Y., Chen Y.Q., Bonacci T.M., Bredt D.S., Li S., Bensch W.R., Moller D.E., Kowala M., Konrad R.J., Cao G. J. Biol. Chem. 283:8258-8265(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[8]	"Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils." Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R. J. Biol. Chem. 283:30235-30245(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX648009 mRNA. No translation available. AC006512 Genomic DNA. No translation available. BC000664 mRNA. Translation: AAH00664.2. BC065194 mRNA. Translation: AAH65194.1. U47924 Genomic DNA. Translation: AAB51326.1. Different initiation. U72515 mRNA. Translation: AAC51640.1. Different initiation. AK315538 mRNA. Translation: BAG37917.1. Different initiation. BT007000 mRNA. Translation: AAP35646.1.
IPI	IPI00306419.
RefSeq	NP_005759.4. NM_005768.5.
UniGene	Hs.655248.
3D structure databases
ProteinModelPortal	Q6P1A2.
ModBase	Search...
PTM databases
PhosphoSite	Q6P1A2.
Polymorphism databases
DMDM	74737127.
Proteomic databases
PaxDb	Q6P1A2.
PRIDE	Q6P1A2.
Protocols and materials databases
DNASU	10162.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261407; ENSP00000261407; ENSG00000111684.
GeneID	10162.
KEGG	hsa:10162.
UCSC	uc001qsi.3. human.
Organism-specific databases
CTD	10162.
GeneCards	GC12M007085.
H-InvDB	HIX0129675.
HGNC	HGNC:30244. LPCAT3.
MIM	611950. gene.
neXtProt	NX_Q6P1A2.
PharmGKB	PA162394266.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5202.
HOGENOM	HOG000019529.
HOVERGEN	HBG054659.
InParanoid	Q6P1A2.
KO	K13515.
OMA	WLKVYKS.
OrthoDB	EOG4G1MG9.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00085.
Gene expression databases
ArrayExpress	Q6P1A2.
Bgee	Q6P1A2.
CleanEx	HS_LPCAT3.
Genevestigator	Q6P1A2.
GermOnline	ENSG00000111684. Homo sapiens.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LPCAT3. human.
GenomeRNAi	10162.
NextBio	38474.
SOURCE	Search...

Entry information

Entry name

MBOA5_HUMAN

Accession

Primary (citable) accession number: Q6P1A2
Secondary accession number(s): B2RDH0 , Q7KZS1, Q92980, Q9BW40

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 84 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.