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Q6P1A2 (MBOA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6P1A2-1)

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: Q6P1A2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     21-100: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Lysophospholipid acyltransferase 5
PRO_0000233382

Regions

Transmembrane44 – 6421Helical; Potential
Transmembrane84 – 10421Helical; Potential
Transmembrane111 – 13121Helical; Potential
Transmembrane180 – 20021Helical; Potential
Transmembrane227 – 24721Helical; Potential
Transmembrane285 – 30521Helical; Potential
Transmembrane364 – 38421Helical; Potential
Transmembrane422 – 44221Helical; Potential
Transmembrane453 – 47321Helical; Potential
Motif484 – 4874Di-lysine motif

Sites

Active site3381 By similarity
Active site3741 By similarity

Natural variations

Alternative sequence21 – 10080Missing in isoform 2.
VSP_053680
Natural variant631F → L.
Corresponds to variant rs34196984 [ dbSNP | Ensembl ].
VAR_050027
Natural variant2171I → T.
Corresponds to variant rs1984564 [ dbSNP | Ensembl ].
VAR_050028

Experimental info

Sequence conflict3871E → K in AAH00664. Ref.4
Sequence conflict3871E → K in AAP35646. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 429258B54585B4A7

FASTA48756,035
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 61FFE235FB189231
Show »

FASTA40746,765

References

« Hide '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] (ISOFORM 1).
Tissue: Endometrium.
[2]"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. expand/collapse author list , 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] (ISOFORM 2).
[3]"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. expand/collapse author list , 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].
[4]"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] (ISOFORM 1).
Tissue: Colon and Pancreas.
[5]"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 (ISOFORM 1).
[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 (ISOFORM 1/2).
[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.
AK296145 mRNA. Translation: BAH12269.1.
AK315538 mRNA. Translation: BAG37917.1. Different initiation.
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.
BT007000 mRNA. Translation: AAP35646.1.
CCDSCCDS8572.1.
RefSeqNP_005759.4. NM_005768.5. [Q6P1A2-1]
UniGeneHs.655248.

3D structure databases

ProteinModelPortalQ6P1A2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115464. 2 interactions.
MINTMINT-3049790.

PTM databases

PhosphoSiteQ6P1A2.

Polymorphism databases

DMDM74737127.

Proteomic databases

MaxQBQ6P1A2.
PaxDbQ6P1A2.
PRIDEQ6P1A2.

Protocols and materials databases

DNASU10162.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261407; ENSP00000261407; ENSG00000111684. [Q6P1A2-1]
GeneID10162.
KEGGhsa:10162.
UCSCuc001qsi.3. human. [Q6P1A2-1]

Organism-specific databases

CTD10162.
GeneCardsGC12M007085.
H-InvDBHIX0129675.
HGNCHGNC:30244. LPCAT3.
MIM611950. gene.
neXtProtNX_Q6P1A2.
PharmGKBPA162394266.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5202.
HOGENOMHOG000019529.
HOVERGENHBG054659.
InParanoidQ6P1A2.
KOK13515.
OMAWLKVYKS.
PhylomeDBQ6P1A2.
TreeFamTF106143.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00085.

Gene expression databases

ArrayExpressQ6P1A2.
BgeeQ6P1A2.
CleanExHS_LPCAT3.
GenevestigatorQ6P1A2.

Family and domain databases

InterProIPR004299. MBOAT_fam.
[Graphical view]
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLPCAT3. human.
GeneWikiMBOAT5.
GenomeRNAi10162.
NextBio35479285.
PROQ6P1A2.
SOURCESearch...

Entry information

Entry nameMBOA5_HUMAN
AccessionPrimary (citable) accession number: Q6P1A2
Secondary accession number(s): B2RDH0 expand/collapse secondary AC list , B7Z3N3, Q7KZS1, Q92980, Q9BW40
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM