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Q6ZWT7

- MBOA2_HUMAN

UniProt

Q6ZWT7 - MBOA2_HUMAN

Protein

Lysophospholipid acyltransferase 2

Gene

MBOAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Acyltransferase which mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes also the acylation of lysophosphatidic acid (LPA) into phosphatidic acid (PA) (LPAAT activity). Has also a very weak lysophosphatidylcholine acyltransferase (LPCAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle.1 Publication

    Catalytic activityi

    Acyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-phosphoethanolamine.
    Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

    Enzyme regulationi

    Partially inhibited by thimerosal.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei342 – 3421By similarity
    Active sitei373 – 3731By similarity

    GO - Molecular functioni

    1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycerophospholipid biosynthetic process Source: Reactome
    2. phosphatidylcholine acyl-chain remodeling Source: Reactome
    3. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
    4. phospholipid metabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_120829. Acyl chain remodelling of PC.
    REACT_121369. Acyl chain remodelling of PE.
    UniPathwayiUPA00085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysophospholipid acyltransferase 2 (EC:2.3.1.-)
    Short name:
    LPLAT 2
    Alternative name(s):
    1-acylglycerophosphate O-acyltransferase (EC:2.3.1.51)
    1-acylglycerophosphoethanolamine O-acyltransferase (EC:2.3.1.n7)
    Lysophosphatidic acid acyltransferase
    Short name:
    LPAAT
    Short name:
    Lyso-PA acyltransferase
    Lysophosphatidylethanolamine acyltransferase
    Short name:
    LPEAT
    Short name:
    Lyso-PE acyltransferase
    Membrane-bound O-acyltransferase domain-containing protein 2
    Short name:
    O-acyltransferase domain-containing protein 2
    Gene namesi
    Name:MBOAT2
    Synonyms:OACT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:25193. MBOAT2.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134987740.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 520520Lysophospholipid acyltransferase 2PRO_0000273020Add
    BLAST

    Proteomic databases

    MaxQBiQ6ZWT7.
    PaxDbiQ6ZWT7.
    PRIDEiQ6ZWT7.

    PTM databases

    PhosphoSiteiQ6ZWT7.

    Expressioni

    Tissue specificityi

    Expressed in neutrophils.1 Publication

    Gene expression databases

    ArrayExpressiQ6ZWT7.
    BgeeiQ6ZWT7.
    CleanExiHS_MBOAT2.
    GenevestigatoriQ6ZWT7.

    Organism-specific databases

    HPAiHPA014836.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000302177.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZWT7.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei22 – 4221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei61 – 8121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei88 – 10821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei184 – 20421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei237 – 25721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei264 – 28421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei366 – 38621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei416 – 43621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei444 – 46421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5202.
    HOGENOMiHOG000015994.
    HOVERGENiHBG058823.
    InParanoidiQ6ZWT7.
    KOiK13517.
    OMAiIVTQVAI.
    OrthoDBiEOG73Z2SW.
    PhylomeDBiQ6ZWT7.
    TreeFamiTF314906.

    Family and domain databases

    InterProiIPR004299. MBOAT_fam.
    [Graphical view]
    PfamiPF03062. MBOAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6ZWT7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAI WFRTYLHSSK    50
    TSSFIRHVVA TLLGLYLALF CFGWYALHFL VQSGISYCIM IIIGVENMHN 100
    YCFVFALGYL TVCQVTRVYI FDYGQYSADF SGPMMIITQK ITSLACEIHD 150
    GMFRKDEELT SSQRDLAVRR MPSLLEYLSY NCNFMGILAG PLCSYKDYIT 200
    FIEGRSYHIT QSGENGKEET QYERTEPSPN TAVVQKLLVC GLSLLFHLTI 250
    CTTLPVEYNI DEHFQATASW PTKIIYLYIS LLAARPKYYF AWTLADAINN 300
    AAGFGFRGYD ENGAARWDLI SNLRIQQIEM STSFKMFLDN WNIQTALWLK 350
    RVCYERTSFS PTIQTFILSA IWHGVYPGYY LTFLTGVLMT LAARAMRNNF 400
    RHYFIEPSQL KLFYDVITWI VTQVAISYTV VPFVLLSIKP SLTFYSSWYY 450
    CLHILGILVL LLLPVKKTQR RKNTHENIQL SQSKKFDEGE NSLGQNSFST 500
    TNNVCNQNQE IASRHSSLKQ 520
    Length:520
    Mass (Da):59,527
    Last modified:April 3, 2007 - v2
    Checksum:i27FFC44815B21288
    GO

    Sequence cautioni

    The sequence BAC11204.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti402 – 4021H → R in BAC11204. (PubMed:16303743)Curated
    Sequence conflicti484 – 4841K → R in BAC85105. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti501 – 5011T → A.
    Corresponds to variant rs16866827 [ dbSNP | Ensembl ].
    VAR_030068

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB305044 mRNA. Translation: BAF93900.1.
    AK027321 mRNA. Translation: BAC85105.1.
    AC012495 Genomic DNA. No translation available.
    AC112723 Genomic DNA. No translation available.
    BC016005 mRNA. Translation: AAH16005.1.
    BC146871 mRNA. Translation: AAI46872.1.
    BC157827 mRNA. Translation: AAI57828.1.
    AK074779 mRNA. Translation: BAC11204.1. Different initiation.
    CCDSiCCDS1660.1.
    RefSeqiNP_620154.2. NM_138799.2.
    UniGeneiHs.467634.
    Hs.593538.

    Genome annotation databases

    EnsembliENST00000305997; ENSP00000302177; ENSG00000143797.
    GeneIDi129642.
    KEGGihsa:129642.
    UCSCiuc002qzg.1. human.

    Polymorphism databases

    DMDMi143811417.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB305044 mRNA. Translation: BAF93900.1 .
    AK027321 mRNA. Translation: BAC85105.1 .
    AC012495 Genomic DNA. No translation available.
    AC112723 Genomic DNA. No translation available.
    BC016005 mRNA. Translation: AAH16005.1 .
    BC146871 mRNA. Translation: AAI46872.1 .
    BC157827 mRNA. Translation: AAI57828.1 .
    AK074779 mRNA. Translation: BAC11204.1 . Different initiation.
    CCDSi CCDS1660.1.
    RefSeqi NP_620154.2. NM_138799.2.
    UniGenei Hs.467634.
    Hs.593538.

    3D structure databases

    ProteinModelPortali Q6ZWT7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000302177.

    PTM databases

    PhosphoSitei Q6ZWT7.

    Polymorphism databases

    DMDMi 143811417.

    Proteomic databases

    MaxQBi Q6ZWT7.
    PaxDbi Q6ZWT7.
    PRIDEi Q6ZWT7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305997 ; ENSP00000302177 ; ENSG00000143797 .
    GeneIDi 129642.
    KEGGi hsa:129642.
    UCSCi uc002qzg.1. human.

    Organism-specific databases

    CTDi 129642.
    GeneCardsi GC02M008910.
    H-InvDB HIX0001805.
    HGNCi HGNC:25193. MBOAT2.
    HPAi HPA014836.
    MIMi 611949. gene.
    neXtProti NX_Q6ZWT7.
    PharmGKBi PA134987740.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5202.
    HOGENOMi HOG000015994.
    HOVERGENi HBG058823.
    InParanoidi Q6ZWT7.
    KOi K13517.
    OMAi IVTQVAI.
    OrthoDBi EOG73Z2SW.
    PhylomeDBi Q6ZWT7.
    TreeFami TF314906.

    Enzyme and pathway databases

    UniPathwayi UPA00085 .
    Reactomei REACT_120829. Acyl chain remodelling of PC.
    REACT_121369. Acyl chain remodelling of PE.

    Miscellaneous databases

    ChiTaRSi MBOAT2. human.
    GenomeRNAii 129642.
    NextBioi 82616.
    PROi Q6ZWT7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZWT7.
    Bgeei Q6ZWT7.
    CleanExi HS_MBOAT2.
    Genevestigatori Q6ZWT7.

    Family and domain databases

    InterProi IPR004299. MBOAT_fam.
    [Graphical view ]
    Pfami PF03062. MBOAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation of lysophospholipids in the yeast Saccharomyces cerevisiae."
      Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M., Miyagawa H., Nozaki H., Nakayama R., Kumagai H.
      J. Biol. Chem. 282:34288-34298(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.
      , 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].
      Tissue: Embryo.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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].
      Tissue: Brain, Lung and Testis.
    5. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-520.
      Tissue: Teratocarcinoma.
    6. "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.

    Entry informationi

    Entry nameiMBOA2_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZWT7
    Secondary accession number(s): A9EDR2, Q8NCE7, Q96KY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 76 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3