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Q6P1A2

- MBOA5_HUMAN

UniProt

Q6P1A2 - MBOA5_HUMAN

Protein

Lysophospholipid acyltransferase 5

Gene

LPCAT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    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 regulationi

    Activity is inhibited by thimerosal.

    Kineticsi

    1. KM=41.29 µM for palmitoyl-CoA1 Publication
    2. KM=36.65 µM for stearoyl-CoA1 Publication
    3. KM=72.68 µM for oleoyl-CoA1 Publication
    4. KM=201.4 µM for linoleoyl-CoA1 Publication
    5. KM=71.56 µM for arachidonoyl-CoA1 Publication
    6. KM=72.19 µM for 1-palmitoyl-lysophosphatidylcholine1 Publication

    Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates1 Publication

    Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates1 Publication

    Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates1 Publication

    Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates1 Publication

    Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei338 – 3381By similarity
    Active sitei374 – 3741By similarity

    GO - Molecular functioni

    1. 1-acylglycerophosphocholine O-acyltransferase activity Source: MGI

    GO - Biological processi

    1. glycerophospholipid biosynthetic process Source: Reactome
    2. phosphatidylcholine acyl-chain remodeling Source: Reactome
    3. phosphatidylethanolamine acyl-chain remodeling Source: Reactome
    4. phosphatidylserine acyl-chain remodeling Source: Reactome
    5. phospholipid metabolic process Source: Reactome
    6. regulation of plasma lipoprotein particle levels Source: Ensembl
    7. 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.
    REACT_121384. Acyl chain remodelling of PS.
    UniPathwayiUPA00085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysophospholipid acyltransferase 5 (EC:2.3.1.-)
    Short name:
    LPLAT 5
    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 namesi
    Name:LPCAT3
    Synonyms:MBOAT5, OACT5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:30244. LPCAT3.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162394266.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 487487Lysophospholipid acyltransferase 5PRO_0000233382Add
    BLAST

    Proteomic databases

    MaxQBiQ6P1A2.
    PaxDbiQ6P1A2.
    PRIDEiQ6P1A2.

    PTM databases

    PhosphoSiteiQ6P1A2.

    Expressioni

    Tissue specificityi

    Highly expressed in liver, pancreas and adipose tissue. Very low expression in skeletal muscle and heart. Detected in neutrophils.2 Publications

    Gene expression databases

    ArrayExpressiQ6P1A2.
    BgeeiQ6P1A2.
    CleanExiHS_LPCAT3.
    GenevestigatoriQ6P1A2.

    Interactioni

    Protein-protein interaction databases

    BioGridi115464. 2 interactions.
    MINTiMINT-3049790.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6P1A2.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei44 – 6421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei84 – 10421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei111 – 13121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei180 – 20021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei227 – 24721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei285 – 30521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei364 – 38421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei422 – 44221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei453 – 47321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi484 – 4874Di-lysine motif

    Domaini

    The di-lysine motif confers endoplasmic reticulum localization.

    Sequence similaritiesi

    Belongs to the membrane-bound acyltransferase family.Sequence Analysis

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5202.
    HOGENOMiHOG000019529.
    HOVERGENiHBG054659.
    InParanoidiQ6P1A2.
    KOiK13515.
    OMAiWLKVYKS.
    PhylomeDBiQ6P1A2.
    TreeFamiTF106143.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6P1A2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MASSAEGDEG TVVALAGVLQ SGFQELSLNK LATSLGASEQ ALRLIISIFL    50
    GYPFALFYRH YLFYKETYLI HLFHTFTGLS IAYFNFGNQL YHSLLCIVLQ 100
    FLILRLMGRT ITAVLTTFCF QMAYLLAGYY YTATGNYDIK WTMPHCVLTL 150
    KLIGLAVDYF DGGKDQNSLS SEQQKYAIRG VPSLLEVAGF SYFYGAFLVG 200
    PQFSMNHYMK LVQGELIDIP GKIPNSIIPA LKRLSLGLFY LVGYTLLSPH 250
    ITEDYLLTED YDNHPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILTGL 300
    GFNGFEEKGK AKWDACANMK VWLFETNPRF TGTIASFNIN TNAWVARYIF 350
    KRLKFLGNKE LSQGLSLLFL ALWHGLHSGY LVCFQMEFLI VIVERQAARL 400
    IQESPTLSKL AAITVLQPFY YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV 450
    YKSIYFLGHI FFLSLLFILP YIHKAMVPRK EKLKKME 487
    Length:487
    Mass (Da):56,035
    Last modified:July 5, 2004 - v1
    Checksum:i429258B54585B4A7
    GO
    Isoform 2 (identifier: Q6P1A2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         21-100: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:407
    Mass (Da):46,765
    Checksum:i61FFE235FB189231
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti387 – 3871E → K in AAH00664. (PubMed:15489334)Curated
    Sequence conflicti387 – 3871E → K in AAP35646. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631F → L.
    Corresponds to variant rs34196984 [ dbSNP | Ensembl ].
    VAR_050027
    Natural varianti217 – 2171I → T.
    Corresponds to variant rs1984564 [ dbSNP | Ensembl ].
    VAR_050028

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei21 – 10080Missing in isoform 2. 1 PublicationVSP_053680Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS8572.1. [Q6P1A2-1]
    RefSeqiNP_005759.4. NM_005768.5. [Q6P1A2-1]
    UniGeneiHs.655248.

    Genome annotation databases

    EnsembliENST00000261407; ENSP00000261407; ENSG00000111684. [Q6P1A2-1]
    GeneIDi10162.
    KEGGihsa:10162.
    UCSCiuc001qsi.3. human. [Q6P1A2-1]

    Polymorphism databases

    DMDMi74737127.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS8572.1. [Q6P1A2-1 ]
    RefSeqi NP_005759.4. NM_005768.5. [Q6P1A2-1 ]
    UniGenei Hs.655248.

    3D structure databases

    ProteinModelPortali Q6P1A2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115464. 2 interactions.
    MINTi MINT-3049790.

    PTM databases

    PhosphoSitei Q6P1A2.

    Polymorphism databases

    DMDMi 74737127.

    Proteomic databases

    MaxQBi Q6P1A2.
    PaxDbi Q6P1A2.
    PRIDEi Q6P1A2.

    Protocols and materials databases

    DNASUi 10162.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261407 ; ENSP00000261407 ; ENSG00000111684 . [Q6P1A2-1 ]
    GeneIDi 10162.
    KEGGi hsa:10162.
    UCSCi uc001qsi.3. human. [Q6P1A2-1 ]

    Organism-specific databases

    CTDi 10162.
    GeneCardsi GC12M007085.
    H-InvDB HIX0129675.
    HGNCi HGNC:30244. LPCAT3.
    MIMi 611950. gene.
    neXtProti NX_Q6P1A2.
    PharmGKBi PA162394266.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5202.
    HOGENOMi HOG000019529.
    HOVERGENi HBG054659.
    InParanoidi Q6P1A2.
    KOi K13515.
    OMAi WLKVYKS.
    PhylomeDBi Q6P1A2.
    TreeFami TF106143.

    Enzyme and pathway databases

    UniPathwayi UPA00085 .
    Reactomei REACT_120829. Acyl chain remodelling of PC.
    REACT_121369. Acyl chain remodelling of PE.
    REACT_121384. Acyl chain remodelling of PS.

    Miscellaneous databases

    ChiTaRSi LPCAT3. human.
    GeneWikii MBOAT5.
    GenomeRNAii 10162.
    NextBioi 35479285.
    PROi Q6P1A2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6P1A2.
    Bgeei Q6P1A2.
    CleanExi HS_LPCAT3.
    Genevestigatori Q6P1A2.

    Family and domain databases

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

    Publicationsi

    1. 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.
      , 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.
      , 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: ColonImported and PancreasImported.
    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.

    Entry informationi

    Entry nameiMBOA5_HUMAN
    AccessioniPrimary (citable) accession number: Q6P1A2
    Secondary accession number(s): B2RDH0
    , B7Z3N3, Q7KZS1, Q92980, Q9BW40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 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 12
      Human chromosome 12: 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