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Q7TPN3

- PIGV_MOUSE

UniProt

Q7TPN3 - PIGV_MOUSE

Protein

GPI mannosyltransferase 2

Gene

Pigv

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (25 Jul 2006)
      Previous versions | rss
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    Functioni

    Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly By similarity.By similarity

    Pathwayi

    GO - Molecular functioni

    1. mannosyltransferase activity Source: Ensembl

    GO - Biological processi

    1. GPI anchor biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    GPI-anchor biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00196.

    Protein family/group databases

    CAZyiGT76. Glycosyltransferase Family 76.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GPI mannosyltransferase 2 (EC:2.4.1.-)
    Alternative name(s):
    GPI mannosyltransferase II
    Short name:
    GPI-MT-II
    Phosphatidylinositol-glycan biosynthesis class V protein
    Short name:
    PIG-V
    Gene namesi
    Name:Pigv
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2442480. Pigv.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 493493GPI mannosyltransferase 2PRO_0000246235Add
    BLAST

    Post-translational modificationi

    Not N-glycosylated.By similarity

    Proteomic databases

    PRIDEiQ7TPN3.

    PTM databases

    PhosphoSiteiQ7TPN3.

    Expressioni

    Gene expression databases

    BgeeiQ7TPN3.
    GenevestigatoriQ7TPN3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TPN3.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini35 – 7743LumenalSequence AnalysisAdd
    BLAST
    Topological domaini99 – 11315CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini135 – 1362LumenalSequence Analysis
    Topological domaini158 – 1614CytoplasmicSequence Analysis
    Topological domaini183 – 19210LumenalSequence Analysis
    Topological domaini214 – 23421CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini256 – 32772LumenalSequence AnalysisAdd
    BLAST
    Topological domaini349 – 37830CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini400 – 46970LumenalSequence AnalysisAdd
    BLAST
    Topological domaini491 – 4933CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei14 – 3421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei78 – 9821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei114 – 13421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei137 – 15721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei162 – 18221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei193 – 21321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei235 – 25521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei328 – 34821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei379 – 39921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei470 – 49021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PIGV family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5542.
    GeneTreeiENSGT00390000013174.
    HOGENOMiHOG000232162.
    HOVERGENiHBG080592.
    InParanoidiQ7TPN3.
    KOiK07542.
    OMAiLNAGYIC.
    OrthoDBiEOG7VDXPB.
    PhylomeDBiQ7TPN3.
    TreeFamiTF314515.

    Family and domain databases

    InterProiIPR007315. GPI_Mannosyltransferase_2.
    [Graphical view]
    PANTHERiPTHR12468. PTHR12468. 1 hit.
    PfamiPF04188. Mannosyl_trans2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7TPN3-1) [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

    MGLLDPSQKE VLRFAVNCRI LTLVLQALFN LIIPDHHADA FCPPRLAPSG    50
    SADQLVEGLL GGLSRWDAEH FLFIAEHGYL YEHNFAFFPG FPLALLMGTE 100
    LLRPLQGLLS QRSCLLVSVA LLNLLFSVLA AVALHDLGCL VLHCPRQALC 150
    AALLFCISPA NVFLAAGYSE ALFAFLTFSA MGQLERGRGW ASGLLFALAA 200
    GVRSNGLVSL GFLLHSQCRG FCSSLAVLSP WKPLVKLMAS VCLSVLIVSL 250
    PFALFQYRAY IQFCSPGSAP SIPEPLLQLA ADKGYRLAGE NAPPWCSWDL 300
    PLIYNYIQDV YWNVGLLRYY ELKQVPNFLL ATPVTVLVVW ATWTYVTTHP 350
    WLCLTLGLQR TKDRENPEKP HRGFLSPKVF VYLVHAAALL VFGGLCMHVQ 400
    VLTRFLASST PIMYWFPAHL LQDQEPLLRC VDTEPGKLPQ EKSPPGQKAP 450
    RNCLMKLFYD WKRCSPVTRC VLVYFLTYWL LGLILHCNFL PWT 493
    Length:493
    Mass (Da):55,026
    Last modified:July 25, 2006 - v2
    Checksum:i8A176D43F3CB7F4C
    GO
    Isoform 2 (identifier: Q7TPN3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         27-400: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:119
    Mass (Da):13,882
    Checksum:i0B052659B20754C8
    GO

    Sequence cautioni

    The sequence BAC33023.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti218 – 2181C → F in BAC34995. (PubMed:16141072)Curated
    Sequence conflicti460 – 4601D → N in AAH55060. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei27 – 400374Missing in isoform 2. 1 PublicationVSP_019840Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK046527 mRNA. Translation: BAC32773.1.
    AK047322 mRNA. Translation: BAC33023.1. Different initiation.
    AK052446 mRNA. Translation: BAC34995.1.
    AK080590 mRNA. Translation: BAC37950.1.
    AK080858 mRNA. Translation: BAC38047.1.
    AK148285 mRNA. Translation: BAE28458.1.
    BC055060 mRNA. Translation: AAH55060.1.
    CCDSiCCDS18755.1. [Q7TPN3-1]
    CCDS51322.1. [Q7TPN3-2]
    RefSeqiNP_001139427.1. NM_001145955.1.
    NP_001139428.1. NM_001145956.1. [Q7TPN3-2]
    NP_848813.3. NM_178698.5. [Q7TPN3-1]
    XP_006538810.1. XM_006538747.1. [Q7TPN3-1]
    UniGeneiMm.217004.

    Genome annotation databases

    EnsembliENSMUST00000062118; ENSMUSP00000050647; ENSMUSG00000043257. [Q7TPN3-1]
    ENSMUST00000067902; ENSMUSP00000065601; ENSMUSG00000043257. [Q7TPN3-2]
    GeneIDi230801.
    KEGGimmu:230801.
    UCSCiuc008vdf.2. mouse. [Q7TPN3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK046527 mRNA. Translation: BAC32773.1 .
    AK047322 mRNA. Translation: BAC33023.1 . Different initiation.
    AK052446 mRNA. Translation: BAC34995.1 .
    AK080590 mRNA. Translation: BAC37950.1 .
    AK080858 mRNA. Translation: BAC38047.1 .
    AK148285 mRNA. Translation: BAE28458.1 .
    BC055060 mRNA. Translation: AAH55060.1 .
    CCDSi CCDS18755.1. [Q7TPN3-1 ]
    CCDS51322.1. [Q7TPN3-2 ]
    RefSeqi NP_001139427.1. NM_001145955.1.
    NP_001139428.1. NM_001145956.1. [Q7TPN3-2 ]
    NP_848813.3. NM_178698.5. [Q7TPN3-1 ]
    XP_006538810.1. XM_006538747.1. [Q7TPN3-1 ]
    UniGenei Mm.217004.

    3D structure databases

    ProteinModelPortali Q7TPN3.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT76. Glycosyltransferase Family 76.

    PTM databases

    PhosphoSitei Q7TPN3.

    Proteomic databases

    PRIDEi Q7TPN3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000062118 ; ENSMUSP00000050647 ; ENSMUSG00000043257 . [Q7TPN3-1 ]
    ENSMUST00000067902 ; ENSMUSP00000065601 ; ENSMUSG00000043257 . [Q7TPN3-2 ]
    GeneIDi 230801.
    KEGGi mmu:230801.
    UCSCi uc008vdf.2. mouse. [Q7TPN3-1 ]

    Organism-specific databases

    CTDi 55650.
    MGIi MGI:2442480. Pigv.

    Phylogenomic databases

    eggNOGi COG5542.
    GeneTreei ENSGT00390000013174.
    HOGENOMi HOG000232162.
    HOVERGENi HBG080592.
    InParanoidi Q7TPN3.
    KOi K07542.
    OMAi LNAGYIC.
    OrthoDBi EOG7VDXPB.
    PhylomeDBi Q7TPN3.
    TreeFami TF314515.

    Enzyme and pathway databases

    UniPathwayi UPA00196 .

    Miscellaneous databases

    ChiTaRSi PIGV. mouse.
    NextBioi 380172.
    PROi Q7TPN3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7TPN3.
    Genevestigatori Q7TPN3.

    Family and domain databases

    InterProi IPR007315. GPI_Mannosyltransferase_2.
    [Graphical view ]
    PANTHERi PTHR12468. PTHR12468. 1 hit.
    Pfami PF04188. Mannosyl_trans2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Adrenal gland, Cerebellum, Corpora quadrigemina and Lung.
    2. "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).
      Strain: FVB/N.
      Tissue: Colon.

    Entry informationi

    Entry nameiPIGV_MOUSE
    AccessioniPrimary (citable) accession number: Q7TPN3
    Secondary accession number(s): Q8BGL2
    , Q8BJR5, Q8BWH9, Q8BXF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3