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A6QP57

- TGM3_BOVIN

UniProt

A6QP57 - TGM3_BOVIN

Protein

Protein-glutamine gamma-glutamyltransferase E

Gene

TGM3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold. In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath By similarity.By similarity

    Catalytic activityi

    Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.PROSITE-ProRule annotation

    Cofactori

    Binds 3 calcium ions per subunit. Binds 1 calcium ion as a zymogen, and binds 2 more calcium ions, or other divalent metal cations, after proteolytic processing By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi221 – 2211Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi224 – 2241Calcium 1By similarity
    Metal bindingi226 – 2261Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi227 – 2271Calcium 1By similarity
    Active sitei272 – 2721PROSITE-ProRule annotation
    Metal bindingi301 – 3011Calcium 2By similarity
    Metal bindingi303 – 3031Calcium 2By similarity
    Metal bindingi305 – 3051Calcium 2By similarity
    Metal bindingi307 – 3071Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi324 – 3241Calcium 2By similarity
    Active sitei330 – 3301PROSITE-ProRule annotation
    Active sitei353 – 3531PROSITE-ProRule annotation
    Metal bindingi393 – 3931Calcium 3By similarity
    Metal bindingi414 – 4141Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi442 – 4421Calcium 3By similarity
    Metal bindingi447 – 4471Calcium 3By similarity
    Sitei465 – 4662Cleavage; by CTSL

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. keratinization Source: UniProtKB-KW
    2. peptide cross-linking Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Keratinization

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-glutamine gamma-glutamyltransferase E (EC:2.3.2.13)
    Alternative name(s):
    Transglutaminase E
    Short name:
    TG(E)
    Short name:
    TGE
    Short name:
    TGase E
    Transglutaminase-3
    Short name:
    TGase-3
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TGM3
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chainPRO_0000408949Add
    BLAST
    Chaini466 – 691226Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chainPRO_0000408950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101PhosphotyrosineBy similarity
    Modified residuei111 – 1111PhosphothreonineBy similarity

    Post-translational modificationi

    Activated by proteolytic processing. In vitro activation is commonly achieved by cleavage with dispase, a neutral bacterial protease. Physiological activation may be catalyzed by CTSL and, to a lesser extent, by CTSS By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Zymogen

    Proteomic databases

    PaxDbiA6QP57.

    Interactioni

    Subunit structurei

    Consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000006432.

    Structurei

    3D structure databases

    ProteinModelPortaliA6QP57.
    SMRiA6QP57. Positions 3-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG80379.
    HOGENOMiHOG000231695.
    HOVERGENiHBG004342.
    InParanoidiA6QP57.
    KOiK05620.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view]
    PANTHERiPTHR11590. PTHR11590. 1 hit.
    PfamiPF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
    SMARTiSM00460. TGc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A6QP57-1 [UniParc]FASTAAdd to Basket

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    MSGLQSVDWQ IASNRQAHHT ERFYGKDLLV RRGQLFQVSL TLSQGLSSGG    50
    RVTFTASTGP YPSESANTKA VFPLSNGTSS SGWGAQLVSS RNNVLNISIL 100
    SPANAPIGRY TLNMQISSQG SDSTLKLGTF ILLFNPWLQA DSVFMSNHAE 150
    REEYVQEDAG IIFVGSTNRI SMIGWNYGQF EEGILNICLS VLDNSLNFRR 200
    DPATDVAHRN DPKYVGRVLS AMINGNDDSG VISGNWSGSY TGGRDPRNWN 250
    GSVEILKEWQ RSGFRPVRYG QCWVFAGTLN TVLRCLGIPS RVITNFNSAH 300
    DTDQNLSVDV YYDPLGRPMD KGSDSVWNFH VWNEAWFVRS DLGPSYNGWQ 350
    VLDATPQERS QGVFQCGPAS VIAIREGNVD WDFDMPFIFA EVNADRITWI 400
    YESNGALKKN SADTHSVGKH ISTKAVGSNS RMDVTEKYKY PEGSSQERQV 450
    FEKALRKLKP TMSFSATSAS SLAREEREPS ISGRFKVAGV LTVGKEVNLI 500
    LMLKNLTSDT KTVTVNMTAW TIVYNGTLVH EVWKDSVTKS LNPEEEIEHP 550
    VKIAYAQYEK YLKADNMIRT TAVCQVTDEP EVVVERDIIL DNPTLTLEVL 600
    DEARVQKPVN VQMLFSNPLD EPVKDCVLMV EGSGLLLGNL KIDVPALRPK 650
    ERSRVRFEIL PTRSGTKQLL ANFSCNKFPA IKAMLSVDVA E 691
    Length:691
    Mass (Da):76,791
    Last modified:August 21, 2007 - v1
    Checksum:i67DB0852E0973B4D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC149161 mRNA. Translation: AAI49162.1.
    RefSeqiNP_001095318.1. NM_001101848.1.
    UniGeneiBt.13628.

    Genome annotation databases

    GeneIDi505080.
    KEGGibta:505080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC149161 mRNA. Translation: AAI49162.1 .
    RefSeqi NP_001095318.1. NM_001101848.1.
    UniGenei Bt.13628.

    3D structure databases

    ProteinModelPortali A6QP57.
    SMRi A6QP57. Positions 3-691.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000006432.

    Proteomic databases

    PaxDbi A6QP57.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 505080.
    KEGGi bta:505080.

    Organism-specific databases

    CTDi 7053.

    Phylogenomic databases

    eggNOGi NOG80379.
    HOGENOMi HOG000231695.
    HOVERGENi HBG004342.
    InParanoidi A6QP57.
    KOi K05620.

    Miscellaneous databases

    NextBioi 20866974.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProi IPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view ]
    PANTHERi PTHR11590. PTHR11590. 1 hit.
    Pfami PF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
    SMARTi SM00460. TGc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Basal ganglia.

    Entry informationi

    Entry nameiTGM3_BOVIN
    AccessioniPrimary (citable) accession number: A6QP57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3