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A6QP57

- TGM3_BOVIN

UniProt

A6QP57 - TGM3_BOVIN

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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

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
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MSGLQSVDWQ IASNRQAHHT ERFYGKDLLV RRGQLFQVSL TLSQGLSSGG
60 70 80 90 100
RVTFTASTGP YPSESANTKA VFPLSNGTSS SGWGAQLVSS RNNVLNISIL
110 120 130 140 150
SPANAPIGRY TLNMQISSQG SDSTLKLGTF ILLFNPWLQA DSVFMSNHAE
160 170 180 190 200
REEYVQEDAG IIFVGSTNRI SMIGWNYGQF EEGILNICLS VLDNSLNFRR
210 220 230 240 250
DPATDVAHRN DPKYVGRVLS AMINGNDDSG VISGNWSGSY TGGRDPRNWN
260 270 280 290 300
GSVEILKEWQ RSGFRPVRYG QCWVFAGTLN TVLRCLGIPS RVITNFNSAH
310 320 330 340 350
DTDQNLSVDV YYDPLGRPMD KGSDSVWNFH VWNEAWFVRS DLGPSYNGWQ
360 370 380 390 400
VLDATPQERS QGVFQCGPAS VIAIREGNVD WDFDMPFIFA EVNADRITWI
410 420 430 440 450
YESNGALKKN SADTHSVGKH ISTKAVGSNS RMDVTEKYKY PEGSSQERQV
460 470 480 490 500
FEKALRKLKP TMSFSATSAS SLAREEREPS ISGRFKVAGV LTVGKEVNLI
510 520 530 540 550
LMLKNLTSDT KTVTVNMTAW TIVYNGTLVH EVWKDSVTKS LNPEEEIEHP
560 570 580 590 600
VKIAYAQYEK YLKADNMIRT TAVCQVTDEP EVVVERDIIL DNPTLTLEVL
610 620 630 640 650
DEARVQKPVN VQMLFSNPLD EPVKDCVLMV EGSGLLLGNL KIDVPALRPK
660 670 680 690
ERSRVRFEIL PTRSGTKQLL ANFSCNKFPA IKAMLSVDVA E
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