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P08587

- TGM2_CAVCU

UniProt

P08587 - TGM2_CAVCU

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Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene
TGM2
Organism
Cavia cutleri (Guinea pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

Catalytic activityi

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

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei277 – 2771 By similarity
Active sitei335 – 3351 By similarity
Active sitei358 – 3581 By similarity
Metal bindingi398 – 3981Calcium By similarity
Metal bindingi400 – 4001Calcium By similarity
Metal bindingi446 – 4461Calcium By similarity
Metal bindingi451 – 4511Calcium By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB-EC
  4. transaminase activity Source: MGI

GO - Biological processi

  1. peptide cross-linking Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-glutamine gamma-glutamyltransferase 2 (EC:2.3.2.13)
Alternative name(s):
Tissue transglutaminase
Transglutaminase C
Short name:
TG(C)
Short name:
TGC
Short name:
TGase C
Transglutaminase-2
Short name:
TGase-2
Gene namesi
Name:TGM2
OrganismiCavia cutleri (Guinea pig)
Taxonomic identifieri10144 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 690689Protein-glutamine gamma-glutamyltransferase 2PRO_0000213706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei467 – 4671N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP08587. 6 interactions.
MINTiMINT-1522105.

Structurei

3D structure databases

ProteinModelPortaliP08587.
SMRiP08587. Positions 15-690.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG004342.

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.

P08587-1 [UniParc]FASTAAdd to Basket

« Hide

MAEDLILERC DLQLEVNGRD HRTADLCRER LVLRRGQPFW LTLHFEGRGY    50
EAGVDTLTFN AVTGPDPSEE AGTMARFSLS SAVEGGTWSA SAVDQQDSTV 100
SLLLSTPADA PIGLYRLSLE ASTGYQGSSF VLGHFILLYN PRCPADAVYM 150
DSDQERQEYV LTQQGFIYQG SAKFINGIPW NFGQFEDGIL DICLMLLDTN 200
PKFLKNAGQD CSRRSRPVYV GRVVSAMVNC NDDQGVLQGR WDNNYSDGVS 250
PMSWIGSVDI LRRWKDYGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN 300
FNSAHDQNSN LLIEYFRNES GEIEGNKSEM IWNFHCWVES WMTRPDLEPG 350
YEGWQALDPT PQEKSEGTYC CGPVPVRAIK EGHLNVKYDA PFVFAEVNAD 400
VVNWIRQKDG SLRKSINHLV VGLKISTKSV GRDEREDITH TYKYPEGSEE 450
EREAFVRANH LNKLATKEEA QEETGVAMRI RVGQNMTMGS DFDIFAYITN 500
GTAESHECQL LLCARIVSYN GVLGPVCSTN DLLNLTLDPF SENSIPLHIL 550
YEKYGDYLTE SNLIKVRGLL IEPAANSYVL AERDIYLENP EIKIRVLGEP 600
KQNRKLIAEV SLKNPLPVPL LGCIFTVEGA GLTKDQKSVE VPDPVEAGEQ 650
AKVRVDLLPT EVGLHKLVVN FECDKLKAVK GYRNVIIGPA 690
Length:690
Mass (Da):77,141
Last modified:January 23, 2007 - v4
Checksum:i047223D38DBEA4A4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AE → EA AA sequence 1 Publication
Sequence conflicti292 – 2921G → A in BAA00068. 1 Publication
Sequence conflicti336 – 35419CWVES…GYEGW → SLLGGVVDDQAGPGAWVRGV in BAA00068. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19646 mRNA. Translation: AAA37056.1.
D00114 mRNA. Translation: BAA00068.1.
PIRiA29996.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19646 mRNA. Translation: AAA37056.1 .
D00114 mRNA. Translation: BAA00068.1 .
PIRi A29996.

3D structure databases

ProteinModelPortali P08587.
SMRi P08587. Positions 15-690.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08587. 6 interactions.
MINTi MINT-1522105.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG004342.

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. "Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence."
    Ikura K., Nasu T.-A., Yokota H., Tsuchiya Y., Sasaki R., Chiba H.
    Biochemistry 27:2898-2905(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Structural properties of guinea pig liver transglutaminase."
    Connellan J.M., Chung S.I., Whetzel N.K., Bradley L.M., Folk J.E.
    J. Biol. Chem. 246:1093-1098(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-5.
    Tissue: Liver.
  3. "Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: evidence for amino-terminal processing."
    Ikura K., Yokota H., Sasaki R., Chiba H.
    Biochemistry 28:2344-2348(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8 AND 684-690, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Liver.
  4. "Cloning of cDNA coding for guinea pig liver transglutaminase."
    Ikura K., Nasu T.-A., Yokota H., Sasaki R., Chiba H.
    Agric. Biol. Chem. 51:957-961(1987)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-632.
    Tissue: Liver.

Entry informationi

Entry nameiTGM2_CAVCU
AccessioniPrimary (citable) accession number: P08587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 107 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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