[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1021/bi00408a035; PubMed=2900023 [NCBI, ExPASy, EBI, Israel, Japan] Ikura K., Nasu T.-A., Yokota H., Tsuchiya Y., Sasaki R., Chiba H.; "Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence."; Biochemistry 27:2898-2905(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 189-632. TISSUE=Liver; Ikura K., Nasu T.-A., Yokota H., Sasaki R., Chiba H.; "Cloning of cDNA coding for guinea pig liver transglutaminase."; Agric. Biol. Chem. 51:957-961(1987).
[3]	PROTEIN SEQUENCE OF 2-5. TISSUE=Liver; PubMed=5543674 [NCBI, ExPASy, EBI, Israel, Japan] Connellan J.M., Chung S.I., Whetzel N.K., Bradley L.M., Folk J.E.; "Structural properties of guinea pig liver transglutaminase."; J. Biol. Chem. 246:1093-1098(1971).

Comments

FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N⁵-alkylglutamine + NH₃.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBUNIT: Monomer.
SIMILARITY: Belongs to the transglutaminase superfamily. Transglutaminase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M19646; AAA37056.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00114; BAA00068.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29996; A29996.

3D structure databases

HSSP

P21980; 1KV3. [HSSP ENTRY / PDB]

SMR

P08587; 15-690.

ModBase

P08587.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR008957; Fibronectin_typ-III-like_fold.
IPR013783; Ig-like_fold.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.
IPR002931; Trnsglumase_like.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.30; FN_III-like; 1.
G3DSA:2.60.40.10; Ig-like_fold; 1.

Pfam

PF00927; Transglut_C; 2.
PF01841; Transglut_core; 1.
PF00868; Transglut_N; 1.
Pfam graphical view of domain structure.

SMART

SM00460; TGc; 1.
SMART graphical view of domain structure.

PROSITE

PS00547; TRANSGLUTAMINASES; 1.

BLOCKS

P08587.

Phylogenomic databases

HOVERGEN

P08587; -.

Other

ProtoNet

P08587.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Acyltransferase; Calcium; Direct protein sequencing; Metal-binding; Phosphoprotein; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 690`	`689`	`Protein-glutamine gamma-glutamyltransferase 2.`	`PRO_0000213706`
`ACT_SITE`	`277 277`		`By similarity.`
`ACT_SITE`	`335 335`		`By similarity.`
`ACT_SITE`	`358 358`		`By similarity.`
`METAL`	`398 398`		`Calcium (By similarity).`
`METAL`	`400 400`		`Calcium (By similarity).`
`METAL`	`446 446`		`Calcium (By similarity).`
`METAL`	`451 451`		`Calcium (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`219 219`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`369 369`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`426 426`		`Phosphoserine (By similarity).`
`CONFLICT`	`2 3`		`AE -> EA (in Ref. 3; AA sequence).`
`CONFLICT`	`292 292`		`G -> A (in Ref. 2; BAA00068).`
`CONFLICT`	`336 354`		`CWVESWMTRPDLEPGYEGW -> SLLGGVVDDQAGPGAWVRGV (in Ref. 2; BAA00068).`

Sequence information

Length: 690 AA [This is the length of the unprocessed precursor]

Molecular weight: 77141 Da [This is the MW of the unprocessed precursor]

CRC64: 047223D38DBEA4A4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEDLILERC DLQLEVNGRD HRTADLCRER LVLRRGQPFW LTLHFEGRGY EAGVDTLTFN 

        70         80         90        100        110        120 
AVTGPDPSEE AGTMARFSLS SAVEGGTWSA SAVDQQDSTV SLLLSTPADA PIGLYRLSLE 

       130        140        150        160        170        180 
ASTGYQGSSF VLGHFILLYN PRCPADAVYM DSDQERQEYV LTQQGFIYQG SAKFINGIPW 

       190        200        210        220        230        240 
NFGQFEDGIL DICLMLLDTN PKFLKNAGQD CSRRSRPVYV GRVVSAMVNC NDDQGVLQGR 

       250        260        270        280        290        300 
WDNNYSDGVS PMSWIGSVDI LRRWKDYGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN 

       310        320        330        340        350        360 
FNSAHDQNSN LLIEYFRNES GEIEGNKSEM IWNFHCWVES WMTRPDLEPG YEGWQALDPT 

       370        380        390        400        410        420 
PQEKSEGTYC CGPVPVRAIK EGHLNVKYDA PFVFAEVNAD VVNWIRQKDG SLRKSINHLV 

       430        440        450        460        470        480 
VGLKISTKSV GRDEREDITH TYKYPEGSEE EREAFVRANH LNKLATKEEA QEETGVAMRI 

       490        500        510        520        530        540 
RVGQNMTMGS DFDIFAYITN GTAESHECQL LLCARIVSYN GVLGPVCSTN DLLNLTLDPF 

       550        560        570        580        590        600 
SENSIPLHIL YEKYGDYLTE SNLIKVRGLL IEPAANSYVL AERDIYLENP EIKIRVLGEP 

       610        620        630        640        650        660 
KQNRKLIAEV SLKNPLPVPL LGCIFTVEGA GLTKDQKSVE VPDPVEAGEQ AKVRVDLLPT 

       670        680        690 
EVGLHKLVVN FECDKLKAVK GYRNVIIGPA

P08587 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools