[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1979171 [NCBI, ExPASy, EBI, Israel, Japan] Phillips M.A., Stewart B.E., Qin Q., Chakravarty R., Floyd E.E., Jetten A.M., Rice R.H.; "Primary structure of keratinocyte transglutaminase."; Proc. Natl. Acad. Sci. U.S.A. 87:9333-9337(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum.
CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N⁵-alkylglutamine + NH₃.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
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

M57263; AAA63495.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC097305; AAH97305.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

B38423; B38423.

NP_113847.1; -.

3D structure databases

HSSP

P00488; 1EVU. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P23606.

PTM databases

PhosphoSite

P23606; -.

Organism-specific databases

RGD

61838; Tgm1.

Gene expression databases

ArrayExpress

P23606; -.

GermOnline

ENSRNOG00000020136; Rattus norvegicus.

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

P23606.

Genome annotation databases

Ensembl

ENSRNOG00000020136; Rattus norvegicus. [Contig view]

GeneID

60335; -.

KEGG

rno:60335; -.

Phylogenomic databases

HOVERGEN

P23606; -.

Other

ProtoNet

P23606.

UniRef

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

Keywords

Acyltransferase; Calcium; Keratinization; Membrane; Metal-binding; Phosphoprotein; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 824`	`824`	`Protein-glutamine gamma-glutamyltransferase K.`	`PRO_0000213704`
`ACT_SITE`	`385 385`		`By similarity.`
`ACT_SITE`	`444 444`		`By similarity.`
`ACT_SITE`	`467 467`		`By similarity.`
`METAL`	`507 507`		`Calcium (By similarity).`
`METAL`	`509 509`		`Calcium (By similarity).`
`METAL`	`556 556`		`Calcium (By similarity).`
`METAL`	`561 561`		`Calcium (By similarity).`
`MOD_RES`	`70 70`		`Phosphoserine (By similarity).`
`MOD_RES`	`100 100`		`Phosphoserine (By similarity).`
`MOD_RES`	`103 103`		`Phosphoserine (By similarity).`

Sequence information

Length: 824 AA [This is the length of the unprocessed precursor]

Molecular weight: 90770 Da [This is the MW of the unprocessed precursor]

CRC64: A7D81C148CEFD938 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEGPRSDVGR WGRSPWQPTT PSPEPEPEPE PDRSSRSRRG GGRSFWARCC GCCSCGNRAD 

        70         80         90        100        110        120 
DDWGPEPSGS RSRGTSSRGG GSRGGDSRGR DSRGGRRPES RGSGVNAAGD GTIREGMLVV 

       130        140        150        160        170        180 
NGVDLLCSRS DQNRREHHTD EFEYDELILR RGQPFHIILF LNREYESSDR IALELLIGNN 

       190        200        210        220        230        240 
PEVGKGTHVI IPVGKGGSGG WKAQVTKTNG HNLTLRVHTS PNAIIGKFQF TVRTRSEAGE 

       250        260        270        280        290        300 
FQLPFDPRNE IYILFNPWCP EDIVYVDHED WRQEYVLNES GRIYYGTEAQ IGERTWNYGQ 

       310        320        330        340        350        360 
FDHGVLDACL YILDRRGMPY GGRGDPVSVS RVVSAMVNSL DDNGVLIGNW TGDYSRGTNP 

       370        380        390        400        410        420 
SAWVGSVEIL LSYLRTGYSV PYGQCWVFAG VTTTVLRCLG LATRTVTNFN SAHDTDTSLT 

       430        440        450        460        470        480 
MDIYFDENMK PLEHLNHDSV WNFHVWNDCW MKRPDLPSGF DGWQVVDATP QETSSGIFCC 

       490        500        510        520        530        540 
GPCSVESIKN GLVYMKYDTP FIFAEVNSDK VYWQRQDDGS FKIVYVEEKA IGTLIVTKAI 

       550        560        570        580        590        600 
NSNMREDITH IYKHPEGSEA ERKAVEKAAA HGSKPNVYAT RDSAEDVAMQ VEAQDAVMGQ 

       610        620        630        640        650        660 
DLTVSVVLTN RGSSRRTVKL HLYLCVTYYT GVSGPTFKET KKEVVLAPGA SDTVAMPVAY 

       670        680        690        700        710        720 
KEYKPHLVDQ GAMLLNVSGH VKESGQVLAK QHTFRLRTPD LSLTLLGAAV VGQECEVQIV 

       730        740        750        760        770        780 
FKNPLPITLT NVVFRLEGSG LQRPKVLNVG DIGGNETVTL RQTFVPVRPG PRQLIASLDS 

       790        800        810        820 
PQLSQVHGVI QVDVAPSSGG RGFSEAVGDS RSGENIPMAF RGGA

P23606 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