[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=11474183 [NCBI, ExPASy, EBI, Israel, Japan] Credille K.M., Venta P.J., Breen M., Lowe J.K., Murphy K.E., Ostrander E.A., Galibert F., Dunstan R.W.; "DNA sequence and physical mapping of the canine transglutaminase 1 gene."; Cytogenet. Cell Genet. 93:73-76(2001).

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 (By similarity).
CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N⁵-alkylglutamine + NH₃.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By similarity).
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

AF262219; AAG13662.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001003079.1; -.

UniGene

Cfa.3494

3D structure databases

HSSP

P00488; 1EX0. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q9GLK0.

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

Q9GLK0.

Genome annotation databases

Ensembl

ENSCAFG00000012182; Canis familiaris. [Contig view]

GeneID

403630; -.

KEGG

cfa:403630; -.

Phylogenomic databases

HOVERGEN

Q9GLK0; -.

Other

ProtoNet

Q9GLK0.

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`	`1 815`	`815`	`Protein-glutamine gamma-glutamyltransferase K.`	`PRO_0000213700`
`ACT_SITE`	`375 375`		`By similarity.`
`ACT_SITE`	`434 434`		`By similarity.`
`ACT_SITE`	`457 457`		`By similarity.`
`METAL`	`497 497`		`Calcium (By similarity).`
`METAL`	`499 499`		`Calcium (By similarity).`
`METAL`	`546 546`		`Calcium (By similarity).`
`METAL`	`551 551`		`Calcium (By similarity).`
`MOD_RES`	`90 90`		`Phosphoserine (By similarity).`
`MOD_RES`	`93 93`		`Phosphoserine (By similarity).`

Sequence information

Length: 815 AA [This is the length of the unprocessed precursor]

Molecular weight: 89757 Da [This is the MW of the unprocessed precursor]

CRC64: 82C49D15DDD25BE4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDGPRSDVGR WGGNPWQPPT TPSPEPEPEP EPERRSRRGG RSFWARCCGC CSCRNRADDD 

        70         80         90        100        110        120 
WGPEPHRDRG SGSGRRRPDS RGSDSRRPGS RASGVNAAGD GTIREGMLVV TGVDLLSSRS 

       130        140        150        160        170        180 
DQNRREHHTD EFEYDELIIR RGQPFHMVLH FSRPYESSDR VALELLIGNN PEVGKGTHVI 

       190        200        210        220        230        240 
IPVGKGGSGG WKAQVTKASG QNLNLRVHTS PNAIIGKFQF TVRTHSEAGE FQLPFDPHNE 

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

       310        320        330        340        350        360 
YILDRRGMPY GGRGDPVSVS RVISAMVNSL DDNGVLIGNW SGDYSRGTNP SAWVGSVEIL 

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

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

       490        500        510        520        530        540 
GLVYMKYDTP FIFAEVNSDK VYWQRQDDGS FKIVYVEEKA IGTLIVTKAV GSNMQDDVTH 

       550        560        570        580        590        600 
IYKHPEGSEA ERKAVETAAA HGSKPNVYTN RDSAEDVALQ VEAQDAVMGQ DLTVSVVLTN 

       610        620        630        640        650        660 
RGSSTRTVKL HLYLSVTFYT GVTGPVFKES KKEVVLAPGA TERVSMPVAY KEYRPQIVDQ 

       670        680        690        700        710        720 
GSMLLNVSGH VKENGQVLAK QHTFRLRTPD LSLTLLGAAV VGQECEVQIV FKNPLPVTLT 

       730        740        750        760        770        780 
NVVFRLEGSG LQRPKILNVG DIGGNETVTL HQKFVPVRPG PRQLIASLDS PQLSQVHGVI 

       790        800        810 
QVDVAPAPGG GGFFSNAGGN SPLGETIPMA SRGGA

Q9GLK0 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