[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=New Zealand white; TISSUE=Tracheobronchial epithelium; DOI=10.1210/me.7.3.387; PubMed=8097865 [NCBI, ExPASy, EBI, Israel, Japan] Saunders N.A., Bernacki S.H., Vollberg T.M., Jetten A.M.; "Regulation of transglutaminase type I expression in squamous differentiating rabbit tracheal epithelial cells and human epidermal keratinocytes: effects of retinoic acid and phorbol esters."; Mol. Endocrinol. 7:387-398(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 368-749. PubMed=2574824 [NCBI, ExPASy, EBI, Israel, Japan] Floyd E.E., Jetten A.M.; "Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids."; Mol. Cell. Biol. 9:4846-4851(1989).
[3]	SEQUENCE REVISION. PubMed=1670769 [NCBI, ExPASy, EBI, Israel, Japan] Kim H.C., Idler W.W., Kim I.-G., Han J.H., Chung S.-I., Steinert P.M.; "The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones."; J. Biol. Chem. 266:536-539(1991).

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).
ENZYME REGULATION: Inhibited by retinoic acid, but phorbol ester treatment activates it.
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

L10714; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]
M30468; AAA31475.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A33477; A33477.
A54269; A54269.

UniGene

Ocu.1972

3D structure databases

HSSP

P21980; 1KV3. [HSSP ENTRY / PDB]

ModBase

P22758.

Ontologies

GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008415;	Molecular function: acyltransferase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003810;	Molecular function: protein-glutamine gamma-glutamyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031424;	Biological process: keratinization (inferred from electronic annotation from UniProtKB-KW).
GO:0018149;	Biological process: peptide cross-linking (inferred from electronic annotation from InterPro).
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.

ProtoNet

P22758.

Phylogenomic databases

HOVERGEN

P22758; -.

Other

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`	`1 836`	`836`	`Protein-glutamine gamma-glutamyltransferase K.`	`PRO_0000213703`
`ACT_SITE`	`397 397`		`By similarity.`
`ACT_SITE`	`456 456`		`By similarity.`
`ACT_SITE`	`479 479`		`By similarity.`
`METAL`	`519 519`		`Calcium (By similarity).`
`METAL`	`521 521`		`Calcium (By similarity).`
`METAL`	`568 568`		`Calcium (By similarity).`
`METAL`	`573 573`		`Calcium (By similarity).`
`MOD_RES`	`98 98`		`Phosphoserine (By similarity).`
`MOD_RES`	`112 112`		`Phosphoserine (By similarity).`

Sequence information

Length: 836 AA [This is the length of the unprocessed precursor]

Molecular weight: 91935 Da [This is the MW of the unprocessed precursor]

CRC64: B3D281F7BECB9C00 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDGPRSDMGR SDVSRSDMSR SDMGRSDMGR SDVGRCGGGP LQPSATPSPE PEPEPEPEPD 

        70         80         90        100        110        120 
RGSRSRGGRG RSFWARCCGC CSCRNAADDD WGREPSDSRD RGSSSRGGRP DSRGGGVNAA 

       130        140        150        160        170        180 
GDGTIREGML VVTGVDLLSS RSDQNRREHH TDEFEYEELI VRRGQPFHLV LFLSRPYESS 

       190        200        210        220        230        240 
DRIALELQIG NNPEVGKGTH VIIPVGKGNS GGWKAQVTKA SGQTLNLRVH SPASAIIGKF 

       250        260        270        280        290        300 
QFTVRTRTEA GEFQLPFDPR NEIYILFNPW CPEDIVYVDH EDWRQDYVLN ESGRIYYGTE 

       310        320        330        340        350        360 
AQIGERTWNY GQFDHGVLDA CLYILDRRGM PYGGRGDPVS VSRVISAMVN SLDDNGVLIG 

       370        380        390        400        410        420 
NWSGDYSRGT NPSAWVGSVE ILLSYLRTGY SVPYGQCWVF AGVTTTVLRC LGLATRTVTN 

       430        440        450        460        470        480 
FNSAHDTDTS LTMDIYFDEN MKPLEHLNRD SVWNFHVWND CWMKRPDLPS GFDGWQVVDA 

       490        500        510        520        530        540 
TPQETSSGIF CCGPCSVESV KNGLVYMKYD TPFIFAEVNS DKVYWQRQDD GSFKIVYVEE 

       550        560        570        580        590        600 
KAIGTLIVTK AVRSHMREDI THIYKHPEGS DAERKAVETA AAHGSKPNVY DSRDSAEDVA 

       610        620        630        640        650        660 
MQVEAQDAVM GQDLTVSVVL TNRSSSRRTV KLHLYLSVTF YTGVTGSIFK ESKKEVVLAA 

       670        680        690        700        710        720 
GSSDSVVMPV AYKEYRPHLV DQGAMLLNVS GHVKESGQVL AKQHTFRVRT PDLSLTLLGA 

       730        740        750        760        770        780 
AVVGQECEVQ IVFRNPLPIT LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQTFVPVR 

       790        800        810        820        830 
PGPRQLIASL DSPQLSQVHG VIQVDVAPAS GGRGFLHAGG DSYSGETIPM TSRGEA

P22758 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