Reviewed, UniProtKB/Swiss-Prot Q08188 (TGM3_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein-glutamine gamma-glutamyltransferase E
      Short name=TGase E
      Short name=TGE
      Short name=TG(E)
    EC=2.3.2.13
Alternative name(s):
    Transglutaminase-3
Cleaved into the following 2 chains:
    1- Recommended name:
            Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
    2- Recommended name:
            Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain

Gene names

Name:

TGM3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. It is responsible for the later stages of cell envelope formation in the epidermis and the hair follicle.
Catalytic activity	Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	This enzyme consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide.
Post-translational modification	Activated by proteolytic processing.
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
Biological process	Keratinization
Coding sequence diversity	Polymorphism
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell envelope organization Inferred from direct assay. Source: UniProtKB hair follicle morphogenesis Traceable author statement. Source: UniProtKB keratinization Inferred from electronic annotation. Source: UniProtKB-KW keratinocyte differentiation Inferred from expression pattern. Source: UniProtKB peptide cross-linking Inferred from direct assay. Source: UniProtKB protein tetramerization Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA extrinsic to internal side of plasma membrane Inferred from direct assay. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA
Molecular function	GDP binding Inferred from direct assay. Source: UniProtKB GTP binding Inferred from direct assay. Source: UniProtKB GTPase activity Inferred from direct assay. Source: UniProtKB acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from direct assay. Source: UniProtKB protein-glutamine gamma-glutamyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 470

469

Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain

PRO_0000033652

Chain

471 – 693

223

Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain

PRO_0000033653

Sites

Active site

273

1

By similarity

Active site

331

1

By similarity

Active site

354

1

By similarity

Metal binding

394

1

Calcium By similarity

Metal binding

396

1

Calcium By similarity

Metal binding

444

1

Calcium By similarity

Metal binding

449

1

Calcium By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Natural variations

Natural variant

13

1

K → T: dbSNP rs214803. Ref.4 Ref.6

VAR_040067

Natural variant

163

1

I → L: dbSNP rs6048066.

VAR_040068

Natural variant

249

1

S → N: dbSNP rs214814.

VAR_040069

Natural variant

562

1

K → R: dbSNP rs1042617. Ref.1

VAR_040070

Natural variant

654

1

R → G: dbSNP rs214830. Ref.4 Ref.6

VAR_040071

Natural variant

687

1

L → M: dbSNP rs45581032.

VAR_055360

Experimental info

Sequence conflict

58 – 59

2

VS → DT in AAA61155. Ref.1

Sequence conflict

251

1

N → G in AAA61155. Ref.1

Sequence conflict

324

1

S → G in BAF84040. Ref.2

Sequence conflict

346

1

S → P in AAA61155. Ref.1

Sequence conflict

674

1

D → G in BAF84040. Ref.2

Secondary structure

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693

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

13 – 19

7

Beta strand

31 – 33

3

Beta strand

38 – 46

9

Beta strand

53 – 59

7

Beta strand

61 – 63

3

Turn

66 – 69

4

Beta strand

70 – 79

10

Beta strand

82 – 92

11

Beta strand

95 – 101

7

Beta strand

109 – 119

11

Beta strand

122 – 134

13

Helix

149 – 155

7

Beta strand

160 – 167

8

Beta strand

170 – 177

8

Helix

185 – 193

9

Helix

197 – 201

5

Helix

203 – 208

6

Helix

209 – 211

3

Helix

213 – 223

11

Turn

227 – 229

3

Beta strand

231 – 235

5

Helix

247 – 249

3

Helix

253 – 262

10

Beta strand

268 – 271

4

Helix

273 – 287

15

Beta strand

291 – 300

10

Beta strand

305 – 313

9

Turn

322 – 325

4

Beta strand

326 – 337

12

Turn

341 – 343

3

Beta strand

349 – 353

5

Helix

372 – 377

6

Turn

383 – 385

3

Helix

386 – 394

9

Beta strand

396 – 403

8

Turn

404 – 407

4

Beta strand

408 – 426

19

Beta strand

433 – 435

3

Helix

437 – 440

4

Helix

447 – 460

14

Beta strand

482 – 489

8

Beta strand

499 – 507

9

Beta strand

509 – 511

3

Beta strand

513 – 524

12

Beta strand

530 – 543

14

Beta strand

548 – 555

8

Helix

557 – 560

4

Turn

561 – 563

3

Beta strand

569 – 577

9

Beta strand

584 – 591

8

Beta strand

597 – 603

7

Beta strand

611 – 618

8

Beta strand

621 – 623

3

Beta strand

627 – 633

7

Turn

635 – 637

3

Beta strand

642 – 646

5

Beta strand

654 – 661

8

Beta strand

667 – 677

11

Beta strand

680 – 692

13

Sequences

	Sequence		Length	Mass (Da)
	Q08188-1 [UniParc]. Last modified March 18, 2008. Version 3. Checksum: 8A55559463BE62E2	FASTA	693	76,758
	10 20 30 40 50 60 MAALGVQSIN WQKAFNRQAH HTDKFSSQEL ILRRGQNFQV LMIMNKGLGS NERLEFIVST 70 80 90 100 110 120 GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI SSPASAPIGR YTMALQIFSQ 130 140 150 160 170 180 GGISSVKLGT FILLFNPWLN VDSVFMGNHA EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ 190 200 210 220 230 240 FEEDILSICL SILDRSLNFR RDAATDVASR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT 250 260 270 280 290 300 YTGGRDPRSW NGSVEILKNW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA 310 320 330 340 350 360 HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW QVLDATPQER 370 380 390 400 410 420 SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW LYDNTTGKQW KNSVNSHTIG 430 440 450 460 470 480 RYISTKAVGS NARMDVTDKY KYPEGSDQER QVFQKALGKL KPNTPFAATS SMGLETEEQE 490 500 510 520 530 540 PSIIGKLKVA GMLAVGKEVN LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT 550 560 570 580 590 600 MSLDPEEEAE HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDI ILDNPTLTLE 610 620 630 640 650 660 VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG PKERSRVRFD 670 680 690 ILPSRSGTKQ LLADFSCNKF PAIKAMLSID VAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse." Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M. J. Biol. Chem. 268:12682-12690(1993) [PubMed: 8099584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-562. Tissue: Foreskin.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[3]	NIEHS SNPs program Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-13; LEU-163; ASN-249; GLY-654 AND MET-687.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS THR-13 AND GLY-654.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-13 AND GLY-654.
[7]	Bienvenut W.V., Bensaad K., Vousden K.H. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13 AND 670-684, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Osteosarcoma.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

L10386 mRNA. Translation: AAA61155.1.
AK290324 mRNA. Translation: BAF83013.1.
AK291351 mRNA. Translation: BAF84040.1.
AK315236 mRNA. Translation: BAG37663.1.
EF102483 Genomic DNA. Translation: ABK41960.1.
AL031678 Genomic DNA. Translation: CAB37633.1.
CH471133 Genomic DNA. Translation: EAX10601.1.
BC109075 mRNA. Translation: AAI09076.1.
BC109076 mRNA. Translation: AAI09077.1.

IPI

IPI00300376.

PIR

A45991.

RefSeq

NP_003236.3.

UniGene

Hs.2022

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L9M	X-ray	2.10	A/B	2-693	[»]
1L9N	X-ray	2.10	A/B	2-693	[»]
1NUD	X-ray	2.70	A/B	2-693	[»]
1NUF	X-ray	2.70	A	2-693	[»]
1NUG	X-ray	2.40	A/B	2-693	[»]
1RLE	X-ray	2.10	A/B	2-693	[»]
1SGX	X-ray	2.00	A/B	2-693	[»]
1VJJ	X-ray	1.90	A/B	2-693	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08188. 1 interaction.

Proteomic databases

PeptideAtlas

Q08188.

PRIDE

Q08188.

Genome annotation databases

Ensembl

ENSG00000125780. Homo sapiens. [Contig view]

GeneID

7053.

KEGG

hsa:7053.

Organism-specific databases

GeneCards

GC20P002224.

H-InvDB

HIX0040608.

HGNC

HGNC:11779. TGM3.

HPA

HPA004728.

MIM

600238. gene.

PharmGKB

PA36492.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q08188.

HOVERGEN

Q08188.

Enzyme and pathway databases

BRENDA

2.3.2.13. 247.

Gene expression databases

ArrayExpress

Q08188.

Bgee

Q08188.

CleanEx

HS_TGM3.

GermOnline

ENSG00000125780. Homo sapiens.

Family and domain databases

InterPro

IPR013783. Ig-like_fold.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 3 hits.

Pfam

PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]

SMART

SM00460. TGc. 1 hit.
[Graphical view]

PROSITE

PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00130. L-Glutamine.

SOURCE

Search...

Entry information

Entry name

TGM3_HUMAN

Accession

Primary (citable) accession number: Q08188
Secondary accession number(s): A8K5N6 , B2RCR6, O95933, Q32ML9, Q32MM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	March 18, 2008
Last modified:	June 16, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)