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 + NH(3).
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

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

Natural variations

Natural variant

13

1

K → T: dbSNP rs214803.

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.

VAR_040070

Natural variant

654

1

R → G: dbSNP rs214830.

VAR_040071

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