Q923B0 (GGACT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-glutamylaminecyclotransferase
Short name=GGACT
EC=2.3.2.4

Alternative name(s):
AIG2-like domain-containing protein 1
Gamma-glutamylamine cyclotransferase

Gene names

Name:	Ggact
Synonyms:	A2ld1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Contributes to degradation of proteins cross-linked by transglutaminases. Degrades the cross-link between a lysine and a glutamic acid residue from two proteins that have been cross-linked by transglutaminases. Catalyzes the formation of 5-oxoproline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine By similarity.
Catalytic activity	(Gamma-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid.
Subunit structure	Monomer Probable. Ref.3
Sequence similarities	Belongs to the gamma-glutamylcyclotransferase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular modified amino acid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	gamma-glutamylcyclotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q923B0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q923B0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     66-79: EIYEVDEQMLRFLD → NWKGGHICHCRWIH
     80-149: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 149

149

Gamma-glutamylaminecyclotransferase

PRO_0000320204

Regions

Region

7 – 10

4

Substrate binding By similarity

Sites

Active site

82

1

Proton acceptor By similarity

Natural variations

Alternative sequence

66 – 79

14

EIYEV…LRFLD → NWKGGHICHCRWIH in isoform 2.

VSP_031641

Alternative sequence

80 – 149

70

Missing in isoform 2.

VSP_031642

Secondary structure

1

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149

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Beta strand

11 – 13

3

Turn

15 – 17

3

Helix

18 – 21

4

Helix

23 – 25

3

Beta strand

28 – 38

11

Beta strand

42 – 45

4

Turn

46 – 49

4

Beta strand

50 – 55

6

Beta strand

59 – 61

3

Beta strand

64 – 70

7

Helix

72 – 81

10

Turn

82 – 86

5

Beta strand

89 – 100

12

Beta strand

108 – 118

11

Helix

122 – 126

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0FB86B86AF2AB46B	FASTA	149	17,080
	10 20 30 40 50 60 MAHIFVYGTL KRGQPNHKVM LDHSHGLAAF RGRGCTVESF PLVIAGEHNI PWLLYLPGKG 70 80 90 100 110 120 HCVTGEIYEV DEQMLRFLDD FEDCPSMYQR TALQVQVLEW EGDGDPGDSV QCFVYTTATY 130 140 APEWLFLPYH ESYDSEGPHG LRYNPRENR
	Isoform 2 [UniParc]. Checksum: 1F4CCF7BBE385459	FASTA	79	8,866
	10 20 30 40 50 60 MAHIFVYGTL KRGQPNHKVM LDHSHGLAAF RGRGCTVESF PLVIAGEHNI PWLLYLPGKG 70 HCVTGNWKGG HICHCRWIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Liver.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: Czech II. Tissue: Mammary tumor.
[3]	"Crystal structure of a conserved hypothetical protein (gi: 13879369) from mouse at 1.90 A resolution reveals a new fold." Klock H.E., Schwarzenbacher R., Xu Q., McMullan D., Abdubek P., Ambing E., Axelrod H., Biorac T., Canaves J.M., Chiu H.-J., Deacon A.M., DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., Hale J., Hampton E. , Han G.W., Haugen J., Hornsby M., Jaroszewski L., Koesema E., Kreusch A., Kuhn P., Miller M.D., Moy K., Nigoghossian E., Paulsen J., Quijano K., Reyes R., Rife C., Sims E., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., White A., Wolf G., Hodgson K.O., Wooley J., Lesley S.A., Wilson I.A. Proteins 61:1132-1136(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
[4]	"Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites." Serrano P., Pedrini B., Geralt M., Jaudzems K., Mohanty B., Horst R., Herrmann T., Elsliger M.A., Wilson I.A., Wuthrich K. Acta Crystallogr. F 66:1393-1405(2010) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK050251 mRNA. Translation: BAC34147.1.
BC006662 mRNA. Translation: AAH06662.1.
BC080839 mRNA. Translation: AAH80839.1.

IPI

IPI00124027.
IPI00471432.

RefSeq

NP_663441.1. NM_145466.2.

UniGene

Mm.379358.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VKB	X-ray	1.90	A	1-149	[»]
2KL2	NMR	-	A	1-149	[»]

ProteinModelPortal

Q923B0.

SMR

Q923B0. Positions 1-149.

ModBase

Search...

Proteomic databases

PaxDb

Q923B0.

PRIDE

Q923B0.

Protocols and materials databases

DNASU

223267.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000038075; ENSMUSP00000037278; ENSMUSG00000041625.
ENSMUST00000110679; ENSMUSP00000135487; ENSMUSG00000041625.

GeneID

223267.

KEGG

mmu:223267.

UCSC

uc011zqm.1. mouse.

Organism-specific databases

CTD

87769.

MGI

MGI:2385008. Ggact.

Phylogenomic databases

eggNOG

NOG242813.

GeneTree

ENSGT00390000010543.

HOGENOM

HOG000261862.

HOVERGEN

HBG105481.

InParanoid

Q923B0.

OMA

CFVYSTA.

OrthoDB

EOG47WNQ1.

Gene expression databases

ArrayExpress

Q923B0.

Bgee

Q923B0.

Genevestigator

Q923B0.

Family and domain databases

Gene3D

3.10.490.10. 1 hit.

InterPro

IPR009288. AIG2-like.
IPR013024. Butirosin_synth_BtrG-like.
[Graphical view]

Pfam

PF06094. AIG2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q923B0.

NextBio

376683.

SOURCE

Search...

Entry information

Entry name

GGACT_MOUSE

Accession

Primary (citable) accession number: Q923B0
Secondary accession number(s): Q66JP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program