Q9BVM4 (GGACT_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	153 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. Ref.5
Catalytic activity	(Gamma-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid. Ref.5
Subunit structure	Monomer. Ref.5
Sequence similarities	Belongs to the gamma-glutamylcyclotransferase family.
Sequence caution	The sequence AAH04360.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
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 direct assay Ref.5. Source: UniProtKB
Molecular_function	gamma-glutamylcyclotransferase activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 153

153

Gamma-glutamylaminecyclotransferase

PRO_0000320203

Regions

Region

7 – 10

4

Substrate binding

Sites

Active site

82

1

Proton acceptor Ref.5

Experimental info

Mutagenesis

82

1

E → A or Q: Loss of activity. Ref.5

Secondary structure

1

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153

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

17 – 20

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 – 98

10

Beta strand

113 – 121

9

Helix

126 – 130

5

Sequences

	Sequence		Length	Mass (Da)
	Q9BVM4 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 1A01F350F761D208	FASTA	153	17,329
	10 20 30 40 50 60 MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG 70 80 90 100 110 120 RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS 130 140 150 RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Lung.
[5]	"Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism." Oakley A.J., Coggan M., Board P.G. J. Biol. Chem. 285:9642-9648(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) IN COMPLEX WITH 5-OXOPROLINE AND NITRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF GLU-82.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK095850 mRNA. Translation: BAG53143.1.
AL136526 Genomic DNA. Translation: CAI39558.1.
CH471085 Genomic DNA. Translation: EAX09037.1.
BC001077 mRNA. Translation: AAH01077.2.
BC004360 mRNA. Translation: AAH04360.1. Different initiation.

IPI

IPI00900332.

RefSeq

NP_001182016.1. NM_001195087.1.
NP_149101.1. NM_033110.2.

UniGene

Hs.350868.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JUB	X-ray	1.20	A	1-153	[»]
3JUC	X-ray	1.20	A	1-153	[»]
3JUD	X-ray	0.98	A	1-153	[»]

ProteinModelPortal

Q9BVM4.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000365426.

Polymorphism databases

DMDM

74752384.

Proteomic databases

PaxDb

Q9BVM4.

PRIDE

Q9BVM4.

Protocols and materials databases

DNASU

87769.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376250; ENSP00000365426; ENSG00000134864.
ENST00000455100; ENSP00000410449; ENSG00000134864.

GeneID

87769.

KEGG

hsa:87769.

UCSC

uc001voq.2. human.

Organism-specific databases

CTD

87769.

GeneCards

GC13M101183.

HGNC

HGNC:25100. GGACT.

MIM

613378. gene.

neXtProt

NX_Q9BVM4.

PharmGKB

PA164714645.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG242813.

HOGENOM

HOG000261862.

HOVERGEN

HBG105481.

InParanoid

Q9BVM4.

OMA

CFVYSTA.

OrthoDB

EOG47WNQ1.

PhylomeDB

Q9BVM4.

Gene expression databases

Bgee

Q9BVM4.

CleanEx

HS_A2LD1.

Genevestigator

Q9BVM4.

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

Q9BVM4.

GenomeRNAi

87769.

NextBio

76214.

SOURCE

Search...

Entry information

Entry name

GGACT_HUMAN

Accession

Primary (citable) accession number: Q9BVM4
Secondary accession number(s): B3KTN1, Q9BT41

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	March 1, 2004
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.