Reviewed, UniProtKB/Swiss-Prot P36269 (GGT5_HUMAN)

Names and origin

Protein names

Recommended name:
    Gamma-glutamyltransferase 5
    EC=2.3.2.2
Alternative name(s):
    Gamma-glutamyltranspeptidase 5
      Short name=GGT 5
    Gamma-glutamyltransferase-like activity 1
    Gamma-glutamyl transpeptidase-related enzyme
      Short name=GGT-rel
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltransferase 5 heavy chain
    2- Recommended name:
            Gamma-glutamyltransferase 5 light chain

Gene names

Name:	GGT5
Synonyms:	GGTLA1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	586 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	Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4).
Catalytic activity	(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid.
Pathway	Sulfur metabolism; glutathione metabolism. Lipid metabolism; leukotriene D4 biosynthesis.
Subunit structure	Heterodimer composed of the light and heavy chains. The active site is located in the light chain By similarity.
Subcellular location	Membrane; Single-pass type II membrane protein By similarity.
Sequence similarities	Belongs to the gamma-glutamyltransferase family.
Sequence caution	The sequence CAB55910.1 differs from that shown. Reason: Frameshift at position 446.

Ontologies

Keywords
Biological process	Glutathione biosynthesis Leukotriene biosynthesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Ref.1 Traceable author statement. Source: ProtInc glutathione biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Ref.1 Traceable author statement. Source: ProtInc plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW gamma-glutamyltransferase activity Ref.1 Inferred from Experiment. Source: Reactome
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P36269-1)

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: P36269-2)

The sequence of this isoform differs from the canonical sequence as follows:
     101-132: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 387	387	Gamma-glutamyltransferase 5 heavy chain By similarity		PRO_0000011072
	Chain	388 – 586	199	Gamma-glutamyltransferase 5 light chain By similarity		PRO_0000011073
Regions
	Topological domain	1 – 8	8	Cytoplasmic Potential
	Transmembrane	9 – 29	21	Signal-anchor for type II membrane protein Potential
	Topological domain	30 – 586	557	Extracellular Potential
Amino acid modifications
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	204	1	N-linked (GlcNAc...) Potential
	Glycosylation	303	1	N-linked (GlcNAc...) Potential
	Glycosylation	347	1	N-linked (GlcNAc...) Potential
	Glycosylation	535	1	N-linked (GlcNAc...) Potential
	Glycosylation	550	1	N-linked (GlcNAc...) Ref.5
Natural variations
	Alternative sequence	101 – 132	32	Missing in isoform 2.		VSP_008146
	Natural variant	11	1	L → I: dbSNP rs5760274.		VAR_028006
	Natural variant	330	1	K → R: dbSNP rs2275984. Ref.1 Ref.3		VAR_028007
	Natural variant	332	1	Q → H: dbSNP rs6004105.		VAR_028008
	Natural variant	475	1	I → V: dbSNP rs7288201.		VAR_024455
Experimental info
	Sequence conflict	408	1	N → Y in CAB55910. Ref.2
	Sequence conflict	437	1	R → W in AAA58503. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: EE37B3CE516F5788	FASTA	586	62,261
	10 20 30 40 50 60 MARGYGATVS LVLLGLGLAL AVIVLAVVLS RHQAPCGPQA FAHAAVAADS KVCSDIGRAI 70 80 90 100 110 120 LQQQGSPVDA TIAALVCTSV VNPQSMGLGG GVIFTIYNVT TGKVEVINAR ETVPASHAPS 130 140 150 160 170 180 LLDQCAQALP LGTGAQWIGV PGELRGYAEA HRRHGRLPWA QLFQPTIALL RGGHVVAPVL 190 200 210 220 230 240 SRFLHNSILR PSLQASTLRQ LFFNGTEPLR PQDPLPWPAL ATTLETVATE GVEVFYTGRL 250 260 270 280 290 300 GQMLVEDIAK EGSQLTLQDL AKFQPEVVDA LEVPLGDYTL YSPPPPAGGA ILSFILNVLR 310 320 330 340 350 360 GFNFSTESMA RPEGRVNVYH HLVETLKFAK GQRWRLGDPR SHPKLQNASR DLLGETLAQL 370 380 390 400 410 420 IRQQIDGRGD HQLSHYSLAE AWGHGTGTSH VSVLGEDGSA VAATSTINTP FGAMVYSPRT 430 440 450 460 470 480 GIILNNELLD LCERCPRGSG TTPSPVSGDR VGGAPGRCWP PVPGERSPSS MVPSILINKA 490 500 510 520 530 540 QGSKLVIGGA GGELIISAVA QAIMSKLWLG FDLRAAIAAP ILHVNSKGCV EYEPNFSQEV 550 560 570 580 QRGLQDRGQN QTQRPFFLNV VQAVSQEGAC VYAVSDLRKS GEAAGY
	Isoform 2. Checksum: 86001882BE5A0D10	FASTA	554	58,992
	10 20 30 40 50 60 MARGYGATVS LVLLGLGLAL AVIVLAVVLS RHQAPCGPQA FAHAAVAADS KVCSDIGRAI 70 80 90 100 110 120 LQQQGSPVDA TIAALVCTSV VNPQSMGLGG GVIFTIYNVT TGAQWIGVPG ELRGYAEAHR 130 140 150 160 170 180 RHGRLPWAQL FQPTIALLRG GHVVAPVLSR FLHNSILRPS LQASTLRQLF FNGTEPLRPQ 190 200 210 220 230 240 DPLPWPALAT TLETVATEGV EVFYTGRLGQ MLVEDIAKEG SQLTLQDLAK FQPEVVDALE 250 260 270 280 290 300 VPLGDYTLYS PPPPAGGAIL SFILNVLRGF NFSTESMARP EGRVNVYHHL VETLKFAKGQ 310 320 330 340 350 360 RWRLGDPRSH PKLQNASRDL LGETLAQLIR QQIDGRGDHQ LSHYSLAEAW GHGTGTSHVS 370 380 390 400 410 420 VLGEDGSAVA ATSTINTPFG AMVYSPRTGI ILNNELLDLC ERCPRGSGTT PSPVSGDRVG 430 440 450 460 470 480 GAPGRCWPPV PGERSPSSMV PSILINKAQG SKLVIGGAGG ELIISAVAQA IMSKLWLGFD 490 500 510 520 530 540 LRAAIAAPIL HVNSKGCVEY EPNFSQEVQR GLQDRGQNQT QRPFFLNVVQ AVSQEGACVY 550 AVSDLRKSGE AAGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from, gamma-glutamyl transpeptidase." Heisterkamp N., Rajpert-De Meyts E., Uribe L., Forman H.J., Groffen J. Proc. Natl. Acad. Sci. U.S.A. 88:6303-6307(1991) [PubMed: 1676842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-330. Tissue: Placenta.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Fetal kidney.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-330.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-550, MASS SPECTROMETRY. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M64099 mRNA. Translation: AAA58503.1. AL117414 mRNA. Translation: CAB55910.1. Frameshift. AP000354 Genomic DNA. No translation available. BC011362 mRNA. Translation: AAH11362.1.
IPI	IPI00002243. IPI00339373.
PIR	A41125. T17220.
RefSeq	NP_001093252.1. NP_004112.2.
UniGene	Hs.437156
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P36269.
Proteomic databases
PRIDE	P36269.
Genome annotation databases
Ensembl	ENST00000263112; ENSP00000263112; ENSG00000099998; Homo sapiens. [Genome view] ENST00000327365; ENSP00000330080; ENSG00000099998; Homo sapiens. [Genome view] ENST00000398292; ENSP00000381340; ENSG00000099998; Homo sapiens. [Genome view] ENST00000418439; ENSP00000392146; ENSG00000099998; Homo sapiens. [Genome view] ENST00000424217; ENSP00000412964; ENSG00000099998; Homo sapiens. [Genome view] ENST00000425408; ENSP00000402917; ENSG00000099998; Homo sapiens. [Genome view] ENST00000438024; ENSP00000389361; ENSG00000099998; Homo sapiens. [Genome view]
GeneID	2687.
UCSC	uc002zzo.2. human. uc002zzr.2. human.
Organism-specific databases
CTD	2687.
GeneCards	GC22M022945.
H-InvDB	HIX0016307.
HGNC	HGNC:4260. GGT5.
HPA	HPA008121.
MIM	137168. gene.
PharmGKB	PA170.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P36269.
Enzyme and pathway databases
BRENDA	2.3.2.2. 247.
Reactome	REACT_15314. Hormone biosynthesis.
Gene expression databases
ArrayExpress	P36269.
Bgee	P36269.
CleanEx	HS_GGT5.
Genevestigator	P36269.
GermOnline	ENSG00000099998. Homo sapiens.
Family and domain databases
InterPro	IPR000101. GGT_peptidase. [Graphical view]
PANTHER	PTHR11686. GGT_peptidase. 1 hit.
Pfam	PF01019. G_glu_transpept. 1 hit. [Graphical view]
PRINTS	PR01210. GGTRANSPTASE.
PROSITE	PS00462. G_GLU_TRANSPEPTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	10606.
SOURCE	Search...

Entry information

Entry name

GGT5_HUMAN

Accession

Primary (citable) accession number: P36269
Secondary accession number(s): Q96FC1, Q9UFM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	October 17, 2006
Last modified:	October 13, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.