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P36269 (GGT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-glutamyltransferase 5

Short name=GGT 5
EC=2.3.2.2
Alternative name(s):
Gamma-glutamyl transpeptidase-related enzyme
Short name=GGT-rel
Gamma-glutamyltransferase-like activity 1
Gamma-glutamyltranspeptidase 5
Glutathione hydrolase 5
EC=3.4.19.13
Leukotriene-C4 hydrolase
EC=3.4.19.14
Gene names
Name:GGT5
Synonyms:GGTLA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.

Glutathione + H2O = L-cysteinylglycine + L-glutamate.

Leukotriene C4 + H2O = leukotriene D4 + L-glutamate.

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.

Post-translational modification

Cleaved by autocatalysis into a large and a small subunit 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.

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: P36269-3)

The sequence of this isoform differs from the canonical sequence as follows:
     445-445: P → PA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Gamma-glutamyltransferase 5 heavy chain By similarity
PRO_0000011072
Chain388 – 586199Gamma-glutamyltransferase 5 light chain By similarity
PRO_0000011073

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 586557Extracellular Potential
Region469 – 4702Glutamate binding By similarity

Sites

Active site3881Nucleophile By similarity
Binding site1101Glutamate By similarity
Binding site4061Glutamate By similarity
Binding site4271Glutamate By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation5351N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Ref.9

Natural variations

Alternative sequence101 – 13232Missing in isoform 2.
VSP_008146
Alternative sequence4451P → PA in isoform 3.
VSP_043470
Natural variant111L → I.
Corresponds to variant rs5760274 [ dbSNP | Ensembl ].
VAR_028006
Natural variant3301K → R. Ref.1 Ref.6
Corresponds to variant rs2275984 [ dbSNP | Ensembl ].
VAR_028007
Natural variant3321Q → H.
Corresponds to variant rs6004105 [ dbSNP | Ensembl ].
VAR_028008
Natural variant4751I → V.
Corresponds to variant rs7288201 [ dbSNP | Ensembl ].
VAR_024455

Experimental info

Sequence conflict4081N → Y in CAB55910. Ref.5
Sequence conflict4371R → W in AAA58503. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: EE37B3CE516F5788

FASTA58662,261
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 86001882BE5A0D10
Show »

FASTA55458,992
Isoform 3 [UniParc].

Checksum: C7F2285F9FFF1A22
Show »

FASTA58762,332

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-330.
Tissue: Placenta.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Small intestine.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal kidney.
[6]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-330.
[7]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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].
[8]"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 3).
Tissue: Brain and PNS.
[9]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-550.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64099 mRNA. Translation: AAA58503.1.
AL117414 mRNA. Translation: CAB55910.1. Frameshift.
BT009808 mRNA. Translation: AAP88810.1.
CT841518 mRNA. Translation: CAJ86448.1.
AK292006 mRNA. Translation: BAF84695.1.
AP000353 Genomic DNA. No translation available.
AP000354 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59643.1.
BC011362 mRNA. Translation: AAH11362.1.
BC073999 mRNA. Translation: AAH73999.1.
PIRA41125.
T17220.
RefSeqNP_001093251.1. NM_001099781.1.
NP_001093252.1. NM_001099782.1.
NP_004112.2. NM_004121.2.
UniGeneHs.437156.

3D structure databases

ProteinModelPortalP36269.
SMRP36269. Positions 38-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000381340.

Protein family/group databases

MEROPST03.002.

PTM databases

PhosphoSiteP36269.

Polymorphism databases

DMDM116242493.

Proteomic databases

PaxDbP36269.
PRIDEP36269.

Protocols and materials databases

DNASU2687.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263112; ENSP00000263112; ENSG00000099998. [P36269-2]
ENST00000327365; ENSP00000330080; ENSG00000099998. [P36269-1]
ENST00000398292; ENSP00000381340; ENSG00000099998. [P36269-3]
GeneID2687.
KEGGhsa:2687.
UCSCuc002zzo.4. human. [P36269-1]
uc002zzp.4. human. [P36269-3]
uc002zzq.4. human. [P36269-2]

Organism-specific databases

CTD2687.
GeneCardsGC22M024615.
H-InvDBHIX0138942.
HGNCHGNC:4260. GGT5.
HPACAB032489.
HPA008121.
MIM137168. gene.
neXtProtNX_P36269.
PharmGKBPA162389442.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0405.
HOGENOMHOG000175620.
HOVERGENHBG005835.
KOK00681.
OMAATHQPRI.
OrthoDBEOG7V7665.
PhylomeDBP36269.
TreeFamTF313608.

Enzyme and pathway databases

BioCycMetaCyc:HS01949-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00204.
UPA00880.

Gene expression databases

ArrayExpressP36269.
BgeeP36269.
CleanExHS_GGT5.
GenevestigatorP36269.

Family and domain databases

InterProIPR000101. GGT_peptidase.
[Graphical view]
PANTHERPTHR11686. PTHR11686. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGGTLA1.
GenomeRNAi2687.
NextBio10606.
PROP36269.
SOURCESearch...

Entry information

Entry nameGGT5_HUMAN
AccessionPrimary (citable) accession number: P36269
Secondary accession number(s): Q53XM9 expand/collapse secondary AC list , Q6GMP0, Q96FC1, Q9UFM5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 17, 2006
Last modified: March 19, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM