ID GGTL3_HUMAN Reviewed; 225 AA.
AC B5MD39; A6NEA2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Putative glutathione hydrolase light chain 3;
DE AltName: Full=Putative gamma-glutamyltransferase light chain 3;
GN Name=GGTLC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP NOMENCLATURE.
RX PubMed=18357469; DOI=10.1007/s00439-008-0487-7;
RA Heisterkamp N., Groffen J., Warburton D., Sneddon T.P.;
RT "The human gamma-glutamyltransferase gene family.";
RL Hum. Genet. 123:321-332(2008).
CC -!- MISCELLANEOUS: Corresponds to the light chain of other gamma-
CC glutamyltransferase family members. Has no catalytic activity.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AC023490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS86996.1; -.
DR AlphaFoldDB; B5MD39; -.
DR SMR; B5MD39; -.
DR IntAct; B5MD39; 1.
DR STRING; 9606.ENSP00000477856; -.
DR BioMuta; GGTLC3; -.
DR jPOST; B5MD39; -.
DR MassIVE; B5MD39; -.
DR MaxQB; B5MD39; -.
DR PaxDb; 9606-ENSP00000477856; -.
DR PeptideAtlas; B5MD39; -.
DR Antibodypedia; 75521; 5 antibodies from 4 providers.
DR Ensembl; ENST00000619998.1; ENSP00000477856.1; ENSG00000274252.1.
DR MANE-Select; ENST00000619998.1; ENSP00000477856.1; NM_001355479.1; NP_001342408.1.
DR UCSC; uc062biv.1; human.
DR AGR; HGNC:33426; -.
DR GeneCards; GGTLC3; -.
DR HGNC; HGNC:33426; GGTLC3.
DR HPA; ENSG00000274252; Group enriched (kidney, thyroid gland).
DR MIM; 612340; gene.
DR neXtProt; NX_B5MD39; -.
DR VEuPathDB; HostDB:ENSG00000274252; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000154601; -.
DR HOGENOM; CLU_014813_1_3_1; -.
DR InParanoid; B5MD39; -.
DR OMA; ALMFHRI; -.
DR PhylomeDB; B5MD39; -.
DR Pharos; B5MD39; Tdark.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; B5MD39; Protein.
DR Bgee; ENSG00000274252; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 72 other cell types or tissues.
DR Genevisible; B5MD39; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:InterPro.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR GO; GO:1901750; P:leukotriene D4 biosynthetic process; ISS:UniProtKB.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR45027:SF5; GLUTATHIONE HYDROLASE LIGHT CHAIN 2-RELATED; 1.
DR PANTHER; PTHR45027; PUTATIVE GLUTATHIONE HYDROLASE LIGHT CHAIN; 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 5: Uncertain;
KW Reference proteome.
FT CHAIN 1..225
FT /note="Putative glutathione hydrolase light chain 3"
FT /id="PRO_0000355316"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 107..108
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 129..130
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
SQ SEQUENCE 225 AA; 24102 MW; 71B6ABC18A2A7F9D CRC64;
MTSEFFAAQL RSQISDHTTH PISYYKPEFY TPDDGGTAHL SVVAEDGSAV SATSTINLYF
GSKVCSPVSG ILFNNEWTTS ALPAFTNEFG APPSPANFIQ PGKQPLLSMC PTIMVGQDGQ
VRMVVGAAGG TQITTDTALA IIYNLWFGYD VKRAVEEPRL HNKLLPNVTT VERNIDQAVT
AALETRHHHT QIASTFIAVV QAIVRTAGGW AAASDSRKGG EPAGY
//
