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   03-AUG-2022, entry version 81.
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   STRING; 9606.ENSP00000477856; -.
DR   BioMuta; GGTLC3; -.
DR   jPOST; B5MD39; -.
DR   MassIVE; B5MD39; -.
DR   MaxQB; B5MD39; -.
DR   PaxDb; B5MD39; -.
DR   PeptideAtlas; B5MD39; -.
DR   PRIDE; B5MD39; -.
DR   Antibodypedia; 75521; 6 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   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; GAPPYFG; -.
DR   PhylomeDB; B5MD39; -.
DR   Pharos; B5MD39; Tdark.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; B5MD39; protein.
DR   Bgee; ENSG00000274252; Expressed in right lobe of thyroid gland and 70 other 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   SUPFAM; SSF56235; SSF56235; 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