GGTL2_HUMAN
ID GGTL2_HUMAN Reviewed; 218 AA.
AC Q14390; A1A516; A2VCM9; Q5NV76; Q6ISH0;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Glutathione hydrolase light chain 2;
DE AltName: Full=Gamma-glutamyltransferase light chain 2;
DE AltName: Full=Gamma-glutamyltransferase-like protein 4;
GN Name=GGTLC2; Synonyms=GGTL4;
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 [MRNA], AND VARIANT GLY-70.
RC TISSUE=Placenta;
RX PubMed=8830654; DOI=10.1016/0014-5793(96)00965-9;
RA Leh L., Courtey C., Gerardin P., Wellman M., Siest G., Visvikis A.;
RT "Cloning and expression of a novel type (III) of human gamma-
RT glutamyltransferase truncated mRNA.";
RL FEBS Lett. 394:258-262(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9074928; DOI=10.1101/gr.7.3.250;
RA Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A.,
RA Schmeits J.L., Wang J., Shimizu N.;
RT "One-megabase sequence analysis of the human immunoglobulin lambda gene
RT locus.";
RL Genome Res. 7:250-261(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-70.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-212.
RX PubMed=17207965; DOI=10.1016/j.ygeno.2006.11.012;
RA Lamesch P., Li N., Milstein S., Fan C., Hao T., Szabo G., Hu Z.,
RA Venkatesan K., Bethel G., Martin P., Rogers J., Lawlor S., McLaren S.,
RA Dricot A., Borick H., Cusick M.E., Vandenhaute J., Dunham I., Hill D.E.,
RA Vidal M.;
RT "hORFeome v3.1: a resource of human open reading frames representing over
RT 10,000 human genes.";
RL Genomics 89:307-315(2007).
RN [6]
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 -!- INTERACTION:
CC Q14390; O43711: TLX3; NbExp=3; IntAct=EBI-12903880, EBI-3939165;
CC -!- TISSUE SPECIFICITY: Placenta and sigmoid tissues.
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 -!- SEQUENCE CAUTION:
CC Sequence=BAA20001.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA67421.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA67421.1; Type=Miscellaneous discrepancy; Note=Contains an unspliced intron inserted in position 120.; Evidence={ECO:0000305};
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DR EMBL; X98922; CAA67421.1; ALT_SEQ; mRNA.
DR EMBL; D87002; BAA20001.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069534; AAH69534.1; -; mRNA.
DR EMBL; EL736203; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13802.2; -.
DR PIR; S74240; S74240.
DR RefSeq; NP_001269808.1; NM_001282879.1.
DR RefSeq; NP_954578.2; NM_199127.2.
DR AlphaFoldDB; Q14390; -.
DR SMR; Q14390; -.
DR BioGRID; 124807; 1.
DR IntAct; Q14390; 1.
DR STRING; 9606.ENSP00000419751; -.
DR MEROPS; T03.006; -.
DR MEROPS; T03.016; -.
DR GlyConnect; 1260; 8 N-Linked glycans (1 site).
DR GlyGen; Q14390; 2 sites, 8 N-linked glycans (1 site).
DR iPTMnet; Q14390; -.
DR PhosphoSitePlus; Q14390; -.
DR BioMuta; GGTLC2; -.
DR DMDM; 294862536; -.
DR jPOST; Q14390; -.
DR MassIVE; Q14390; -.
DR MaxQB; Q14390; -.
DR PaxDb; Q14390; -.
DR PeptideAtlas; Q14390; -.
DR PRIDE; Q14390; -.
DR Antibodypedia; 54292; 88 antibodies from 13 providers.
DR DNASU; 91227; -.
DR Ensembl; ENST00000448514.3; ENSP00000415676.2; ENSG00000100121.14.
DR Ensembl; ENST00000480559.6; ENSP00000419751.1; ENSG00000100121.14.
DR GeneID; 91227; -.
DR KEGG; hsa:91227; -.
DR MANE-Select; ENST00000448514.3; ENSP00000415676.2; NM_199127.3; NP_954578.2.
DR UCSC; uc010gtt.3; human.
DR CTD; 91227; -.
DR GeneCards; GGTLC2; -.
DR HGNC; HGNC:18596; GGTLC2.
DR HPA; ENSG00000100121; Tissue enriched (testis).
DR MIM; 612339; gene.
DR neXtProt; NX_Q14390; -.
DR OpenTargets; ENSG00000100121; -.
DR PharmGKB; PA162389523; -.
DR VEuPathDB; HostDB:ENSG00000100121; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000154601; -.
DR InParanoid; Q14390; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; Q14390; -.
DR PathwayCommons; Q14390; -.
DR SignaLink; Q14390; -.
DR BioGRID-ORCS; 91227; 675 hits in 991 CRISPR screens.
DR GenomeRNAi; 91227; -.
DR Pharos; Q14390; Tbio.
DR PRO; PR:Q14390; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q14390; protein.
DR Bgee; ENSG00000100121; Expressed in right testis and 94 other tissues.
DR ExpressionAtlas; Q14390; baseline and differential.
DR Genevisible; Q14390; 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 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..218
FT /note="Glutathione hydrolase light chain 2"
FT /id="PRO_0000205982"
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 VARIANT 70
FT /note="E -> G (in dbSNP:rs2904923)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8830654"
FT /id="VAR_035113"
FT VARIANT 75
FT /note="D -> N (in dbSNP:rs2330126)"
FT /id="VAR_055836"
FT CONFLICT 8
FT /note="A -> R (in Ref. 1; CAA67421)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="E -> V (in Ref. 1; CAA67421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23661 MW; 66AD78A639C74E36 CRC64;
MTSEFFAAQL RAQISDDTTH PISYYKPEFY TPVDGGTAHL SVVAEDGSAV SATSTINLYF
GSKVRSPVSE ILFNDEMDDF SSPNITNEFG VPPSPANFIQ PGKQPLSSMC PTIMVGQDGQ
PPSHADHTPM PQAIIYNLWF GYDVKRAVEE PRLHNQLLPN VTTVERNIDQ AVTAALETRH
HHTQIASTFI AVVQAIVRTA GGWAAASDSR KGGEPAGY
