ID   GGT7_HUMAN              Reviewed;         662 AA.
AC   Q9UJ14; Q8N899; Q8NF66; Q9BYP5; Q9BYP6;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Glutathione hydrolase 7 {ECO:0000303|PubMed:18357469};
DE            EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
DE   AltName: Full=Gamma-glutamyltransferase 7;
DE            Short=GGT 7;
DE            EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
DE   AltName: Full=Gamma-glutamyltransferase-like 3;
DE   AltName: Full=Gamma-glutamyltransferase-like 5;
DE   AltName: Full=Gamma-glutamyltranspeptidase 7;
DE   Contains:
DE     RecName: Full=Glutathione hydrolase 7 heavy chain;
DE   Contains:
DE     RecName: Full=Glutathione hydrolase 7 light chain;
DE   Flags: Precursor;
GN   Name=GGT7 {ECO:0000312|HGNC:HGNC:4259}; Synonyms=GGTL3, GGTL5;
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] (ISOFORM 3), AND INTERACTION WITH TLCD3A.
RX   PubMed=12270127; DOI=10.1016/s0006-291x(02)02227-1;
RA   He X.H., Di Y., Li J., Xie Y., Tang Y., Zhang F., Wei L., Zhang Y.,
RA   Qin W.X., Huo K., Li Y., Wan D.F., Gu J.R.;
RT   "Molecular cloning and characterization of CT120, a novel membrane-
RT   associated gene involved in amino acid transport and glutathione
RT   metabolism.";
RL   Biochem. Biophys. Res. Commun. 297:528-536(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Spleen;
RX   PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA   Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA   Ohara O.;
RT   "Characterization of long cDNA clones from human adult spleen. II. The
RT   complete sequences of 81 cDNA clones.";
RL   DNA Res. 10:49-57(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [5]
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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Hydrolyzes and transfers gamma-glutamyl moieties from
CC       glutathione and other gamma-glutamyl compounds to acceptors.
CC       {ECO:0000250|UniProtKB:P19440}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC         5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC         Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC         ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC         ChEBI:CHEBI:78608; EC=2.3.2.2;
CC         Evidence={ECO:0000250|UniProtKB:P19440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905;
CC         Evidence={ECO:0000250|UniProtKB:P19440};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC         Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC         Evidence={ECO:0000250|UniProtKB:P19440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC         Evidence={ECO:0000250|UniProtKB:P19440};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC         cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC         ChEBI:CHEBI:143103; EC=3.4.19.13;
CC         Evidence={ECO:0000250|UniProtKB:P19440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC         Evidence={ECO:0000250|UniProtKB:P19440};
CC   -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC       {ECO:0000250|UniProtKB:P19440}.
CC   -!- SUBUNIT: [Isoform 3]: Interacts with TLCD3A.
CC       {ECO:0000269|PubMed:12270127}.
CC   -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC       site is located in the light chain. {ECO:0000250|UniProtKB:P19440}.
CC   -!- INTERACTION:
CC       Q9UJ14; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-1058791, EBI-12256978;
CC       Q9UJ14; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-1058791, EBI-2807956;
CC       Q9UJ14; P49447: CYB561; NbExp=3; IntAct=EBI-1058791, EBI-8646596;
CC       Q9UJ14; O00155: GPR25; NbExp=6; IntAct=EBI-1058791, EBI-10178951;
CC       Q9UJ14; Q8TAF8: LHFPL5; NbExp=11; IntAct=EBI-1058791, EBI-2820517;
CC       Q9UJ14; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-1058791, EBI-12133176;
CC       Q9UJ14; Q13021: MALL; NbExp=6; IntAct=EBI-1058791, EBI-750078;
CC       Q9UJ14; Q96G79: SLC35A4; NbExp=3; IntAct=EBI-1058791, EBI-12363689;
CC       Q9UJ14; Q9NWH2: TMEM242; NbExp=6; IntAct=EBI-1058791, EBI-10315004;
CC       Q9UJ14; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-1058791, EBI-12195249;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19440}; Single-
CC       pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=a;
CC         IsoId=Q9UJ14-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UJ14-4; Sequence=VSP_008134, VSP_008138, VSP_008139;
CC       Name=3; Synonyms=GGTL3B, B;
CC         IsoId=Q9UJ14-5; Sequence=VSP_008136, VSP_008137;
CC       Name=4;
CC         IsoId=Q9UJ14-6; Sequence=VSP_008133, VSP_008140, VSP_008141;
CC   -!- TISSUE SPECIFICITY: Widely expressed, but at low level, except in the
CC       airway epithelial cells. Detected in brain, heart, kidney, liver, lung,
CC       spleen, testis and trachea.
CC   -!- PTM: Cleaved by autocatalysis into a large and a small subunit and the
CC       autocatalytic cleavage is essential to the functional activation of the
CC       enzyme. {ECO:0000250|UniProtKB:P19440}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC03394.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY138815; AAN15928.1; -; mRNA.
DR   EMBL; AK097100; BAC04950.1; -; mRNA.
DR   EMBL; AK090413; BAC03394.1; ALT_INIT; mRNA.
DR   EMBL; AL049709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS13242.2; -. [Q9UJ14-1]
DR   RefSeq; NP_821158.2; NM_178026.2. [Q9UJ14-1]
DR   AlphaFoldDB; Q9UJ14; -.
DR   SMR; Q9UJ14; -.
DR   BioGRID; 108953; 217.
DR   IntAct; Q9UJ14; 54.
DR   MINT; Q9UJ14; -.
DR   STRING; 9606.ENSP00000338964; -.
DR   MEROPS; T03.017; -.
DR   GlyConnect; 1258; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q9UJ14; 10 sites, 1 glycan.
DR   GlyGen; Q9UJ14; 11 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UJ14; -.
DR   PhosphoSitePlus; Q9UJ14; -.
DR   SwissPalm; Q9UJ14; -.
DR   BioMuta; GGT7; -.
DR   DMDM; 152031612; -.
DR   CPTAC; CPTAC-1493; -.
DR   EPD; Q9UJ14; -.
DR   jPOST; Q9UJ14; -.
DR   MassIVE; Q9UJ14; -.
DR   MaxQB; Q9UJ14; -.
DR   PaxDb; 9606-ENSP00000338964; -.
DR   PeptideAtlas; Q9UJ14; -.
DR   ProteomicsDB; 84578; -. [Q9UJ14-1]
DR   ProteomicsDB; 84579; -. [Q9UJ14-4]
DR   ProteomicsDB; 84580; -. [Q9UJ14-5]
DR   Pumba; Q9UJ14; -.
DR   Antibodypedia; 2429; 150 antibodies from 24 providers.
DR   DNASU; 2686; -.
DR   Ensembl; ENST00000336431.10; ENSP00000338964.5; ENSG00000131067.17. [Q9UJ14-1]
DR   GeneID; 2686; -.
DR   KEGG; hsa:2686; -.
DR   MANE-Select; ENST00000336431.10; ENSP00000338964.5; NM_178026.3; NP_821158.2.
DR   UCSC; uc002xay.4; human. [Q9UJ14-1]
DR   AGR; HGNC:4259; -.
DR   CTD; 2686; -.
DR   DisGeNET; 2686; -.
DR   GeneCards; GGT7; -.
DR   HGNC; HGNC:4259; GGT7.
DR   HPA; ENSG00000131067; Low tissue specificity.
DR   MIM; 612342; gene.
DR   neXtProt; NX_Q9UJ14; -.
DR   OpenTargets; ENSG00000131067; -.
DR   PharmGKB; PA28669; -.
DR   VEuPathDB; HostDB:ENSG00000131067; -.
DR   eggNOG; KOG2410; Eukaryota.
DR   GeneTree; ENSGT00940000156917; -.
DR   HOGENOM; CLU_014813_4_1_1; -.
DR   InParanoid; Q9UJ14; -.
DR   OMA; ICGMGPP; -.
DR   OrthoDB; 2910309at2759; -.
DR   PhylomeDB; Q9UJ14; -.
DR   TreeFam; TF333329; -.
DR   PathwayCommons; Q9UJ14; -.
DR   Reactome; R-HSA-174403; Glutathione synthesis and recycling.
DR   Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-HSA-9753281; Paracetamol ADME.
DR   SignaLink; Q9UJ14; -.
DR   UniPathway; UPA00204; -.
DR   BioGRID-ORCS; 2686; 19 hits in 1165 CRISPR screens.
DR   ChiTaRS; GGT7; human.
DR   GeneWiki; GGTL3; -.
DR   GenomeRNAi; 2686; -.
DR   Pharos; Q9UJ14; Tbio.
DR   PRO; PR:Q9UJ14; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9UJ14; Protein.
DR   Bgee; ENSG00000131067; Expressed in right hemisphere of cerebellum and 163 other cell types or tissues.
DR   ExpressionAtlas; Q9UJ14; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0036374; F:glutathione hydrolase activity; IBA:GO_Central.
DR   GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR   GO; GO:1901750; P:leukotriene D4 biosynthetic process; ISS:UniProtKB.
DR   GO; GO:1902883; P:negative regulation of response to oxidative stress; IMP: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; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR11686:SF9; GLUTATHIONE HYDROLASE 7; 1.
DR   Pfam; PF01019; G_glu_transpept; 1.
DR   PRINTS; PR01210; GGTRANSPTASE.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   Genevisible; Q9UJ14; HS.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Glutathione biosynthesis;
KW   Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Zymogen.
FT   CHAIN           1..472
FT                   /note="Glutathione hydrolase 7 heavy chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011066"
FT   CHAIN           473..662
FT                   /note="Glutathione hydrolase 7 light chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011067"
FT   TOPO_DOM        1..106
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P07314"
FT   TRANSMEM        107..127
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..662
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P07314"
FT   REGION          26..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MZ4"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99JP7"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99JP7"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        586
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..283
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12693554"
FT                   /id="VSP_008133"
FT   VAR_SEQ         1..76
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_008134"
FT   VAR_SEQ         226..251
FT                   /note="PGLLVGVPGMVKGLHEAHQLYGRLPW -> VGTLVRRESSGESLFIALLLTQ
FT                   ALIC (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12270127"
FT                   /id="VSP_008136"
FT   VAR_SEQ         252..662
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12270127"
FT                   /id="VSP_008137"
FT   VAR_SEQ         273..289
FT                   /note="ARALAEQLPPNMSERFR -> GQWGLGIWERHEVDGEG (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_008138"
FT   VAR_SEQ         290..662
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_008139"
FT   VAR_SEQ         369..425
FT                   /note="HLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALAS
FT                   RLGDP -> DLSPGSQGPPSGEASQSMATSFWPRDSSPFHRRETKAVSYLGSQLLKQTR
FT                   VSPPSEK (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12693554"
FT                   /id="VSP_008140"
FT   VAR_SEQ         426..662
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12693554"
FT                   /id="VSP_008141"
FT   CONFLICT        5
FT                   /note="N -> K (in Ref. 1; AAN15928)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   662 AA;  70467 MW;  29DDBC719CADD195 CRC64;
     MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS
     FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG
     VTVALVMQIY FGDPQIFQQG AVVTDAARCT SLGIEVLSKQ GSSVDAAVAA ALCLGIVAPH
     SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREETLQR SWETKPGLLV GVPGMVKGLH
     EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLARALAEQL PPNMSERFRE TFLPSGRPPL
     PGSLLHRPDL AEVLDVLGTS GPAAFYAGGN LTLEMVAEAQ HAGGVITEED FSNYSALVEK
     PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS
     RLGDPVYDST ITESMDDMLS KVEAAYLRGH INDSQAAPAP LLPVYELDGA PTAAQVLIMG
     PDDFIVAMVS SLNQPFGSGL ITPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL
     SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
     QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFIIAVKD PRSPDAAGAT
     IL
//