GGT7_HUMAN
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 03-AUG-2022, entry version 177.
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; 207.
DR IntAct; Q9UJ14; 53.
DR MINT; Q9UJ14; -.
DR STRING; 9606.ENSP00000338964; -.
DR MEROPS; T03.017; -.
DR GlyConnect; 1258; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UJ14; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9UJ14; -.
DR PhosphoSitePlus; 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; Q9UJ14; -.
DR PeptideAtlas; Q9UJ14; -.
DR PRIDE; Q9UJ14; -.
DR ProteomicsDB; 84578; -. [Q9UJ14-1]
DR ProteomicsDB; 84579; -. [Q9UJ14-4]
DR ProteomicsDB; 84580; -. [Q9UJ14-5]
DR Antibodypedia; 2429; 144 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 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; FMVIGSP; -.
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; 18 hits in 1083 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 161 other tissues.
DR ExpressionAtlas; Q9UJ14; baseline and differential.
DR Genevisible; Q9UJ14; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0036374; F:glutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
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; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
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
