GGT5_MOUSE
ID GGT5_MOUSE Reviewed; 573 AA.
AC Q9Z2A9; Q8C7B4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Glutathione hydrolase 5 proenzyme;
DE EC=3.4.19.13 {ECO:0000250|UniProtKB:P36269};
DE AltName: Full=Gamma-glutamyl leukotrienase {ECO:0000303|PubMed:9774450};
DE Short=GGL {ECO:0000303|PubMed:9774450};
DE AltName: Full=Gamma-glutamyltransferase 5;
DE Short=GGT 5;
DE EC=2.3.2.2 {ECO:0000250|UniProtKB:P36269};
DE AltName: Full=Gamma-glutamyltransferase-like activity 1;
DE AltName: Full=Gamma-glutamyltranspeptidase 5;
DE AltName: Full=Leukotriene-C4 hydrolase;
DE EC=3.4.19.14 {ECO:0000269|PubMed:11463821, ECO:0000269|PubMed:12163373, ECO:0000269|PubMed:9774450};
DE Contains:
DE RecName: Full=Glutathione hydrolase 5 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 5 light chain;
DE Flags: Precursor;
GN Name=Ggt5; Synonyms=Ggtla1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=C57BL/6 X 129; TISSUE=Spleen;
RX PubMed=9774450; DOI=10.1074/jbc.273.43.28277;
RA Carter B.Z., Shi Z.-Z., Barrios R., Lieberman M.W.;
RT "Gamma-glutamyl leukotrienase, a gamma-glutamyl transpeptidase gene family
RT member, is expressed primarily in spleen.";
RL J. Biol. Chem. 273:28277-28285(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=11463821; DOI=10.1128/mcb.21.16.5389-5395.2001;
RA Shi Z.Z., Han B., Habib G.M., Matzuk M.M., Lieberman M.W.;
RT "Disruption of gamma-glutamyl leukotrienase results in disruption of
RT leukotriene D(4) synthesis in vivo and attenuation of the acute
RT inflammatory response.";
RL Mol. Cell. Biol. 21:5389-5395(2001).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND GLYCOSYLATION.
RX PubMed=12163373; DOI=10.1016/s0002-9440(10)64204-6;
RA Han B., Luo G., Shi Z.Z., Barrios R., Atwood D., Liu W., Habib G.M.,
RA Sifers R.N., Corry D.B., Lieberman M.W.;
RT "Gamma-glutamyl leukotrienase, a novel endothelial membrane protein, is
RT specifically responsible for leukotriene D(4) formation in vivo.";
RL Am. J. Pathol. 161:481-490(2002).
CC -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and
CC glutathione-S-conjugate (By similarity). Converts leukotriene C4
CC (LTC4), a glutathione-S-conjugate, to leukotriene D4 (LTD4)
CC (PubMed:9774450, PubMed:11463821, PubMed:12163373). Does not cleaves
CC gamma-glutamyl compounds such as gamma-glutamyl leucine. May also
CC catalyze a transpeptidation reaction in addition to the hydrolysis
CC reaction, transferring the gamma-glutamyl moiety to an acceptor amino
CC acid to form a new gamma-glutamyl compound. Acts as a negative
CC regulator of geranylgeranyl glutathione bioactivity by cleaving off its
CC gamma-glutamyl group, playing a role in adaptive immune responses (By
CC similarity). {ECO:0000250|UniProtKB:P36269,
CC ECO:0000269|PubMed:11463821, ECO:0000269|PubMed:12163373,
CC ECO:0000269|PubMed:9774450}.
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:P36269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905;
CC Evidence={ECO:0000250|UniProtKB:P36269};
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:P36269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC Evidence={ECO:0000250|UniProtKB:P36269};
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:P36269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC Evidence={ECO:0000250|UniProtKB:P36269};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4;
CC Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14;
CC Evidence={ECO:0000269|PubMed:11463821, ECO:0000269|PubMed:12163373,
CC ECO:0000269|PubMed:9774450};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564;
CC Evidence={ECO:0000269|PubMed:12163373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-[(2E,6E,10E)-geranylgeranyl]-L-glutathione = L-
CC glutamate + S-[(2E,6E,10E)-geranylgeranyl]-L-cysteinylglycine;
CC Xref=Rhea:RHEA:65120, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:156326, ChEBI:CHEBI:156330;
CC Evidence={ECO:0000250|UniProtKB:P36269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65121;
CC Evidence={ECO:0000250|UniProtKB:P36269};
CC -!- ACTIVITY REGULATION: Inhibited by serine-borate.
CC {ECO:0000250|UniProtKB:P36269}.
CC -!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.
CC {ECO:0000269|PubMed:11463821, ECO:0000269|PubMed:12163373,
CC ECO:0000269|PubMed:9774450}.
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000250|UniProtKB:P36269}.
CC -!- SUBUNIT: Heterodimer composed of the light and heavy chains
CC (PubMed:12163373). The active site is located in the light chain (By
CC similarity). {ECO:0000250|UniProtKB:P19440,
CC ECO:0000269|PubMed:12163373}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12163373}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:12163373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z2A9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2A9-2; Sequence=VSP_008147, VSP_008148;
CC -!- TISSUE SPECIFICITY: Very low level of expression. Detected in spleen
CC lymphocytes, medullary and paracortical thymic lymphocytes, lung
CC interstitial cells, bronchial epithelium, proximal tubules in kidney,
CC crypt cells in small intestine, neurons in brain stem and cerebral
CC cortex and in Purkinje cells. {ECO:0000269|PubMed:12163373,
CC ECO:0000269|PubMed:9774450}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Very low expression.
CC {ECO:0000269|PubMed:9774450}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12163373}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice shown no obvious phenotype but in
CC most organs they have only 10% of the wild-type levels of gamma-
CC glutamyl leukotrienase activity (PubMed:11463821). Mice deficient in
CC GGT5 have significantly more airway hyper-reactivity in a model of
CC experimental asthma (PubMed:12163373). {ECO:0000269|PubMed:11463821,
CC ECO:0000269|PubMed:12163373}.
CC -!- MISCELLANEOUS: A previous study reported that GSH and oxidized
CC glutathione (GSSG) are not substrates for murine GGT5 (PubMed:9774450).
CC However, this result contrasts with two studies reported that GSH is
CC indeed a substrate for GGT5 (By similarity).
CC {ECO:0000250|UniProtKB:P36269, ECO:0000269|PubMed:9774450}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF077765; AAC71001.1; -; mRNA.
DR EMBL; AK052183; BAC34873.1; -; mRNA.
DR EMBL; AK170326; BAE41720.1; -; mRNA.
DR EMBL; AC087540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466553; EDL31901.1; -; Genomic_DNA.
DR EMBL; BC113775; AAI13776.1; -; mRNA.
DR CCDS; CCDS23928.1; -. [Q9Z2A9-1]
DR RefSeq; NP_035950.2; NM_011820.4. [Q9Z2A9-1]
DR AlphaFoldDB; Q9Z2A9; -.
DR SMR; Q9Z2A9; -.
DR STRING; 10090.ENSMUSP00000072074; -.
DR MEROPS; T03.002; -.
DR GlyConnect; 2331; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Z2A9; 7 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9Z2A9; -.
DR PhosphoSitePlus; Q9Z2A9; -.
DR SwissPalm; Q9Z2A9; -.
DR EPD; Q9Z2A9; -.
DR jPOST; Q9Z2A9; -.
DR MaxQB; Q9Z2A9; -.
DR PaxDb; Q9Z2A9; -.
DR PeptideAtlas; Q9Z2A9; -.
DR PRIDE; Q9Z2A9; -.
DR ProteomicsDB; 266803; -. [Q9Z2A9-1]
DR ProteomicsDB; 266804; -. [Q9Z2A9-2]
DR Antibodypedia; 285; 130 antibodies from 27 providers.
DR DNASU; 23887; -.
DR Ensembl; ENSMUST00000072217; ENSMUSP00000072074; ENSMUSG00000006344. [Q9Z2A9-1]
DR GeneID; 23887; -.
DR KEGG; mmu:23887; -.
DR UCSC; uc007fqq.1; mouse. [Q9Z2A9-1]
DR CTD; 2687; -.
DR MGI; MGI:1346063; Ggt5.
DR VEuPathDB; HostDB:ENSMUSG00000006344; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000155794; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; Q9Z2A9; -.
DR OMA; VCGMGPP; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; Q9Z2A9; -.
DR TreeFam; TF313608; -.
DR BRENDA; 3.4.19.14; 3474.
DR Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR SABIO-RK; Q9Z2A9; -.
DR UniPathway; UPA00204; -.
DR UniPathway; UPA00880; -.
DR BioGRID-ORCS; 23887; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9Z2A9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9Z2A9; protein.
DR Bgee; ENSMUSG00000006344; Expressed in granulocyte and 82 other tissues.
DR ExpressionAtlas; Q9Z2A9; baseline and differential.
DR Genevisible; Q9Z2A9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0036374; F:glutathione hydrolase activity; ISO:MGI.
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:0002951; F:leukotriene-C(4) hydrolase; IMP:UniProtKB.
DR GO; GO:0000048; F:peptidyltransferase activity; ISO:MGI.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:1901750; P:leukotriene D4 biosynthetic process; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
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.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Glutathione biosynthesis;
KW Glycoprotein; Hydrolase; Leukotriene biosynthesis; Membrane; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..388
FT /note="Glutathione hydrolase 5 heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT /id="PRO_0000011074"
FT CHAIN 389..573
FT /note="Glutathione hydrolase 5 light chain"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT /id="PRO_0000011075"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12163373"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000269|PubMed:12163373"
FT TOPO_DOM 30..573
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:12163373"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 110
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 407
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 428
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 454..455
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 447..456
FT /note="VPGERPPSSM -> DYHEQAVAWL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9774450"
FT /id="VSP_008147"
FT VAR_SEQ 457..573
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9774450"
FT /id="VSP_008148"
FT CONFLICT 479
FT /note="L -> P (in Ref. 1; AAC71001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 61674 MW; CB00F377DA1BE83E CRC64;
MAWGHRATVC LVLLGVGLGL VIVVLAAVLS PRQASCGPGA FTRAAVAADS KICSDIGRAI
LQQRGSPVDA AIAALVCTGV VNPQSMGLGG GVVFTIYNAS TGKVEIINAR ETVPASYDQG
LLNQCKNVLP LGTGAQWIGV PGELRGYAEA HRRHGRLPWA QLFQPTIALL REGFRVPFIL
SQFLNNSILR PHLSASTLRQ LFFNGTETLR SQDPFPWPAL ANTLETVAKE GAEVLYTGRL
GRMLVEDIAK QGSLLTVQDL AAFQPEVVEP LEMPLGNYTL YSPPPPAGGA ILSFILNVLK
GFNFSAETVA RPGGEVNMYH HLVETLKFAV GQRWRLWDPS SHPGIQNISR DLLREDLAQR
IRQQIDGRGD HHQLSHYNLT GVRGNRMGTS HVSVLGEDGS AVAATSTINT PFGAMVYSPR
TGILLNNELL DLCWRHMPTS PITPPPVPGE RPPSSMVPSI LVNKGQGSKL VIGGAGGELI
ISAVAQTIMN KLWLGFDLTE AIASPILHVN SKGHVEYEPK FNQEVQKGLQ DRGQIQSQSQ
RPVFLNAVQA VFQEGPCVYA ASDLRKAGKA SGY
