MTH_DROME
ID MTH_DROME Reviewed; 514 AA.
AC O97148; B5RJF9; Q9GN21; Q9GN78; Q9GND6; Q9GNE8; Q9GT57; Q9GT58; Q9GT59;
AC Q9GT60; Q9W0R4;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=G-protein coupled receptor Mth;
DE AltName: Full=Protein methuselah;
DE Flags: Precursor;
GN Name=mth; ORFNames=CG6936;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=9794765; DOI=10.1126/science.282.5390.943;
RA Lin Y.-J., Seroude L., Benzer S.;
RT "Extended life-span and stress resistance in the Drosophila mutant
RT methuselah.";
RL Science 282:943-946(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), AND VARIANTS ILE-54;
RP ALA-132; ASN-151; VAL-281; ASN-357; ASN-387 AND VAL-407.
RC STRAIN=CT97_1, CT97_3, CT97_4, DPF96_3.0, DPF96_74.2, HFL97_12, HFL97_15,
RC HFL97_16, HFL97_8, JFL97_1, JFL97_5, JFL97_9, MA97_1, MA97_4, MA97_6,
RC MFL97_1, MFL97_3, MFL97_6, SC96_19.4, VT97_1, VT97_39, VT97_41, ZIM(H)23,
RC ZIM(H)26, ZIM(H)39, ZIM(H)44, ZIM(S)15, ZIM(S)24, ZIM(S)35, ZIM(S)37, and
RC ZIM(S)49;
RX PubMed=10995474; DOI=10.1073/pnas.190338897;
RA Schmidt P.S., Duvernell D.D., Eanes W.F.;
RT "Adaptive evolution of a candidate gene for aging in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10861-10865(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12367510; DOI=10.1016/s0896-6273(02)00932-7;
RA Song W., Ranjan R., Dawson-Scully K., Bronk P., Marin L., Seroude L.,
RA Lin Y.J., Nie Z., Atwood H.L., Benzer S., Zinsmaier K.E.;
RT "Presynaptic regulation of neurotransmission in Drosophila by the G
RT protein-coupled receptor methuselah.";
RL Neuron 36:105-119(2002).
RN [8]
RP FUNCTION.
RX PubMed=15133470; DOI=10.1038/ncb1133;
RA Cvejic S., Zhu Z., Felice S.J., Berman Y., Huang X.Y.;
RT "The endogenous ligand Stunted of the GPCR Methuselah extends lifespan in
RT Drosophila.";
RL Nat. Cell Biol. 6:540-546(2004).
RN [9]
RP FUNCTION.
RX PubMed=19672878; DOI=10.1002/pro.221;
RA Ja W.W., Carvalho G.B., Madrigal M., Roberts R.W., Benzer S.;
RT "The Drosophila G protein-coupled receptor, Methuselah, exhibits a
RT promiscuous response to peptides.";
RL Protein Sci. 18:2203-2208(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-219, AND DISULFIDE BOND.
RX PubMed=11274391; DOI=10.1073/pnas.051625298;
RA West A.P. Jr., Llamas L.L., Snow P.M., Benzer S., Bjorkman P.J.;
RT "Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-
RT coupled receptor associated with extended lifespan.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3744-3749(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 25-212 IN COMPLEX WITH SYNTHETIC
RP RWR MOTIF CONTAINING PEPTIDES, GLYCOSYLATION AT ASN-45; ASN-123 AND
RP ASN-170, AND DISULFIDE BOND.
RX PubMed=17546039; DOI=10.1038/nchembio.2007.2;
RA Ja W.W., West A.P. Jr., Delker S.L., Bjorkman P.J., Benzer S.,
RA Roberts R.W.;
RT "Extension of Drosophila melanogaster life span with a GPCR peptide
RT inhibitor.";
RL Nat. Chem. Biol. 3:415-419(2007).
CC -!- FUNCTION: Involved in biological aging and stress response. Essential
CC for adult survival. Required in the presynaptic motor neuron to up-
CC regulate neurotransmitter exocytosis at larval glutamatergic
CC neuromuscular junctions (NMJs). Regulates a step associated with
CC docking and clustering of vesicles at release sites. SP/Acp70A and sun
CC are agonists that activate mth in vitro. {ECO:0000269|PubMed:12367510,
CC ECO:0000269|PubMed:15133470, ECO:0000269|PubMed:19672878,
CC ECO:0000269|PubMed:9794765}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17546039}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12367510};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12367510}. Note=Plasma
CC membrane of presynaptic terminals and innervating axons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O97148-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O97148-2; Sequence=VSP_002023;
CC -!- DISRUPTION PHENOTYPE: Increase in average life-span and enhanced
CC resistance to various forms of stress, including starvation, high
CC temperature and dietary paraquat, a free-radical generator.
CC {ECO:0000269|PubMed:9794765}.
CC -!- MISCELLANEOUS: Agonists of mth share minimal sequence homology,
CC suggesting a remarkable promiscuity of mth for activation.
CC {ECO:0000269|PubMed:19672878}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG22708.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22710.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22711.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22712.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22713.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22714.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22715.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22717.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22719.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22720.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22721.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22722.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22723.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22724.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22725.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22726.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22727.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22728.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22729.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22730.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22731.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22732.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22734.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22735.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22736.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22737.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG22738.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF109308; AAD16981.1; -; mRNA.
DR EMBL; AF280552; AAG22708.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280553; AAG22709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280554; AAG22710.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280555; AAG22711.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280556; AAG22712.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280557; AAG22713.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280558; AAG22714.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280559; AAG22715.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280560; AAG22716.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280561; AAG22717.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280562; AAG22718.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280563; AAG22719.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280564; AAG22720.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280565; AAG22721.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280566; AAG22722.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280567; AAG22723.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280568; AAG22724.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280569; AAG22725.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280570; AAG22726.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280571; AAG22727.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280572; AAG22728.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280573; AAG22729.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280574; AAG22730.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280575; AAG22731.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280576; AAG22732.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280577; AAG22733.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280578; AAG22734.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280579; AAG22735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280580; AAG22736.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280581; AAG22737.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF280582; AAG22738.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014296; AAF47379.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11440.1; -; Genomic_DNA.
DR EMBL; AY052111; AAK93535.1; -; mRNA.
DR EMBL; BT044433; ACH92498.1; -; mRNA.
DR RefSeq; NP_001246535.1; NM_001259606.2. [O97148-1]
DR RefSeq; NP_523871.1; NM_079147.4. [O97148-1]
DR RefSeq; NP_728521.1; NM_167829.3. [O97148-2]
DR PDB; 1FJR; X-ray; 2.30 A; A/B=25-219.
DR PDB; 2PZX; X-ray; 3.50 A; A/B/C/D=25-212.
DR PDBsum; 1FJR; -.
DR PDBsum; 2PZX; -.
DR AlphaFoldDB; O97148; -.
DR SMR; O97148; -.
DR BioGRID; 63614; 1.
DR STRING; 7227.FBpp0072470; -.
DR BindingDB; O97148; -.
DR ChEMBL; CHEMBL3309000; -.
DR TCDB; 9.A.14.14.2; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; O97148; 6 sites.
DR iPTMnet; O97148; -.
DR PaxDb; O97148; -.
DR DNASU; 38058; -.
DR EnsemblMetazoa; FBtr0072570; FBpp0072469; FBgn0023000. [O97148-1]
DR EnsemblMetazoa; FBtr0072571; FBpp0072470; FBgn0023000. [O97148-2]
DR EnsemblMetazoa; FBtr0306850; FBpp0297746; FBgn0023000. [O97148-1]
DR GeneID; 38058; -.
DR KEGG; dme:Dmel_CG6936; -.
DR UCSC; CG6936-RA; d. melanogaster. [O97148-1]
DR CTD; 38058; -.
DR FlyBase; FBgn0023000; mth.
DR VEuPathDB; VectorBase:FBgn0023000; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000168274; -.
DR HOGENOM; CLU_002753_3_0_1; -.
DR InParanoid; O97148; -.
DR OMA; DFCITAG; -.
DR PhylomeDB; O97148; -.
DR BioGRID-ORCS; 38058; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; O97148; -.
DR GenomeRNAi; 38058; -.
DR PRO; PR:O97148; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0023000; Expressed in embryonic/larval hemocyte (Drosophila) and 40 other tissues.
DR ExpressionAtlas; O97148; baseline and differential.
DR Genevisible; O97148; DM.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IPI:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:FlyBase.
DR GO; GO:0042277; F:peptide binding; IPI:FlyBase.
DR GO; GO:0007568; P:aging; IMP:FlyBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0008340; P:determination of adult lifespan; IDA:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:1901562; P:response to paraquat; IMP:FlyBase.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:FlyBase.
DR CDD; cd00251; Mth_Ecto; 1.
DR Gene3D; 2.170.180.11; -; 1.
DR Gene3D; 2.30.160.11; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR044860; Methusela_ecto_dom_1.
DR InterPro; IPR023311; Methusela_ecto_dom_2.
DR InterPro; IPR010596; Methuselah_N_dom.
DR InterPro; IPR036272; Methuselah_N_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF06652; Methuselah_N; 1.
DR SUPFAM; SSF63877; SSF63877; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Exocytosis; G-protein coupled receptor; Glycoprotein; Membrane;
KW Neurotransmitter transport; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT CHAIN 25..514
FT /note="G-protein coupled receptor Mth"
FT /id="PRO_0000013020"
FT TOPO_DOM 25..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0007744|PDB:1FJR"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0007744|PDB:1FJR"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0007744|PDB:1FJR"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..83
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0000269|PubMed:17546039, ECO:0007744|PDB:1FJR,
FT ECO:0007744|PDB:2PZX"
FT DISULFID 85..90
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0000269|PubMed:17546039, ECO:0007744|PDB:1FJR,
FT ECO:0007744|PDB:2PZX"
FT DISULFID 94..188
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0000269|PubMed:17546039, ECO:0007744|PDB:1FJR,
FT ECO:0007744|PDB:2PZX"
FT DISULFID 95..106
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0000269|PubMed:17546039, ECO:0007744|PDB:1FJR,
FT ECO:0007744|PDB:2PZX"
FT DISULFID 150..209
FT /evidence="ECO:0000269|PubMed:11274391,
FT ECO:0000269|PubMed:17546039, ECO:0007744|PDB:1FJR,
FT ECO:0007744|PDB:2PZX"
FT VAR_SEQ 487..514
FT /note="SIRGEGEEVNNSEEEISLENTTTRNVLL -> RNHPKSTRSVISNRSMASRI
FT TVGTTPKNKARNSPLA (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.6"
FT /id="VSP_002023"
FT VARIANT 54
FT /note="L -> I (in strain: MA97_6)"
FT /evidence="ECO:0000269|PubMed:10995474"
FT VARIANT 132
FT /note="S -> A (in strain: ZIM(S)49 and ZIM(H)44)"
FT /evidence="ECO:0000269|PubMed:10995474"
FT VARIANT 151
FT /note="D -> N (in strain: CT97_3, MFL97_1 and ZIM(S)37)"
FT /evidence="ECO:0000269|PubMed:10995474"
FT VARIANT 281
FT /note="F -> V (in strain: ZIM(S)49 and ZIM(H)44)"
FT /evidence="ECO:0000269|PubMed:10995474"
FT VARIANT 357
FT /note="H -> N (in strain: DPF96_3.0, HFL97_15, JFL97_1,
FT JFL97_9 and ZIM(S)37)"
FT /evidence="ECO:0000269|PubMed:10995474"
FT VARIANT 387
FT /note="T -> N (in strain: ZIM(S)35)"
FT /evidence="ECO:0000269|PubMed:10995474"
FT VARIANT 407
FT /note="A -> V (in strain: ZIM(H)23)"
FT /evidence="ECO:0000269|PubMed:10995474"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1FJR"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1FJR"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1FJR"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1FJR"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1FJR"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1FJR"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:1FJR"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:1FJR"
SQ SEQUENCE 514 AA; 59644 MW; F2A5370CECCD1D5C CRC64;
MKTLLVLRIS TVILVVLVIQ KSYADILECD YFDTVDISAA QKLQNGSYLF EGLLVPAILT
GEYDFRILPD DSKQKVARHI RGCVCKLKPC VRFCCPHDHI MDNGVCYDNM SDEELAELDP
FLNVTLDDGS VSRRHFKNEL IVQWDLPMPC DGMFYLDNRE EQDKYTLFEN GTFFRHFDRV
TLRKREYCLQ HLTFADGNAT SIRIAPHNCL IVPSITGQTV VMISSLICMV LTIAVYLFVK
KLQNLHGKCF ICYMVCLFMG YLFLLLDLWQ ISISFCKPAG FLGYFFVMAA FFWLSVISLH
LWNTFRGSSH KANRFLFEHR FLAYNTYAWG MAVVLTGITV LADNIVENQD WNPRVGHEGH
CWIYTQAWSA MLYFYGPMVF LIAFNITMFI LTAKRILGVK KDIQNFAHRQ ERKQKLNSDK
QTYTFFLRLF IIMGLSWSLE IGSYFSQSNQ TWANVFLVAD YLNWSQGIII FILFVLKRST
WRLLQESIRG EGEEVNNSEE EISLENTTTR NVLL
