ID   PTP10_DROME             Reviewed;        1990 AA.
AC   P35992; A4V4B4; B7Z142; F0JAM3; M9PEB6; M9PJI5; Q0KHT5; Q86NN9; Q8IR87;
AC   Q9VYW1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 4.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Tyrosine-protein phosphatase 10D;
DE            EC=3.1.3.48;
DE   AltName: Full=Receptor-linked protein-tyrosine phosphatase 10D;
DE            Short=DPTP10D;
DE   Flags: Precursor;
GN   Name=Ptp10D; ORFNames=CG1817;
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] (ISOFORMS B AND E), FUNCTION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=1657401; DOI=10.1016/0092-8674(91)90062-4;
RA   Yang X., Seow K.T., Bahri S.M., Oon S.H., Chia W.;
RT   "Two Drosophila receptor-like tyrosine phosphatase genes are expressed in a
RT   subset of developing axons and pioneer neurons in the embryonic CNS.";
RL   Cell 67:661-673(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=1657402; DOI=10.1016/0092-8674(91)90063-5;
RA   Tian S.-S., Tsoulfas P., Zinn K.;
RT   "Three receptor-linked protein-tyrosine phosphatases are selectively
RT   expressed on central nervous system axons in the Drosophila embryo.";
RL   Cell 67:675-685(1991).
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), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 43-1197 (ISOFORMS G/B/E).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Booth B., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May have a role in axon outgrowth and guidance.
CC       {ECO:0000269|PubMed:1657401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Isoform G is produced by readthrough of a stop codon between
CC         the codons for Arg-1631 and His-1633. This is likely to be a rare
CC         event with most transcripts using the stop codon following Arg-1631.
CC         {ECO:0000305};
CC       Name=G {ECO:0000312|FlyBase:FBgn0004370}; Synonyms=F
CC       {ECO:0000312|FlyBase:FBgn0004370};
CC         IsoId=P35992-5; Sequence=Displayed;
CC       Name=B {ECO:0000312|FlyBase:FBgn0004370}; Synonyms=Long;
CC         IsoId=P35992-1; Sequence=VSP_057308;
CC       Name=E {ECO:0000312|FlyBase:FBgn0004370}; Synonyms=Short, I
CC       {ECO:0000312|FlyBase:FBgn0004370};
CC         IsoId=P35992-2; Sequence=VSP_005143;
CC       Name=H {ECO:0000312|FlyBase:FBgn0004370};
CC         IsoId=P35992-6; Sequence=VSP_057306, VSP_057307, VSP_057308;
CC   -!- TISSUE SPECIFICITY: In 9-12 hour embryos, expression is specifically
CC       seen in the anterior commissure and its junctions with the longitudinal
CC       tracts. {ECO:0000269|PubMed:1657401, ECO:0000269|PubMed:1657402}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed throughout development to adulthood, lowest expression is
CC       during second and third larval instars. {ECO:0000269|PubMed:1657401}.
CC   -!- MISCELLANEOUS: This protein is translated by readthrough of a stop
CC       codon. Readthrough of the terminator codon TAG occurs between the
CC       codons for Arg-1631 and His-1633. There is currently no sequence that
CC       provides the identity of residue 1632. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class subfamily. {ECO:0000305}.
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DR   EMBL; M80465; AAA28484.1; -; mRNA.
DR   EMBL; M80538; AAA28952.1; -; mRNA.
DR   EMBL; AE014298; AAF48072.3; -; Genomic_DNA.
DR   EMBL; AE014298; AAS65319.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAS65320.2; -; Genomic_DNA.
DR   EMBL; AE014298; ACL82919.1; -; Genomic_DNA.
DR   EMBL; AE014298; AGB95296.1; -; Genomic_DNA.
DR   EMBL; AE014298; AGB95297.1; -; Genomic_DNA.
DR   EMBL; BT004474; AAO42638.1; -; mRNA.
DR   EMBL; BT126065; ADY17764.1; -; mRNA.
DR   PIR; C41214; C41214.
DR   PIR; D41214; D41214.
DR   RefSeq; NP_001138187.1; NM_001144715.2. [P35992-2]
DR   RefSeq; NP_001259453.1; NM_001272524.1. [P35992-6]
DR   RefSeq; NP_001259454.1; NM_001272525.1. [P35992-2]
DR   RefSeq; NP_727544.2; NM_167292.3. [P35992-1]
DR   RefSeq; NP_996413.2; NM_206690.2. [P35992-5]
DR   RefSeq; NP_996414.2; NM_206691.3. [P35992-5]
DR   PDB; 3S3E; X-ray; 2.40 A; A/B=1250-1533.
DR   PDB; 3S3F; X-ray; 2.70 A; A/B=1250-1533.
DR   PDB; 3S3H; X-ray; 2.80 A; A/B=1250-1533.
DR   PDB; 3S3K; X-ray; 3.20 A; A/B=1250-1533.
DR   PDBsum; 3S3E; -.
DR   PDBsum; 3S3F; -.
DR   PDBsum; 3S3H; -.
DR   PDBsum; 3S3K; -.
DR   SMR; P35992; -.
DR   BioGRID; 58524; 11.
DR   IntAct; P35992; 5.
DR   STRING; 7227.FBpp0303419; -.
DR   GlyCosmos; P35992; 27 sites, No reported glycans.
DR   GlyGen; P35992; 27 sites.
DR   PaxDb; 7227-FBpp0303420; -.
DR   EnsemblMetazoa; FBtr0073522; FBpp0073369; FBgn0004370. [P35992-1]
DR   EnsemblMetazoa; FBtr0273235; FBpp0271743; FBgn0004370. [P35992-2]
DR   EnsemblMetazoa; FBtr0330392; FBpp0303418; FBgn0004370. [P35992-5]
DR   EnsemblMetazoa; FBtr0330393; FBpp0303419; FBgn0004370. [P35992-5]
DR   EnsemblMetazoa; FBtr0330394; FBpp0303420; FBgn0004370. [P35992-6]
DR   EnsemblMetazoa; FBtr0331406; FBpp0303823; FBgn0004370. [P35992-2]
DR   GeneID; 32115; -.
DR   KEGG; dme:Dmel_CG1817; -.
DR   AGR; FB:FBgn0004370; -.
DR   CTD; 32115; -.
DR   FlyBase; FBgn0004370; Ptp10D.
DR   VEuPathDB; VectorBase:FBgn0004370; -.
DR   eggNOG; KOG0791; Eukaryota.
DR   GeneTree; ENSGT00940000154814; -.
DR   HOGENOM; CLU_001541_1_0_1; -.
DR   InParanoid; P35992; -.
DR   OMA; RNYTFTL; -.
DR   OrthoDB; 5399547at2759; -.
DR   PhylomeDB; P35992; -.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   SignaLink; P35992; -.
DR   BioGRID-ORCS; 32115; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Ptp10D; fly.
DR   GenomeRNAi; 32115; -.
DR   PRO; PR:P35992; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0004370; Expressed in cleaving embryo and 20 other cell types or tissues.
DR   ExpressionAtlas; P35992; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR   GO; GO:0060446; P:branching involved in open tracheal system development; IMP:FlyBase.
DR   GO; GO:0007417; P:central nervous system development; IGI:FlyBase.
DR   GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR   GO; GO:0008045; P:motor neuron axon guidance; IGI:FlyBase.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR   GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IGI:FlyBase.
DR   GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IGI:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IGI:FlyBase.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR   CDD; cd00063; FN3; 9.
DR   CDD; cd14548; R3-PTPc; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041201; PTPRJ_TM.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 9.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 11.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 6.
DR   PROSITE; PS50853; FN3; 9.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
DR   Genevisible; P35992; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW   Glycoprotein; Hydrolase; Membrane; Neurogenesis; Protein phosphatase;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..1990
FT                   /note="Tyrosine-protein phosphatase 10D"
FT                   /id="PRO_0000025427"
FT   TOPO_DOM        43..1197
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1198..1218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1219..1990
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          125..218
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          219..314
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          407..498
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          499..584
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          585..674
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          675..771
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          775..865
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          866..956
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          957..1057
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1272..1527
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1595..1637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1657..1693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1726..1879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1595..1619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1667..1693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1726..1761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1785..1801
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1811..1831
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1468
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         1436
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1468..1474
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1512
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        588
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        668
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        687
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        719
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        723
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        823
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        841
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        874
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        908
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        925
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1001
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         216
FT                   /note="K -> SRRTRHKELLDIKILRE (in isoform H)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057306"
FT   VAR_SEQ         1191
FT                   /note="T -> TEMLSSP (in isoform H)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057307"
FT   VAR_SEQ         1549..1980
FT                   /note="Missing (in isoform E)"
FT                   /evidence="ECO:0000303|PubMed:1657401,
FT                   ECO:0000303|PubMed:1657402"
FT                   /id="VSP_005143"
FT   VAR_SEQ         1632..1990
FT                   /note="Missing (in isoform B and isoform H)"
FT                   /evidence="ECO:0000303|PubMed:1657401, ECO:0000305"
FT                   /id="VSP_057308"
FT   CONFLICT        124
FT                   /note="D -> I (in Ref. 1; AAA28484)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="S -> L (in Ref. 1; AAA28484)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="P -> L (in Ref. 5; AAO42638)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="F -> S (in Ref. 1; AAA28484 and 2; AAA28952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        558
FT                   /note="G -> A (in Ref. 1; AAA28484 and 2; AAA28952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        810
FT                   /note="L -> S (in Ref. 1; AAA28484 and 2; AAA28952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1403
FT                   /note="N -> S (in Ref. 5; AAO42638)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1254..1256
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1257..1277
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   TURN            1278..1285
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1290..1292
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   TURN            1294..1296
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1297..1299
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1309..1311
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1312..1314
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   TURN            1319..1321
FT                   /evidence="ECO:0007829|PDB:3S3H"
FT   TURN            1322..1325
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1326..1332
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1340..1344
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1349..1351
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1352..1361
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1366..1369
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1373..1375
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1387..1390
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1392..1394
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1397..1406
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1408..1419
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1422..1431
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1436..1438
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1444..1457
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1464..1467
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1469..1472
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1473..1487
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   TURN            1488..1490
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   STRAND          1492..1494
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1496..1506
FT                   /evidence="ECO:0007829|PDB:3S3E"
FT   HELIX           1514..1528
FT                   /evidence="ECO:0007829|PDB:3S3E"
SQ   SEQUENCE   1990 AA;  222740 MW;  76FAAA08565AE8DA CRC64;
     MLYQLSKATT RIRLKRQKAV PQHRWLWSLA FLAAFTLKDV RCADLAISIP NNPGLDDGAS
     YRLDYSPPFG YPEPNTTIAS REIGDEIQFS RALPGTKYNF WLYYTNFTHH DWLTWTVTIT
     TAPDPPSNLS VQVRSGKNAI ILWSPPTQGS YTAFKIKVLG LSEASSSYNR TFQVNDNTFQ
     HSVKELTPGA TYQVQAYTIY DGKESVAYTS RNFTTKPNTP GKFIVWFRNE TTLLVLWQPP
     YPAGIYTHYK VSIEPPDAND SVLYVEKEGE PPGPAQAAFK GLVPGRAYNI SVQTMSEDEI
     SLPTTAQYRT VPLRPLNVTF DRDFITSNSF RVLWEAPKGI SEFDKYQVSV ATTRRQSTVP
     RSNEPVAFFD FRDIAEPGKT FNVIVKTVSG KVTSWPATGD VTLRPLPVRN LRSINDDKTN
     TMIITWEADP ASTQDEYRIV YHELETFNGD TSTLTTDRTR FTLESLLPGR NYSLSVQAVS
     KKMESNETSI FVVTRPSSPI IEDLKSIRMG LNISWKSDVN SKQEQYEVLY SRNGTSDLRT
     QKTKESRLVI KNLQPGAGYE LKVFAVSHDL RSEPHAYFQA VYPNPPRNMT IETVRSNSVL
     VHWSPPESGE FTEYSIRYRT DSEQQWVRLP SVRSTEADIT DMTKGEKYTI QVNTVSFGVE
     SPVPQEVNTT VPPNPVSNII QLVDSRNITL EWPKPEGRVE SYILKWWPSD NPGRVQTKNV
     SENKSADDLS TVRVLIGELM PGVQYKFDIQ TTSYGILSGI TSLYPRTMPL IQSDVVVANG
     EKEDERDTIT LSYTPTPQSS SKFDIYRFSL GDAEIRDKEK LANDTDRKVT FTGLVPGRLY
     NITVWTVSGG VASLPIQRQD RLYPEPITQL HATNITDTEI SLRWDLPKGE YNDFDIAYLT
     ADNLLAQNMT TRNEITISDL RPHRNYTFTV VVRSGTESSV LRSSSPLSAS FTTNEAVPGR
     VERFHPTDVQ PSEINFEWSL PSSEANGVIR QFSIAYTNIN NLTDAGMQDF ESEEAFGVIK
     NLKPGETYVF KIQAKTAIGF GPEREYRQTM PILAPPRPAT QVVPTEVYRS SSTIQIRFRK
     NYFSDQNGQV RMYTIIVAED DAKNASGLEM PSWLDVQSYS VWLPYQAIDP YYPFENRSVE
     DFTIGTENCD NHKIGYCNGP LKSGTTYRVK VRAFTGADKF TDTAYSFPIQ TDQDNTSLIV
     AITVPLTIIL VLLVTLLFYK RRRNNCRKTT KDSRANDNMS LPDSVIEQNR PILIKNFAEH
     YRLMSADSDF RFSEEFEELK HVGRDQPCTF ADLPCNRPKN RFTNILPYDH SRFKLQPVDD
     DEGSDYINAN YVPGHNSPRE FIVTQGPLHS TRDDFWRMCW ESNSRAIVML TRCFEKGREK
     CDQYWPNDTV PVFYGDIKVQ ILNDSHYADW VMTEFMLCRG SEQRILRHFH FTTWPDFGVP
     NPPQTLVRFV RAFRDRIGAE QRPIVVHCSA GVGRSGTFIT LDRILQQINT SDYVDIFGIV
     YAMRKERVWM VQTEQQYICI HQCLLAVLEG KENIVGPARE MHDNEGYEGQ QVQLDENGDV
     VATIEGHLSH HDLQQAEAEA IDDENAAILH DDQQPLTSSF TGHHTHMPPT TSMSSFGGGG
     GGHTNVDAPD RXHSVVNQSD NNNSVVIVLV DNKPSSMICK DSKGGNIDVL ESQQQQQQQQ
     QQQPNQGGHN ITTISAINGY NTLQHRRKSQ LITFSSSSCD IKNSLSHEYI NGSNGSAANG
     PPSSGSGSGS GPGSNRASRA NVRLSFAEED VMILPQNHSQ QSNHQDDEVF TRRRSLLEVE
     IGVEVGEDGE LAPHEMEEDL EEEDEDEELY MHDEFETHID TKSNNANDDS GGGSYEDSHA
     LHSSLGGSNR NSLEKDDDDI EVDVISTDVS CYDQLLGSSC NTRNGDDDDI ATLVGDGDYS
     TTKLSKASRL SGAGVGGLVV SGGGGGTAIG GGIAVNGGGV LGNGVGSEAG GGIIYANPFM
     DDEGIAESGM
//