PTP10_DROME
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 03-AUG-2022, entry version 189.
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.FBpp0303420; -.
DR GlyGen; P35992; 27 sites.
DR PaxDb; P35992; -.
DR PRIDE; P35992; -.
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 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; STPGQNC; -.
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 tissues.
DR ExpressionAtlas; P35992; baseline and differential.
DR Genevisible; P35992; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.10; -; 10.
DR Gene3D; 3.90.190.10; -; 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 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; SSF49265; SSF49265; 6.
DR SUPFAM; SSF52799; SSF52799; 1.
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.
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
