PTPRA_MOUSE
ID PTPRA_MOUSE Reviewed; 829 AA.
AC P18052; A2AHF2; Q61808;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase alpha;
DE Short=Protein-tyrosine phosphatase alpha;
DE Short=R-PTP-alpha;
DE EC=3.1.3.48;
DE AltName: Full=LCA-related phosphatase;
DE AltName: Full=PTPTY-28;
DE Flags: Precursor;
GN Name=Ptpra; Synonyms=Lrp, Ptpa;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=2162042; DOI=10.1073/pnas.87.12.4444;
RA Matthews R.J., Cahir E.D., Thomas M.L.;
RT "Identification of an additional member of the protein-tyrosine-phosphatase
RT family: evidence for alternative splicing in the tyrosine phosphatase
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4444-4448(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=2166945; DOI=10.1073/pnas.87.16.6112;
RA Sap J., D'Eustachio P., Givol D., Schlessinger J.;
RT "Cloning and expression of a widely expressed receptor tyrosine
RT phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6112-6116(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8406469; DOI=10.1006/geno.1993.1279;
RA Wong E.C., Mullersman J.E., Thomas M.L.;
RT "Leukocyte common antigen-related phosphatase (LRP) gene structure:
RT conservation of the genomic organization of transmembrane protein tyrosine
RT phosphatases.";
RL Genomics 17:33-38(1993).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 322-356.
RX PubMed=1590786; DOI=10.1016/s0006-291x(05)80015-4;
RA den Hertog J., Pals C.E., Jonk L.J., Kruijer W.;
RT "Differential expression of a novel murine non-receptor protein tyrosine
RT phosphatase during differentiation of P19 embryonal carcinoma cells.";
RL Biochem. Biophys. Res. Commun. 184:1241-1249(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 358-467, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Myeloid leukemia cell;
RX PubMed=1932742;
RA Yi T., Cleveland J.L., Ihle J.N.;
RT "Identification of novel protein tyrosine phosphatases of hematopoietic
RT cells by polymerase chain reaction amplification.";
RL Blood 78:2222-2228(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 358-467.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7832766; DOI=10.1042/bj3050499;
RA Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT "A novel receptor-type protein tyrosine phosphatase with a single catalytic
RT domain is specifically expressed in mouse brain.";
RL Biochem. J. 305:499-504(1995).
RN [9]
RP PROTEIN SEQUENCE OF 566-576, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 651-756.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=1454056; DOI=10.1007/bf00419663;
RA Schepens J., Zeeuwen P., Wieringa B., Hendriks W.;
RT "Identification and typing of members of the protein-tyrosine phosphatase
RT gene family expressed in mouse brain.";
RL Mol. Biol. Rep. 16:241-248(1992).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-204 AND TYR-825, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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 [16]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH BCAR3; BCAR1 AND SRC,
RP INTERACTION WITH GRB2 AND BCAR3, SUBCELLULAR LOCATION, AND PHOSPHORYLATION
RP AT TYR-825.
RX PubMed=22801373; DOI=10.1128/mcb.00214-12;
RA Sun G., Cheng S.Y., Chen M., Lim C.J., Pallen C.J.;
RT "Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to
RT position Cas for activation at integrin-mediated focal adhesions.";
RL Mol. Cell. Biol. 32:3776-3789(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 202-503.
RX PubMed=8700232; DOI=10.1038/382555a0;
RA Bilwes A.M., den Hertog J., Hunter T., Noel J.P.;
RT "Structural basis for inhibition of receptor protein-tyrosine phosphatase-
RT alpha by dimerization.";
RL Nature 382:555-559(1996).
CC -!- FUNCTION: Tyrosine protein phosphatase which is involved in integrin-
CC mediated focal adhesion formation (PubMed:22801373). Following integrin
CC engagement, specifically recruits BCAR3, BCAR1 and CRK to focal
CC adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and
CC the subsequent activation of PAK and small GTPase RAC1 and CDC42
CC (PubMed:22801373). {ECO:0000269|PubMed:22801373}.
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 -!- SUBUNIT: Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2
CC domain), and SRC (PubMed:22801373). Within the complex, interacts (when
CC phosphorylated on Tyr-825) with BCAR3 (via SH2 domain)
CC (PubMed:22801373). Interacts with GRB2 (PubMed:22801373).
CC {ECO:0000269|PubMed:22801373}.
CC -!- INTERACTION:
CC P18052; P70232: Chl1; NbExp=4; IntAct=EBI-6597520, EBI-7703109;
CC P18052; Q60631: Grb2; NbExp=4; IntAct=EBI-6597520, EBI-1688;
CC P18052; Q60673: Ptprn; NbExp=3; IntAct=EBI-6597520, EBI-8328895;
CC P18052; P05480: Src; NbExp=2; IntAct=EBI-6597520, EBI-298680;
CC P18052; P68403: Prkcb; Xeno; NbExp=3; IntAct=EBI-6597520, EBI-397072;
CC P18052; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-6597520, EBI-848039;
CC P18052; P12931: SRC; Xeno; NbExp=3; IntAct=EBI-6597520, EBI-621482;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22801373};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal
CC adhesion {ECO:0000269|PubMed:22801373}. Note=Localizes to focal
CC adhesion sites following integrin engagement.
CC {ECO:0000269|PubMed:22801373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P18052-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P18052-2; Sequence=VSP_011880, VSP_005146;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain and
CC kidney. {ECO:0000269|PubMed:1932742, ECO:0000269|PubMed:2162042,
CC ECO:0000269|PubMed:2166945}.
CC -!- PTM: Integrin binding to extracellular matrix induces phosphorylation
CC at Tyr-825 which induces PTPRA localization and recruitment of BCAR3,
CC BCAR1 and CRK to focal adhesions. {ECO:0000269|PubMed:22801373}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 4 subfamily. {ECO:0000305}.
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DR EMBL; M36033; AAA39448.1; -; mRNA.
DR EMBL; M36034; AAA39449.2; -; Genomic_DNA.
DR EMBL; L13607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28272.1; -; Genomic_DNA.
DR EMBL; Z23054; CAA80589.1; -; mRNA.
DR EMBL; Z23055; CAA80590.1; -; mRNA.
DR CCDS; CCDS16743.1; -. [P18052-1]
DR PIR; A47373; A47373.
DR RefSeq; NP_033006.2; NM_008980.2. [P18052-1]
DR PDB; 1P15; X-ray; 2.00 A; A/B=577-829.
DR PDB; 1YFO; X-ray; 2.25 A; A/B=202-539.
DR PDBsum; 1P15; -.
DR PDBsum; 1YFO; -.
DR AlphaFoldDB; P18052; -.
DR SMR; P18052; -.
DR BioGRID; 202491; 30.
DR CORUM; P18052; -.
DR IntAct; P18052; 12.
DR MINT; P18052; -.
DR STRING; 10090.ENSMUSP00000076533; -.
DR GlyConnect; 2665; 1 N-Linked glycan (1 site).
DR GlyGen; P18052; 8 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P18052; -.
DR PhosphoSitePlus; P18052; -.
DR EPD; P18052; -.
DR jPOST; P18052; -.
DR MaxQB; P18052; -.
DR PaxDb; P18052; -.
DR PeptideAtlas; P18052; -.
DR PRIDE; P18052; -.
DR ProteomicsDB; 301915; -. [P18052-1]
DR ProteomicsDB; 301916; -. [P18052-2]
DR Antibodypedia; 7130; 518 antibodies from 35 providers.
DR DNASU; 19262; -.
DR Ensembl; ENSMUST00000077303; ENSMUSP00000076533; ENSMUSG00000027303. [P18052-1]
DR GeneID; 19262; -.
DR KEGG; mmu:19262; -.
DR UCSC; uc008mjc.2; mouse. [P18052-1]
DR CTD; 5786; -.
DR MGI; MGI:97808; Ptpra.
DR VEuPathDB; HostDB:ENSMUSG00000027303; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000159585; -.
DR InParanoid; P18052; -.
DR OMA; YWPSDGT; -.
DR PhylomeDB; P18052; -.
DR TreeFam; TF351829; -.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR BioGRID-ORCS; 19262; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ptpra; mouse.
DR EvolutionaryTrace; P18052; -.
DR PRO; PR:P18052; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P18052; protein.
DR Bgee; ENSMUSG00000027303; Expressed in dentate gyrus of hippocampal formation granule cell and 259 other tissues.
DR ExpressionAtlas; P18052; baseline and differential.
DR Genevisible; P18052; MM.
DR GO; GO:0005925; C:focal adhesion; IMP:UniProtKB.
DR GO; GO:0099699; C:integral component of synaptic membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:UniProtKB.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR016336; Tyr_Pase_rcpt_a/e-type.
DR InterPro; IPR027262; Tyr_Pase_rcpt_alpha.
DR PANTHER; PTHR19134:SF433; PTHR19134:SF433; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PIRSF; PIRSF500808; PTPR_alpha; 1.
DR PIRSF; PIRSF002006; PTPR_alpha_epsilon; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Membrane;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000305"
FT CHAIN 20..829
FT /note="Receptor-type tyrosine-protein phosphatase alpha"
FT /id="PRO_0000025434"
FT TOPO_DOM 20..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 232..528
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 560..818
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 79..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 469
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 759
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 469..475
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 825
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22801373,
FT ECO:0007744|PubMed:17947660, ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 268
FT /note="F -> Y (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2162042,
FT ECO:0000303|PubMed:2166945"
FT /id="VSP_011880"
FT VAR_SEQ 269..303
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2162042,
FT ECO:0000303|PubMed:2166945"
FT /id="VSP_005146"
FT CONFLICT 231
FT /note="L -> I (in Ref. 1; AAA39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="S -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="C -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 214..238
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:1YFO"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1YFO"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 403..413
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 445..457
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:1YFO"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 497..504
FT /evidence="ECO:0007829|PDB:1YFO"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 515..530
FT /evidence="ECO:0007829|PDB:1YFO"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:1P15"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 630..633
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:1P15"
FT HELIX 641..650
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 696..706
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 712..721
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:1P15"
FT HELIX 736..746
FT /evidence="ECO:0007829|PDB:1P15"
FT TURN 747..751
FT /evidence="ECO:0007829|PDB:1P15"
FT STRAND 755..763
FT /evidence="ECO:0007829|PDB:1P15"
FT HELIX 764..782
FT /evidence="ECO:0007829|PDB:1P15"
FT HELIX 789..795
FT /evidence="ECO:0007829|PDB:1P15"
FT TURN 805..808
FT /evidence="ECO:0007829|PDB:1P15"
FT HELIX 809..817
FT /evidence="ECO:0007829|PDB:1P15"
FT TURN 818..820
FT /evidence="ECO:0007829|PDB:1P15"
SQ SEQUENCE 829 AA; 93698 MW; 4724A0F477D304B5 CRC64;
MDSWFILVLF GSGLIHVSAN NATTVSPSLG TTRLIKTSTT ELAKEENKTS NSTSSVISLS
VAPTFSPNLT LEPTYVTTVN SSHSDNGTRR AASTESGGTT ISPNGSWLIE NQFTDAITEP
WEGNSSTAAT TPETFPPADE TPIIAVMVAL SSLLVIVFII IVLYMLRFKK YKQAGSHSNS
FRLSNGRTED VEPQSVPLLA RSPSTNRKYP PLPVDKLEEE INRRMADDNK LFREEFNALP
ACPIQATCEA ASKEENKEKN RYVNILPFLS LAVSKDAVKA LNKTTPLLER RFIGKSNSRG
CLSDDHSRVH LTPVEGVPDS DYINASFING YQEKNKFIAA QGPKEETVND FWRMIWEQNT
ATIVMVTNLK ERKECKCAQY WPDQGCWTYG NVRVSVEDVT VLVDYTVRKF CIQQVGDVTN
RKPQRLITQF HFTSWPDFGV PFTPIGMLKF LKKVKACNPQ YAGAIVVHCS AGVGRTGTFV
VIDAMLDMMH SERKVDVYGF VSRIRAQRCQ MVQTDMQYVF IYQALLEHYL YGDTELEVTS
LETHLQKIYN KIPGTSNNGL EEEFKKLTSI KIQNDKMRTG NLPANMKKNR VLQIIPYEFN
RVIIPVKRGE ENTDYVNASF IDGYRQKDSY IASQGPLLHT IEDFWRMIWE WKSCSIVMLT
ELEERGQEKC AQYWPSDGLV SYGDITVELK KEEECESYTV RDLLVTNTRE NKSRQIRQFH
FHGWPEVGIP SDGKGMINII AAVQKQQQQS GNHPITVHCS AGAGRTGTFC ALSTVLERVK
AEGILDVFQT VKSLRLQRPH MVQTLEQYEF CYKVVQEYID AFSDYANFK
