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Database: UniProt
Entry: P10586
LinkDB: P10586
Original site: P10586 
ID   PTPRF_HUMAN             Reviewed;        1907 AA.
AC   P10586; D3DPX6; D3DPX7; Q5T021; Q5T022; Q5W9G2; Q86WS0;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   03-SEP-2014, entry version 176.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase F;
DE            EC=3.1.3.48;
DE   AltName: Full=Leukocyte common antigen related;
DE            Short=LAR;
DE   Flags: Precursor;
GN   Name=PTPRF; Synonyms=LAR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Tonsil;
RX   PubMed=2972792; DOI=10.1084/jem.168.5.1523;
RA   Streuli M., Krueger N.X., Hall L.R., Schlossman S.F., Saito H.;
RT   "A new member of the immunoglobulin superfamily that has a cytoplasmic
RT   region homologous to the leukocyte common antigen.";
RL   J. Exp. Med. 168:1523-1530(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
RA   Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
RT   "Alternative splice variants encoding unstable protein domains exist
RT   in the human brain.";
RL   J. Mol. Biol. 343:1207-1220(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Retinoblastoma;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=2554325; DOI=10.1073/pnas.86.22.8698;
RA   Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.;
RT   "A family of receptor-linked protein tyrosine phosphatases in humans
RT   and Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989).
RN   [7]
RP   MUTAGENESIS.
RX   PubMed=1695146;
RA   Streuli M., Krueger N.X., Thai T., Tang M., Saito H.;
RT   "Distinct functional roles of the two intracellular phosphatase like
RT   domains of the receptor-linked protein tyrosine phosphatases LCA and
RT   LAR.";
RL   EMBO J. 9:2399-2407(1990).
RN   [8]
RP   INTERACTION WITH INSR.
RX   PubMed=8995282; DOI=10.1074/jbc.272.11.7519;
RA   Ahmad F., Goldstein B.J.;
RT   "Functional association between the insulin receptor and the
RT   transmembrane protein-tyrosine phosphatase LAR in intact cells.";
RL   J. Biol. Chem. 272:448-457(1997).
RN   [9]
RP   INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
RX   PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA   Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT   "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT   interacting proteins.";
RL   J. Biol. Chem. 273:15611-15620(1998).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-966.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-959 AND ASN-966.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   FUNCTION IN EPHA2 DEPHOSPHORYLATION.
RX   PubMed=23358419; DOI=10.1128/MCB.01708-12;
RA   Lee H., Bennett A.M.;
RT   "Receptor protein tyrosine phosphatase-receptor tyrosine kinase
RT   substrate screen identifies EphA2 as a target for LAR in cell
RT   migration.";
RL   Mol. Cell. Biol. 33:1430-1441(2013).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1334-1897, FUNCTION, AND
RP   MUTAGENESIS OF CYS-1548.
RX   PubMed=10338209; DOI=10.1016/S0092-8674(00)80755-2;
RA   Nam H.J., Poy F., Krueger N.X., Saito H., Frederick C.A.;
RT   "Crystal structure of the tandem phosphatase domains of RPTP LAR.";
RL   Cell 97:449-457(1999).
RN   [15]
RP   STRUCTURE BY NMR OF 319-415 AND 596-1010.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structures of FN3 domains of human receptor-type tyrosine-
RT   protein phosphatase F.";
RL   Submitted (AUG-2007) to the PDB data bank.
CC   -!- FUNCTION: Possible cell adhesion receptor. It possesses an
CC       intrinsic protein tyrosine phosphatase activity (PTPase) and
CC       dephosphorylates EPHA2 regulating its activity.
CC   -!- FUNCTION: The first PTPase domain has enzymatic activity, while
CC       the second one seems to affect the substrate specificity of the
CC       first one.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with GRIP1 (By similarity). Interacts with
CC       PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P10586-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P10586-2; Sequence=VSP_036617;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily.
CC   -!- SIMILARITY: Contains 8 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD66835.1; Type=Erroneous initiation;
CC       Sequence=CAA68754.1; Type=Erroneous initiation;
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DR   EMBL; Y00815; CAA68754.1; ALT_INIT; mRNA.
DR   EMBL; AB177857; BAD66835.1; ALT_INIT; mRNA.
DR   EMBL; AL583862; CAI14894.1; -; Genomic_DNA.
DR   EMBL; AC092815; CAI14894.1; JOINED; Genomic_DNA.
DR   EMBL; AL583862; CAI14895.1; -; Genomic_DNA.
DR   EMBL; AC092815; CAI14895.1; JOINED; Genomic_DNA.
DR   EMBL; CH471059; EAX07086.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07087.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07088.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07089.1; -; Genomic_DNA.
DR   EMBL; BC048768; AAH48768.1; -; mRNA.
DR   CCDS; CCDS489.2; -. [P10586-1]
DR   CCDS; CCDS490.2; -. [P10586-2]
DR   PIR; S03841; TDHULK.
DR   RefSeq; NP_002831.2; NM_002840.3. [P10586-1]
DR   RefSeq; NP_569707.2; NM_130440.2. [P10586-2]
DR   UniGene; Hs.272062; -.
DR   PDB; 1LAR; X-ray; 2.00 A; A/B=1333-1907.
DR   PDB; 2DJU; NMR; -; A=319-411.
DR   PDB; 2DN7; NMR; -; A=821-914.
DR   PDB; 2EDX; NMR; -; A=596-716.
DR   PDB; 2EDY; NMR; -; A=915-1010.
DR   PDB; 2YD5; X-ray; 2.20 A; A=29-231.
DR   PDB; 2YD8; X-ray; 2.05 A; A=29-231.
DR   PDB; 4N5U; X-ray; 1.46 A; A=601-705.
DR   PDBsum; 1LAR; -.
DR   PDBsum; 2DJU; -.
DR   PDBsum; 2DN7; -.
DR   PDBsum; 2EDX; -.
DR   PDBsum; 2EDY; -.
DR   PDBsum; 2YD5; -.
DR   PDBsum; 2YD8; -.
DR   PDBsum; 4N5U; -.
DR   ProteinModelPortal; P10586; -.
DR   SMR; P10586; 30-1010, 1334-1902.
DR   BioGrid; 111756; 15.
DR   IntAct; P10586; 6.
DR   MINT; MINT-1189049; -.
DR   STRING; 9606.ENSP00000353030; -.
DR   BindingDB; P10586; -.
DR   ChEMBL; CHEMBL3521; -.
DR   PhosphoSite; P10586; -.
DR   DMDM; 226709091; -.
DR   MaxQB; P10586; -.
DR   PaxDb; P10586; -.
DR   PRIDE; P10586; -.
DR   DNASU; 5792; -.
DR   Ensembl; ENST00000359947; ENSP00000353030; ENSG00000142949. [P10586-1]
DR   Ensembl; ENST00000372413; ENSP00000361490; ENSG00000142949. [P10586-2]
DR   Ensembl; ENST00000372414; ENSP00000361491; ENSG00000142949. [P10586-1]
DR   Ensembl; ENST00000438120; ENSP00000398822; ENSG00000142949. [P10586-2]
DR   GeneID; 5792; -.
DR   KEGG; hsa:5792; -.
DR   UCSC; uc001cjr.3; human. [P10586-1]
DR   UCSC; uc001cjs.3; human. [P10586-2]
DR   CTD; 5792; -.
DR   GeneCards; GC01P043990; -.
DR   HGNC; HGNC:9670; PTPRF.
DR   HPA; HPA012710; -.
DR   MIM; 179590; gene.
DR   neXtProt; NX_P10586; -.
DR   PharmGKB; PA34015; -.
DR   eggNOG; COG5599; -.
DR   HOVERGEN; HBG053758; -.
DR   InParanoid; P10586; -.
DR   KO; K05695; -.
DR   OMA; VFTPTIE; -.
DR   PhylomeDB; P10586; -.
DR   TreeFam; TF312900; -.
DR   SignaLink; P10586; -.
DR   ChiTaRS; PTPRF; human.
DR   EvolutionaryTrace; P10586; -.
DR   GeneWiki; PTPRF; -.
DR   GenomeRNAi; 5792; -.
DR   NextBio; 22550; -.
DR   PMAP-CutDB; Q5T022; -.
DR   PRO; PR:P10586; -.
DR   ArrayExpress; P10586; -.
DR   Bgee; P10586; -.
DR   CleanEx; HS_PTPRF; -.
DR   Genevestigator; P10586; -.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:1900121; P:negative regulation of receptor binding; IMP:UniProtKB.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR   GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:ProtInc.
DR   Gene3D; 2.60.40.10; -; 10.
DR   Gene3D; 3.90.190.10; -; 2.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49265; SSF49265; 5.
DR   SUPFAM; SSF52799; SSF52799; 2.
DR   PROSITE; PS50853; FN3; 8.
DR   PROSITE; PS50835; IG_LIKE; 3.
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 adhesion; Complete proteome;
KW   Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase;
KW   Immunoglobulin domain; Membrane; Polymorphism; Protein phosphatase;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30   1907       Receptor-type tyrosine-protein
FT                                phosphatase F.
FT                                /FTId=PRO_0000025432.
FT   TOPO_DOM     30   1263       Extracellular (Potential).
FT   TRANSMEM   1264   1284       Helical; (Potential).
FT   TOPO_DOM   1285   1907       Cytoplasmic (Potential).
FT   DOMAIN       33    123       Ig-like C2-type 1.
FT   DOMAIN      135    224       Ig-like C2-type 2.
FT   DOMAIN      232    314       Ig-like C2-type 3.
FT   DOMAIN      321    411       Fibronectin type-III 1.
FT   DOMAIN      416    510       Fibronectin type-III 2.
FT   DOMAIN      514    604       Fibronectin type-III 3.
FT   DOMAIN      609    706       Fibronectin type-III 4.
FT   DOMAIN      711    819       Fibronectin type-III 5.
FT   DOMAIN      820    914       Fibronectin type-III 6.
FT   DOMAIN      918   1010       Fibronectin type-III 7.
FT   DOMAIN     1014   1098       Fibronectin type-III 8.
FT   DOMAIN     1352   1607       Tyrosine-protein phosphatase 1.
FT   DOMAIN     1639   1898       Tyrosine-protein phosphatase 2.
FT   REGION       68     77       Heparin-binding (By similarity).
FT   REGION     1548   1554       Substrate binding (By similarity).
FT   ACT_SITE   1548   1548       Phosphocysteine intermediate (Probable).
FT   ACT_SITE   1839   1839       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1516   1516       Substrate (By similarity).
FT   BINDING    1592   1592       Substrate (By similarity).
FT   CARBOHYD    117    117       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    250    250       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    295    295       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    721    721       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    959    959       N-linked (GlcNAc...); atypical.
FT   CARBOHYD    966    966       N-linked (GlcNAc...).
FT   DISULFID     54    107       By similarity.
FT   DISULFID    156    207       By similarity.
FT   DISULFID    253    298       By similarity.
FT   VAR_SEQ     772    780       Missing (in isoform 2).
FT                                /FTId=VSP_036617.
FT   VARIANT     412    412       A -> V (in dbSNP:rs1065775).
FT                                /FTId=VAR_054766.
FT   VARIANT     450    450       Y -> C (in dbSNP:rs3748796).
FT                                /FTId=VAR_020299.
FT   VARIANT     562    562       D -> N (in dbSNP:rs3748800).
FT                                /FTId=VAR_020300.
FT   MUTAGEN    1548   1548       C->S: Loss of activity.
FT   CONFLICT    646    646       Y -> H (in Ref. 1; CAA68754).
FT   CONFLICT   1421   1421       I -> T (in Ref. 5; AAH48768).
FT   STRAND       31     37
FT   STRAND       42     45
FT   STRAND       50     60
FT   STRAND       63     68
FT   TURN         75     77
FT   STRAND       78     83
FT   HELIX        84     86
FT   STRAND       88     93
FT   HELIX        98    101
FT   STRAND      103    111
FT   STRAND      114    125
FT   HELIX       127    129
FT   STRAND      136    139
FT   STRAND      144    147
FT   STRAND      152    154
FT   STRAND      157    159
FT   STRAND      165    170
FT   HELIX       177    179
FT   STRAND      183    186
FT   STRAND      192    194
FT   HELIX       199    201
FT   STRAND      203    211
FT   STRAND      214    217
FT   STRAND      221    226
FT   STRAND      323    331
FT   STRAND      334    340
FT   STRAND      348    356
FT   STRAND      371    378
FT   STRAND      384    392
FT   STRAND      404    407
FT   STRAND      611    619
FT   STRAND      622    628
FT   HELIX       632    634
FT   STRAND      639    652
FT   STRAND      657    663
FT   STRAND      667    671
FT   STRAND      679    690
FT   STRAND      692    695
FT   STRAND      699    702
FT   STRAND      920    923
FT   STRAND      925    927
FT   STRAND      935    937
FT   STRAND      950    957
FT   STRAND      963    971
FT   STRAND      984    987
FT   HELIX      1334   1344
FT   TURN       1347   1349
FT   HELIX      1350   1358
FT   HELIX      1368   1371
FT   TURN       1373   1375
FT   HELIX      1376   1378
FT   TURN       1388   1390
FT   TURN       1401   1404
FT   STRAND     1407   1413
FT   STRAND     1416   1423
FT   TURN       1428   1430
FT   HELIX      1431   1440
FT   STRAND     1445   1448
FT   STRAND     1452   1454
FT   STRAND     1466   1472
FT   STRAND     1475   1484
FT   STRAND     1486   1497
FT   STRAND     1503   1511
FT   STRAND     1516   1518
FT   HELIX      1524   1536
FT   STRAND     1544   1553
FT   HELIX      1554   1571
FT   HELIX      1576   1584
FT   HELIX      1594   1610
FT   HELIX      1617   1619
FT   HELIX      1620   1627
FT   HELIX      1638   1644
FT   TURN       1645   1647
FT   TURN       1657   1660
FT   HELIX      1662   1667
FT   TURN       1677   1679
FT   TURN       1690   1693
FT   STRAND     1696   1700
FT   STRAND     1703   1705
FT   STRAND     1709   1712
FT   HELIX      1717   1719
FT   HELIX      1720   1729
FT   STRAND     1734   1737
FT   STRAND     1741   1743
FT   STRAND     1746   1749
FT   STRAND     1755   1757
FT   STRAND     1759   1761
FT   STRAND     1764   1773
FT   STRAND     1775   1786
FT   TURN       1787   1789
FT   STRAND     1792   1800
FT   STRAND     1805   1807
FT   HELIX      1813   1828
FT   STRAND     1835   1844
FT   HELIX      1845   1862
FT   STRAND     1863   1865
FT   HELIX      1867   1874
FT   TURN       1875   1877
FT   HELIX      1885   1900
SQ   SEQUENCE   1907 AA;  212879 MW;  4A7C14A2090EA88F CRC64;
     MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP
     KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
     KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS
     NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
     QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA
     ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE
     GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
     QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP
     GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI
     IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR
     TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD
     GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
     NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QWRPEESEDY
     ETTISGLTPE TTYSVTVAAY TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW
     HPPKELPGEL LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL
     GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS YTVVFRDINS
     QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS PSIQSRTMPV EQVFAKNFRV
     AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR
     GSSAGGLQHL VSIRTAPDLL PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID
     RVGGSMLTPR WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL
     GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE
     MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN
     YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NLEVNKPKNR
     YANVIAYDHS RVILTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE
     QRTATVVMMT RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS
     SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV
     IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAATC GHTEVPARNL
     YAHIQKLGQV PPGESVTAME LEFKLLASSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR
     VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK
     LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF
     TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR
     YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT
//
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