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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   26-NOV-2014, entry version 179.
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. {ECO:0000255|PROSITE-ProRule:PRU10044}.
CC   -!- SUBUNIT: Interacts with GRIP1 (By similarity). Interacts with
CC       PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR. {ECO:0000250,
CC       ECO:0000269|PubMed:8995282, ECO:0000269|PubMed:9624153}.
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. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 8 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD66835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA68754.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; 20.
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; 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   GeneTree; ENSGT00760000118900; -.
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   Bgee; P10586; -.
DR   CleanEx; HS_PTPRF; -.
DR   ExpressionAtlas; P10586; baseline and differential.
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       {ECO:0000255}.
FT   CHAIN        30   1907       Receptor-type tyrosine-protein
FT                                phosphatase F.
FT                                /FTId=PRO_0000025432.
FT   TOPO_DOM     30   1263       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1264   1284       Helical. {ECO:0000255}.
FT   TOPO_DOM   1285   1907       Cytoplasmic. {ECO:0000255}.
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                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      416    510       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      514    604       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      609    706       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      711    819       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      820    914       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      918   1010       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1014   1098       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1352   1607       Tyrosine-protein phosphatase 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   DOMAIN     1639   1898       Tyrosine-protein phosphatase 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   REGION       68     77       Heparin-binding. {ECO:0000250}.
FT   REGION     1548   1554       Substrate binding. {ECO:0000250}.
FT   ACT_SITE   1548   1548       Phosphocysteine intermediate.
FT                                {ECO:0000305}.
FT   ACT_SITE   1839   1839       Phosphocysteine intermediate.
FT                                {ECO:0000250}.
FT   BINDING    1516   1516       Substrate. {ECO:0000250}.
FT   BINDING    1592   1592       Substrate. {ECO:0000250}.
FT   CARBOHYD    117    117       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    250    250       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    295    295       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    721    721       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    959    959       N-linked (GlcNAc...); atypical.
FT                                {ECO:0000269|PubMed:19349973}.
FT   CARBOHYD    966    966       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19349973}.
FT   DISULFID     54    107       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    156    207       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    253    298       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   VAR_SEQ     772    780       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:15491607}.
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                                {ECO:0000269|PubMed:10338209}.
FT   CONFLICT    646    646       Y -> H (in Ref. 1; CAA68754).
FT                                {ECO:0000305}.
FT   CONFLICT   1421   1421       I -> T (in Ref. 5; AAH48768).
FT                                {ECO:0000305}.
FT   STRAND       31     37       {ECO:0000244|PDB:2YD8}.
FT   STRAND       42     45       {ECO:0000244|PDB:2YD8}.
FT   STRAND       50     60       {ECO:0000244|PDB:2YD8}.
FT   STRAND       63     68       {ECO:0000244|PDB:2YD8}.
FT   TURN         75     77       {ECO:0000244|PDB:2YD8}.
FT   STRAND       78     83       {ECO:0000244|PDB:2YD8}.
FT   HELIX        84     86       {ECO:0000244|PDB:2YD8}.
FT   STRAND       88     93       {ECO:0000244|PDB:2YD8}.
FT   HELIX        98    101       {ECO:0000244|PDB:2YD8}.
FT   STRAND      103    111       {ECO:0000244|PDB:2YD8}.
FT   STRAND      114    125       {ECO:0000244|PDB:2YD8}.
FT   HELIX       127    129       {ECO:0000244|PDB:2YD8}.
FT   STRAND      136    139       {ECO:0000244|PDB:2YD8}.
FT   STRAND      144    147       {ECO:0000244|PDB:2YD8}.
FT   STRAND      152    154       {ECO:0000244|PDB:2YD8}.
FT   STRAND      157    159       {ECO:0000244|PDB:2YD8}.
FT   STRAND      165    170       {ECO:0000244|PDB:2YD8}.
FT   HELIX       177    179       {ECO:0000244|PDB:2YD8}.
FT   STRAND      183    186       {ECO:0000244|PDB:2YD8}.
FT   STRAND      192    194       {ECO:0000244|PDB:2YD8}.
FT   HELIX       199    201       {ECO:0000244|PDB:2YD8}.
FT   STRAND      203    211       {ECO:0000244|PDB:2YD8}.
FT   STRAND      214    217       {ECO:0000244|PDB:2YD8}.
FT   STRAND      221    226       {ECO:0000244|PDB:2YD8}.
FT   STRAND      323    331       {ECO:0000244|PDB:2DJU}.
FT   STRAND      334    340       {ECO:0000244|PDB:2DJU}.
FT   STRAND      348    356       {ECO:0000244|PDB:2DJU}.
FT   STRAND      371    378       {ECO:0000244|PDB:2DJU}.
FT   STRAND      384    392       {ECO:0000244|PDB:2DJU}.
FT   STRAND      404    407       {ECO:0000244|PDB:2DJU}.
FT   STRAND      611    619       {ECO:0000244|PDB:4N5U}.
FT   STRAND      622    628       {ECO:0000244|PDB:4N5U}.
FT   HELIX       632    634       {ECO:0000244|PDB:4N5U}.
FT   STRAND      639    652       {ECO:0000244|PDB:4N5U}.
FT   STRAND      657    663       {ECO:0000244|PDB:4N5U}.
FT   STRAND      667    671       {ECO:0000244|PDB:4N5U}.
FT   STRAND      679    690       {ECO:0000244|PDB:4N5U}.
FT   STRAND      692    695       {ECO:0000244|PDB:4N5U}.
FT   STRAND      699    702       {ECO:0000244|PDB:4N5U}.
FT   STRAND      920    923       {ECO:0000244|PDB:2EDY}.
FT   STRAND      925    927       {ECO:0000244|PDB:2EDY}.
FT   STRAND      935    937       {ECO:0000244|PDB:2EDY}.
FT   STRAND      950    957       {ECO:0000244|PDB:2EDY}.
FT   STRAND      963    971       {ECO:0000244|PDB:2EDY}.
FT   STRAND      984    987       {ECO:0000244|PDB:2EDY}.
FT   HELIX      1334   1344       {ECO:0000244|PDB:1LAR}.
FT   TURN       1347   1349       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1350   1358       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1368   1371       {ECO:0000244|PDB:1LAR}.
FT   TURN       1373   1375       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1376   1378       {ECO:0000244|PDB:1LAR}.
FT   TURN       1388   1390       {ECO:0000244|PDB:1LAR}.
FT   TURN       1401   1404       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1407   1413       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1416   1423       {ECO:0000244|PDB:1LAR}.
FT   TURN       1428   1430       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1431   1440       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1445   1448       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1452   1454       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1466   1472       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1475   1484       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1486   1497       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1503   1511       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1516   1518       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1524   1536       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1544   1553       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1554   1571       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1576   1584       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1594   1610       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1617   1619       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1620   1627       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1638   1644       {ECO:0000244|PDB:1LAR}.
FT   TURN       1645   1647       {ECO:0000244|PDB:1LAR}.
FT   TURN       1657   1660       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1662   1667       {ECO:0000244|PDB:1LAR}.
FT   TURN       1677   1679       {ECO:0000244|PDB:1LAR}.
FT   TURN       1690   1693       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1696   1700       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1703   1705       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1709   1712       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1717   1719       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1720   1729       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1734   1737       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1741   1743       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1746   1749       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1755   1757       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1759   1761       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1764   1773       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1775   1786       {ECO:0000244|PDB:1LAR}.
FT   TURN       1787   1789       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1792   1800       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1805   1807       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1813   1828       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1835   1844       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1845   1862       {ECO:0000244|PDB:1LAR}.
FT   STRAND     1863   1865       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1867   1874       {ECO:0000244|PDB:1LAR}.
FT   TURN       1875   1877       {ECO:0000244|PDB:1LAR}.
FT   HELIX      1885   1900       {ECO:0000244|PDB:1LAR}.
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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