ID PTPRG_HUMAN Reviewed; 1445 AA.
AC P23470; B2RU12; Q15623; Q59EE0; Q68DU5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 01-MAY-2013, entry version 145.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase gamma;
DE Short=Protein-tyrosine phosphatase gamma;
DE Short=R-PTP-gamma;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=PTPRG; Synonyms=PTPG;
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).
RX PubMed=8382771;
RA Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D.,
RA D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K.,
RA Musacchio J.M., Sap J., Schlessinger J.;
RT "Identification of a carbonic anhydrase-like domain in the
RT extracellular region of RPTP gamma defines a new subfamily of receptor
RT tyrosine phosphatases.";
RL Mol. Cell. Biol. 13:1497-1506(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8833149; DOI=10.1006/geno.1996.0109;
RA Kastury K., Ohta M., Lasota J., Moir D., Dorman T., Laforgia S.,
RA Druck T., Huebner K.;
RT "Structure of the human receptor tyrosine phosphatase gamma gene
RT (PTPRG) and relation to the familial RCC t(3;8) chromosome
RT translocation.";
RL Genomics 32:225-235(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-1445 (ISOFORM 2).
RC TISSUE=Prostate;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 836-1445.
RC TISSUE=Placenta;
RX PubMed=2170109;
RA Krueger N.X., Streuli M., Saito H.;
RT "Structural diversity and evolution of human receptor-like protein
RT tyrosine phosphatases.";
RL EMBO J. 9:3241-3252(1990).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 874-1118 AND 1175-1409.
RC TISSUE=Brain;
RX PubMed=2169617; DOI=10.1073/pnas.87.18.7000;
RA Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M.,
RA Ricca G., Jaye M., Schlessinger J.;
RT "Cloning of three human tyrosine phosphatases reveals a multigene
RT family of receptor-linked protein-tyrosine-phosphatases expressed in
RT brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113 AND ASN-444, AND MASS
RP SPECTROMETRY.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 827-1445, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ARG-958; LYS-960; ASP-1305 AND
RP ASP-1306.
RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT "Large-scale structural analysis of the classical human protein
RT tyrosine phosphatome.";
RL Cell 136:352-363(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 830-1127.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human receptor phosphatase PTPRG.";
RL Submitted (JUL-2006) to the PDB data bank.
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 819-1130.
RG New York structural genomix research consortium (NYSGXRC);
RT "Structural genomics of protein phosphatases.";
RL Submitted (MAR-2008) to the PDB data bank.
CC -!- FUNCTION: Possesses tyrosine phosphatase activity.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- SUBUNIT: Monomer; active form. Homodimer; inactive form
CC (Probable).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23470-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23470-2; Sequence=VSP_024353;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Found in a variety of tissues.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 5 subfamily.
CC -!- SIMILARITY: Contains 1 alpha-carbonic anhydrase domain.
CC -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93108.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPRGID41930ch3p21.html";
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DR EMBL; L09247; AAA60224.1; -; mRNA.
DR EMBL; U46116; AAC50439.1; -; Genomic_DNA.
DR EMBL; U46089; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46090; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46091; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46092; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46093; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46094; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46095; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46096; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46097; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46098; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46099; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46100; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46101; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46102; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46103; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46104; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46105; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46106; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46107; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46108; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46109; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46110; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46111; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46112; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46113; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46114; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46115; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; AB209871; BAD93108.1; ALT_INIT; mRNA.
DR EMBL; AC004695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65397.1; -; Genomic_DNA.
DR EMBL; BC140904; AAI40905.1; -; mRNA.
DR EMBL; CR749269; CAH18125.1; -; mRNA.
DR EMBL; X54132; CAA38067.1; -; mRNA.
DR IPI; IPI00011651; -.
DR IPI; IPI00796281; -.
DR PIR; A48148; A48148.
DR RefSeq; NP_002832.3; NM_002841.3.
DR UniGene; Hs.595541; -.
DR PDB; 2H4V; X-ray; 1.55 A; A/B=831-1127.
DR PDB; 2HY3; X-ray; 2.60 A; A/B=820-1130.
DR PDB; 2NLK; X-ray; 2.40 A; A=827-1445.
DR PDB; 2PBN; X-ray; 1.70 A; A=820-1130.
DR PDB; 3JXH; X-ray; 1.70 A; C=56-320.
DR PDB; 3QCB; X-ray; 2.10 A; A/B=825-1128.
DR PDB; 3QCC; X-ray; 2.10 A; A/B=825-1128.
DR PDB; 3QCD; X-ray; 1.80 A; A=825-1128.
DR PDB; 3QCE; X-ray; 2.10 A; A/B=825-1128.
DR PDB; 3QCF; X-ray; 2.50 A; A/B=825-1128.
DR PDB; 3QCG; X-ray; 2.05 A; A=825-1128.
DR PDB; 3QCH; X-ray; 2.40 A; A=825-1128.
DR PDB; 3QCI; X-ray; 2.27 A; A=825-1128.
DR PDB; 3QCJ; X-ray; 2.26 A; A=825-1128.
DR PDB; 3QCK; X-ray; 2.05 A; A=825-1128.
DR PDB; 3QCL; X-ray; 2.40 A; A=825-1128.
DR PDB; 3QCM; X-ray; 2.40 A; A/B=825-1128.
DR PDB; 3QCN; X-ray; 2.41 A; A=825-1128.
DR PDBsum; 2H4V; -.
DR PDBsum; 2HY3; -.
DR PDBsum; 2NLK; -.
DR PDBsum; 2PBN; -.
DR PDBsum; 3JXH; -.
DR PDBsum; 3QCB; -.
DR PDBsum; 3QCC; -.
DR PDBsum; 3QCD; -.
DR PDBsum; 3QCE; -.
DR PDBsum; 3QCF; -.
DR PDBsum; 3QCG; -.
DR PDBsum; 3QCH; -.
DR PDBsum; 3QCI; -.
DR PDBsum; 3QCJ; -.
DR PDBsum; 3QCK; -.
DR PDBsum; 3QCL; -.
DR PDBsum; 3QCM; -.
DR PDBsum; 3QCN; -.
DR ProteinModelPortal; P23470; -.
DR IntAct; P23470; 22.
DR MINT; MINT-1349880; -.
DR STRING; 9606.ENSP00000418112; -.
DR PhosphoSite; P23470; -.
DR DMDM; 229463033; -.
DR PaxDb; P23470; -.
DR PRIDE; P23470; -.
DR DNASU; 5793; -.
DR Ensembl; ENST00000295874; ENSP00000295874; ENSG00000144724.
DR Ensembl; ENST00000474889; ENSP00000418112; ENSG00000144724.
DR GeneID; 5793; -.
DR KEGG; hsa:5793; -.
DR UCSC; uc003dlb.3; human.
DR UCSC; uc003dlc.3; human.
DR CTD; 5793; -.
DR GeneCards; GC03P061522; -.
DR H-InvDB; HIX0024329; -.
DR HGNC; HGNC:9671; PTPRG.
DR MIM; 176886; gene.
DR neXtProt; NX_P23470; -.
DR PharmGKB; PA34016; -.
DR eggNOG; COG5599; -.
DR HOGENOM; HOG000060222; -.
DR HOVERGEN; HBG053760; -.
DR KO; K01104; -.
DR OMA; WRGCNKI; -.
DR OrthoDB; EOG4FN4GW; -.
DR PhylomeDB; P23470; -.
DR BindingDB; P23470; -.
DR ChEMBL; CHEMBL4905; -.
DR ChiTaRS; PTPRG; human.
DR EvolutionaryTrace; P23470; -.
DR GenomeRNAi; 5793; -.
DR NextBio; 22556; -.
DR ArrayExpress; P23470; -.
DR Bgee; P23470; -.
DR CleanEx; HS_PTPRG; -.
DR Genevestigator; P23470; -.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR001148; Carbonic_anhydrase_a.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00194; PTPc; 2.
DR SUPFAM; SSF51069; Euk_COanhd; 1.
DR SUPFAM; SSF49265; FN_III-like; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
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; Complete proteome; Glycoprotein;
KW Hydrolase; Membrane; Phosphoprotein; Polymorphism;
KW Protein phosphatase; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 19
FT CHAIN 20 1445 Receptor-type tyrosine-protein
FT phosphatase gamma.
FT /FTId=PRO_0000025441.
FT TOPO_DOM 20 736 Extracellular (Potential).
FT TRANSMEM 737 762 Helical; (Potential).
FT TOPO_DOM 763 1445 Cytoplasmic (Potential).
FT DOMAIN 58 321 Alpha-carbonic anhydrase.
FT DOMAIN 346 443 Fibronectin type-III.
FT DOMAIN 848 1119 Tyrosine-protein phosphatase 1.
FT DOMAIN 1150 1410 Tyrosine-protein phosphatase 2.
FT REGION 1060 1066 Substrate binding (By similarity).
FT ACT_SITE 1060 1060 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 1028 1028 Substrate (By similarity).
FT BINDING 1104 1104 Substrate (By similarity).
FT SITE 1351 1351 Ancestral active site.
FT MOD_RES 115 115 Phosphothreonine (By similarity).
FT MOD_RES 1182 1182 Phosphoserine.
FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 113 113 N-linked (GlcNAc...).
FT CARBOHYD 156 156 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 359 359 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 444 444 N-linked (GlcNAc...).
FT CARBOHYD 619 619 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 631 631 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 722 722 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 764 792 Missing (in isoform 2).
FT /FTId=VSP_024353.
FT VARIANT 574 574 G -> S (in dbSNP:rs2292245).
FT /FTId=VAR_020301.
FT VARIANT 639 639 Q -> R (in dbSNP:rs9870460).
FT /FTId=VAR_031562.
FT MUTAGEN 958 958 R->E: Loss of dimerization; when
FT associated with E-960.
FT MUTAGEN 960 960 K->E: Loss of dimerization; when
FT associated with E-958.
FT MUTAGEN 1305 1305 D->K: Loss of dimerization; when
FT associated with K-1306.
FT MUTAGEN 1306 1306 D->K: Loss of dimerization; when
FT associated with K-1305.
FT CONFLICT 80 80 G -> S (in Ref. 1; AAA60224).
FT CONFLICT 92 92 Y -> H (in Ref. 2; AAC50439).
FT CONFLICT 549 549 A -> V (in Ref. 2; AAC50439).
FT CONFLICT 756 756 I -> T (in Ref. 2; AAC50439).
FT CONFLICT 805 805 S -> R (in Ref. 7; CAH18125).
FT CONFLICT 1316 1316 C -> Y (in Ref. 7; CAH18125).
FT CONFLICT 1407 1407 M -> R (in Ref. 1; AAA60224 and 2;
FT AAC50439).
FT HELIX 64 66
FT HELIX 68 70
FT HELIX 71 74
FT HELIX 76 79
FT HELIX 90 92
FT STRAND 103 106
FT STRAND 116 119
FT STRAND 124 127
FT STRAND 133 135
FT STRAND 143 152
FT STRAND 162 165
FT STRAND 171 179
FT TURN 181 183
FT HELIX 187 192
FT STRAND 197 209
FT HELIX 212 214
FT HELIX 215 223
FT STRAND 230 232
FT HELIX 238 241
FT STRAND 249 254
FT STRAND 265 272
FT STRAND 274 277
FT HELIX 278 285
FT STRAND 288 290
FT STRAND 299 301
FT HELIX 831 861
FT TURN 867 870
FT HELIX 872 877
FT HELIX 887 889
FT STRAND 890 892
FT TURN 899 901
FT HELIX 902 905
FT STRAND 906 912
FT STRAND 915 917
FT STRAND 921 924
FT HELIX 929 931
FT HELIX 932 942
FT STRAND 946 949
FT STRAND 953 955
FT STRAND 967 973
FT STRAND 976 985
FT STRAND 987 998
FT STRAND 1016 1023
FT STRAND 1028 1031
FT HELIX 1036 1047
FT STRAND 1056 1064
FT HELIX 1065 1082
FT STRAND 1084 1086
FT HELIX 1088 1095
FT TURN 1096 1098
FT HELIX 1106 1121
FT HELIX 1129 1131
FT HELIX 1132 1139
FT HELIX 1149 1157
FT STRAND 1172 1174
FT STRAND 1207 1211
FT STRAND 1219 1224
FT HELIX 1228 1230
FT HELIX 1231 1241
FT STRAND 1245 1248
FT STRAND 1270 1272
FT STRAND 1275 1286
FT STRAND 1292 1305
FT STRAND 1308 1315
FT STRAND 1318 1320
FT HELIX 1326 1328
FT HELIX 1329 1340
FT STRAND 1347 1354
FT HELIX 1356 1374
FT STRAND 1375 1377
FT HELIX 1379 1389
FT HELIX 1397 1408
SQ SEQUENCE 1445 AA; 162003 MW; A48A007BA14082BC CRC64;
MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGALHE NRHGSAVQIR RRKASGDPYW
AYSGAYGPEH WVTSSVSCGG RHQSPIDILD QYARVGEEYQ ELQLDGFDNE SSNKTWMKNT
GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSINGRRF PVEMQIFFYN
PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD
LLPASLGSYY RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE
YLRNNFRPQQ RLHDRVVSKS AVRDSWNHDM TDFLENPLGT EASKVCSSPP IHMKVQPLNQ
TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SHVSPDSLYL
FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW
TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT
AASASKQAAR PVLATTEALA SPGPDGDSSP TKDGEGTEEG EKDEKSESED GEREHEEDGE
KDSEKKEKSG VTHAAEERNQ TEPSPTPSSP NRTAEGGHQT IPGHEQDHTA VPTDQTGGRR
DAGPGLDPDM VTSTQVPPTA TEEQYAGSDP KRPEMPSKKP MSRGDRFSED SRFITVNPAE
KNTSGMISRP APGRMEWIIP LIVVSALTFV CLILLIAVLV YWRGCNKIKS KGFPRRFREV
PSSGERGEKG SRKCFQTAHF YVEDSSSPRV VPNESIPIIP IPDDMEAIPV KQFVKHIGEL
YSNNQHGFSE DFEEVQRCTA DMNITAEHSN HPENKHKNRY INILAYDHSR VKLRPLPGKD
SKHSDYINAN YVDGYNKAKA YIATQGPLKS TFEDFWRMIW EQNTGIIVMI TNLVEKGRRK
CDQYWPTENS EEYGNIIVTL KSTKIHACYT VRRFSIRNTK VKKGQKGNPK GRQNERVVIQ
YHYTQWPDMG VPEYALPVLT FVRRSSAARM PETGPVLVHC SAGVGRTGTY IVIDSMLQQI
KDKSTVNVLG FLKHIRTQRN YLVQTEEQYI FIHDALLEAI LGKETEVSSN QLHSYVNSIL
IPGVGGKTRL EKQFKLVTQC NAKYVECFSA QKECNKEKNR NSSVVPSERA RVGLAPLPGM
KGTDYINASY IMGYYRSNEF IITQHPLPHT TKDFWRMIWD HNAQIIVMLP DNQSLAEDEF
VYWPSREESM NCEAFTVTLI SKDRLCLSNE EQIIIHDFIL EATQDDYVLE VRHFQCPKWP
NPDAPISSTF ELINVIKEEA LTRDGPTIVH DEYGAVSAGM LCALTTLSQQ LENENAVDVF
QVAKMINLMR PGVFTDIEQY QFIYKAMLSL VSTKENGNGP MTVDKNGAVL IADESDPAES
MESLV
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