PTN5_HUMAN
ID PTN5_HUMAN Reviewed; 565 AA.
AC P54829; B3KXG7; B7Z386; B7ZAF5; D3DQY7; Q6P1Z2; Q8N2A1; Q8NDP8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 5;
DE EC=3.1.3.48;
DE AltName: Full=Neural-specific protein-tyrosine phosphatase;
DE AltName: Full=Striatum-enriched protein-tyrosine phosphatase;
DE Short=STEP;
GN Name=PTPN5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP ALA-170.
RC TISSUE=Amygdala, Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-170.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-565 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7490079; DOI=10.1006/geno.1995.1173;
RA Li X., Luna J., Lombroso P.J., Francke U.;
RT "Molecular cloning of the human homolog of a striatum-enriched phosphatase
RT (STEP) gene and chromosomal mapping of the human and murine loci.";
RL Genomics 28:442-449(1995).
RN [7]
RP PHOSPHORYLATION AT SER-245; THR-255 AND SER-268, AND FUNCTION.
RX PubMed=21777200; DOI=10.1042/bj20110240;
RA Mukherjee S., Poddar R., Deb I., Paul S.;
RT "Dephosphorylation of specific sites in the kinase-specificity sequence
RT domain leads to ubiquitin-mediated degradation of the tyrosine phosphatase
RT STEP.";
RL Biochem. J. 440:115-125(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 280-563 IN COMPLEX WITH SUBSTRATE
RP ANALOG.
RX PubMed=16441242; DOI=10.1042/bj20051931;
RA Eswaran J., von Kries J.P., Marsden B., Longman E., Debreczeni J.E.,
RA Ugochukwu E., Turnbull A., Lee W.H., Knapp S., Barr A.J.;
RT "Crystal structures and inhibitor identification for PTPN5, PTPRR and
RT PTPN7: a family of human MAPK-specific protein tyrosine phosphatases.";
RL Biochem. J. 395:483-491(2006).
CC -!- FUNCTION: May regulate the activity of several effector molecules
CC involved in synaptic plasticity and neuronal cell survival, including
CC MAPKs, Src family kinases and NMDA receptors.
CC {ECO:0000269|PubMed:21777200}.
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 -!- INTERACTION:
CC P54829; Q6UXB4: CLEC4G; NbExp=3; IntAct=EBI-1220572, EBI-2114729;
CC P54829; Q07325: CXCL9; NbExp=3; IntAct=EBI-1220572, EBI-3911467;
CC P54829; O14569: CYB561D2; NbExp=3; IntAct=EBI-1220572, EBI-717654;
CC P54829; O75355-2: ENTPD3; NbExp=3; IntAct=EBI-1220572, EBI-12279764;
CC P54829; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-1220572, EBI-2341610;
CC P54829; P78383: SLC35B1; NbExp=3; IntAct=EBI-1220572, EBI-12147661;
CC P54829; P54274: TERF1; NbExp=2; IntAct=EBI-1220572, EBI-710997;
CC P54829; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-1220572, EBI-11994282;
CC P54829; Q9BSA0: TMEM51; NbExp=3; IntAct=EBI-1220572, EBI-10297449;
CC P54829; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-1220572, EBI-726044;
CC P54829; Q9UEU0: VTI1B; NbExp=4; IntAct=EBI-1220572, EBI-723716;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=STEP61;
CC IsoId=P54829-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54829-2; Sequence=VSP_042654;
CC Name=3;
CC IsoId=P54829-3; Sequence=VSP_054561;
CC -!- PTM: Phosphorylation at Ser-245 by PKA deactivates PTPN5.
CC Phosphorylation at Thr-255 and Ser-268 by MAPKs stabilizes the
CC phosphatase, dephosphorylation of these sites results in ubiquitin-
CC mediated degradation of the active phosphatase.
CC {ECO:0000269|PubMed:21777200}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AK090923; BAC03548.1; -; mRNA.
DR EMBL; AK127312; BAG54479.1; -; mRNA.
DR EMBL; AK295604; BAH12122.1; -; mRNA.
DR EMBL; AK316270; BAH14641.1; -; mRNA.
DR EMBL; AL832541; CAD38632.2; -; mRNA.
DR EMBL; AC103974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68363.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68365.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68367.1; -; Genomic_DNA.
DR EMBL; BC064807; AAH64807.1; -; mRNA.
DR EMBL; U27831; AAA87555.1; -; mRNA.
DR CCDS; CCDS41626.1; -. [P54829-2]
DR CCDS; CCDS60746.1; -. [P54829-3]
DR CCDS; CCDS7845.1; -. [P54829-1]
DR RefSeq; NP_001035059.1; NM_001039970.1. [P54829-2]
DR RefSeq; NP_001265165.1; NM_001278236.1. [P54829-2]
DR RefSeq; NP_001265167.1; NM_001278238.1. [P54829-3]
DR RefSeq; NP_001265168.1; NM_001278239.1.
DR RefSeq; NP_008837.1; NM_006906.1. [P54829-1]
DR RefSeq; NP_116170.3; NM_032781.3. [P54829-1]
DR PDB; 2BIJ; X-ray; 2.05 A; A=282-563.
DR PDB; 2BV5; X-ray; 1.80 A; A=280-561.
DR PDB; 2CJZ; X-ray; 1.70 A; A=282-563.
DR PDB; 5OVR; X-ray; 2.15 A; A=282-561.
DR PDB; 5OVX; X-ray; 2.10 A; A=282-563.
DR PDB; 5OW1; X-ray; 2.05 A; A=282-563.
DR PDB; 6H8R; X-ray; 1.66 A; A=282-563.
DR PDBsum; 2BIJ; -.
DR PDBsum; 2BV5; -.
DR PDBsum; 2CJZ; -.
DR PDBsum; 5OVR; -.
DR PDBsum; 5OVX; -.
DR PDBsum; 5OW1; -.
DR PDBsum; 6H8R; -.
DR AlphaFoldDB; P54829; -.
DR SMR; P54829; -.
DR BioGRID; 124312; 80.
DR ELM; P54829; -.
DR IntAct; P54829; 39.
DR MINT; P54829; -.
DR STRING; 9606.ENSP00000351342; -.
DR BindingDB; P54829; -.
DR ChEMBL; CHEMBL2007628; -.
DR DEPOD; PTPN5; -.
DR iPTMnet; P54829; -.
DR PhosphoSitePlus; P54829; -.
DR BioMuta; PTPN5; -.
DR DMDM; 317373540; -.
DR MassIVE; P54829; -.
DR PaxDb; P54829; -.
DR PeptideAtlas; P54829; -.
DR PRIDE; P54829; -.
DR ProteomicsDB; 56735; -. [P54829-1]
DR ProteomicsDB; 56736; -. [P54829-2]
DR ProteomicsDB; 7064; -.
DR Antibodypedia; 25176; 303 antibodies from 29 providers.
DR DNASU; 84867; -.
DR Ensembl; ENST00000358540.7; ENSP00000351342.2; ENSG00000110786.18. [P54829-1]
DR Ensembl; ENST00000396168.1; ENSP00000379471.1; ENSG00000110786.18. [P54829-3]
DR Ensembl; ENST00000396170.5; ENSP00000379473.1; ENSG00000110786.18. [P54829-2]
DR GeneID; 84867; -.
DR KEGG; hsa:84867; -.
DR MANE-Select; ENST00000358540.7; ENSP00000351342.2; NM_006906.2; NP_008837.1.
DR UCSC; uc001mpd.5; human. [P54829-1]
DR CTD; 84867; -.
DR DisGeNET; 84867; -.
DR GeneCards; PTPN5; -.
DR HGNC; HGNC:9657; PTPN5.
DR HPA; ENSG00000110786; Tissue enriched (brain).
DR MIM; 176879; gene.
DR neXtProt; NX_P54829; -.
DR OpenTargets; ENSG00000110786; -.
DR PharmGKB; PA34001; -.
DR VEuPathDB; HostDB:ENSG00000110786; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000159916; -.
DR HOGENOM; CLU_001645_10_2_1; -.
DR InParanoid; P54829; -.
DR OMA; GWPQGYG; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P54829; -.
DR TreeFam; TF331016; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P54829; -.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR SignaLink; P54829; -.
DR SIGNOR; P54829; -.
DR BioGRID-ORCS; 84867; 11 hits in 1069 CRISPR screens.
DR EvolutionaryTrace; P54829; -.
DR GeneWiki; PTPN5; -.
DR GenomeRNAi; 84867; -.
DR Pharos; P54829; Tchem.
DR PRO; PR:P54829; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P54829; protein.
DR Bgee; ENSG00000110786; Expressed in endothelial cell and 113 other tissues.
DR ExpressionAtlas; P54829; baseline and differential.
DR Genevisible; P54829; HS.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
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; IPR008356; Tyr_Pase_KIM-con.
DR InterPro; IPR016334; Tyr_Pase_rcpt_R/non-rcpt_5.
DR PANTHER; PTHR46198; PTHR46198; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF001997; PTPRR; 1.
DR PRINTS; PR01778; KIMPTPASE.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
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; Endoplasmic reticulum; Hydrolase;
KW Membrane; Phosphoprotein; Protein phosphatase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..565
FT /note="Tyrosine-protein phosphatase non-receptor type 5"
FT /id="PRO_0000363657"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 300..555
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 496
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 496..502
FT /ligand="substrate"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 245
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:21777200"
FT MOD_RES 255
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000269|PubMed:21777200"
FT MOD_RES 268
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:21777200"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054561"
FT VAR_SEQ 98..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042654"
FT VARIANT 170
FT /note="P -> A (in dbSNP:rs4757707)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_054369"
FT VARIANT 561
FT /note="H -> R (in dbSNP:rs11024773)"
FT /id="VAR_054370"
FT CONFLICT 32..34
FT /note="PGL -> LGR (in Ref. 6; AAA87555)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="W -> R (in Ref. 1; BAC03548)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="G -> A (in Ref. 2; CAD38632)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="H -> D (in Ref. 2; CAD38632)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="I -> M (in Ref. 6; AAA87555)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="A -> S (in Ref. 6; AAA87555)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="S -> G (in Ref. 6; AAA87555)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="V -> L (in Ref. 2; CAD38632)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="D -> V (in Ref. 6; AAA87555)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..323
FT /note="LV -> RC (in Ref. 6; AAA87555)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="T -> H (in Ref. 6; AAA87555)"
FT /evidence="ECO:0000305"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2BV5"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:6H8R"
FT TURN 401..405
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 422..431
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 433..444
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 447..456
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 468..483
FT /evidence="ECO:0007829|PDB:6H8R"
FT STRAND 492..500
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 501..519
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:6H8R"
FT HELIX 542..559
FT /evidence="ECO:0007829|PDB:6H8R"
SQ SEQUENCE 565 AA; 63538 MW; DE32BEFFEFF7C494 CRC64;
MNYEGARSER ENHAADDSEG GALDMCCSER LPGLPQPIVM EALDEAEGLQ DSQREMPPPP
PPSPPSDPAQ KPPPRGAGSH SLTVRSSLCL FAASQFLLAC GVLWFSGYGH IWSQNATNLV
SSLLTLLKQL EPTAWLDSGT WGVPSLLLVF LSVGLVLVTT LVWHLLRTPP EPPTPLPPED
RRQSVSRQPS FTYSEWMEEK IEDDFLDLDP VPETPVFDCV MDIKPEADPT SLTVKSMGLQ
ERRGSNVSLT LDMCTPGCNE EGFGYLMSPR EESAREYLLS ASRVLQAEEL HEKALDPFLL
QAEFFEIPMN FVDPKEYDIP GLVRKNRYKT ILPNPHSRVC LTSPDPDDPL SSYINANYIR
GYGGEEKVYI ATQGPIVSTV ADFWRMVWQE HTPIIVMITN IEEMNEKCTE YWPEEQVAYD
GVEITVQKVI HTEDYRLRLI SLKSGTEERG LKHYWFTSWP DQKTPDRAPP LLHLVREVEE
AAQQEGPHCA PIIVHCSAGI GRTGCFIATS ICCQQLRQEG VVDILKTTCQ LRQDRGGMIQ
TCEQYQFVHH VMSLYEKQLS HQSPE
