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 27-MAR-2024, entry version 192. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8SLS; X-ray; 1.71 A; A=280-561. DR PDB; 8SLT; X-ray; 1.96 A; A=280-561. DR PDB; 8SLU; X-ray; 1.84 A; A=280-561. DR PDBsum; 2BIJ; -. DR PDBsum; 2BV5; -. DR PDBsum; 2CJZ; -. DR PDBsum; 5OVR; -. DR PDBsum; 5OVX; -. DR PDBsum; 5OW1; -. DR PDBsum; 6H8R; -. DR PDBsum; 8SLS; -. DR PDBsum; 8SLT; -. DR PDBsum; 8SLU; -. DR AlphaFoldDB; P54829; -. DR SMR; P54829; -. DR BioGRID; 124312; 80. DR ELM; P54829; -. DR IntAct; P54829; 40. 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; 9606-ENSP00000351342; -. DR PeptideAtlas; P54829; -. DR ProteomicsDB; 56735; -. [P54829-1] DR ProteomicsDB; 56736; -. [P54829-2] DR ProteomicsDB; 7064; -. DR Antibodypedia; 25176; 328 antibodies from 30 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 AGR; HGNC:9657; -. 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; GDNMYLF; -. DR OrthoDB; 2914248at2759; -. 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; 12 hits in 1161 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 114 other cell types or tissues. DR ExpressionAtlas; P54829; baseline and differential. 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:0016020; C: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:0006470; P:protein dephosphorylation; TAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd14613; PTPc-N5; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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; PROTEIN-TYROSINE-PHOSPHATASE; 1. DR PANTHER; PTHR46198:SF1; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 5; 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; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. DR Genevisible; P54829; HS. 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:8SLS" 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 //