PTN4_HUMAN
ID PTN4_HUMAN Reviewed; 926 AA.
AC P29074; B2RBV8; Q9UDA7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 4;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase MEG1;
DE Short=MEG;
DE Short=PTPase-MEG1;
GN Name=PTPN4;
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 [MRNA].
RX PubMed=1648233; DOI=10.1073/pnas.88.13.5867;
RA Gu M., York J.D., Warshawsky I., Majerus P.W.;
RT "Identification, cloning, and expression of a cytosolic megakaryocyte
RT protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein
RT 4.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5867-5871(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 745-858.
RC TISSUE=Leukemia;
RX PubMed=8483328;
RA Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.;
RT "Identification of novel protein-tyrosine phosphatases in a human leukemia
RT cell line, F-36P.";
RL Leukemia 7:742-746(1993).
RN [5]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND CLEAVAGE.
RX PubMed=8910369; DOI=10.1074/jbc.271.44.27751;
RA Gu M., Majerus P.W.;
RT "The properties of the protein tyrosine phosphatase PTPMEG.";
RL J. Biol. Chem. 271:27751-27759(1996).
RN [6]
RP FUNCTION.
RX PubMed=25825441; DOI=10.4049/jimmunol.1402183;
RA Huai W., Song H., Wang L., Li B., Zhao J., Han L., Gao C., Jiang G.,
RA Zhang L., Zhao W.;
RT "Phosphatase PTPN4 preferentially inhibits TRIF-dependent TLR4 pathway by
RT dephosphorylating TRAM.";
RL J. Immunol. 194:4458-4465(2015).
RN [7]
RP STRUCTURE BY NMR OF 507-612.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PDZ domain of protein tyrosine phosphatase, non-
RT receptor type 4.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATTENUATED RABIES
RP VIRUS PROTEIN G (MICROBIAL INFECTION).
RX PubMed=20086240; DOI=10.1126/scisignal.2000510;
RA Prehaud C., Wolff N., Terrien E., Lafage M., Megret F., Babault N.,
RA Cordier F., Tan G.S., Maitrepierre E., Menager P., Chopy D., Hoos S.,
RA England P., Delepierre M., Schnell M.J., Buc H., Lafon M.;
RT "Attenuation of rabies virulence: takeover by the cytoplasmic domain of its
RT envelope protein.";
RL Sci. Signal. 3:RA5-RA5(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 499-604, INTERACTION WITH MAPK12,
RP AND FUNCTION.
RX PubMed=27246854; DOI=10.1074/jbc.m115.707208;
RA Maisonneuve P., Caillet-Saguy C., Vaney M.C., Bibi-Zainab E., Sawyer K.,
RA Raynal B., Haouz A., Delepierre M., Lafon M., Cordier F., Wolff N.;
RT "Molecular Basis of the Interaction of the Human Protein Tyrosine
RT Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein
RT Kinase p38gamma.";
RL J. Biol. Chem. 291:16699-16708(2016).
CC -!- FUNCTION: Phosphatase that plays a role in immunity, learning, synaptic
CC plasticity or cell homeostasis (PubMed:25825441, PubMed:27246854).
CC Regulates neuronal cell homeostasis by protecting neurons against
CC apoptosis (PubMed:20086240). Negatively regulates TLR4-induced
CC interferon beta production by dephosphorylating adapter TICAM2 and
CC inhibiting subsequent TRAM-TRIF interaction (PubMed:25825441).
CC Dephosphorylates also the immunoreceptor tyrosine-based activation
CC motifs/ITAMs of the TCR zeta subunit and thereby negatively regulates
CC TCR-mediated signaling pathway (By similarity). May act at junctions
CC between the membrane and the cytoskeleton. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9WU22, ECO:0000269|PubMed:20086240,
CC ECO:0000269|PubMed:25825441, ECO:0000269|PubMed:27246854}.
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 -!- SUBUNIT: Interacts with MAPK12 (via C-terminus); this interaction
CC abolishes PTPN4 catalytic autoinhibition and thus activates the
CC phosphatase activity. {ECO:0000269|PubMed:27246854}.
CC -!- SUBUNIT: (Microbial infection) Interacts with attenuated rabies virus
CC protein G; this interaction is required for virally-induced apoptosis.
CC {ECO:0000269|PubMed:20086240}.
CC -!- INTERACTION:
CC P29074; P55212: CASP6; NbExp=3; IntAct=EBI-710431, EBI-718729;
CC P29074; P06307: CCK; NbExp=3; IntAct=EBI-710431, EBI-6624398;
CC P29074; P46108: CRK; NbExp=3; IntAct=EBI-710431, EBI-886;
CC P29074; Q92993: KAT5; NbExp=2; IntAct=EBI-710431, EBI-399080;
CC P29074; P13473-2: LAMP2; NbExp=3; IntAct=EBI-710431, EBI-21591415;
CC P29074; P53778: MAPK12; NbExp=2; IntAct=EBI-710431, EBI-602406;
CC P29074; P16333: NCK1; NbExp=3; IntAct=EBI-710431, EBI-389883;
CC P29074; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-710431, EBI-5280197;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8910369};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8910369}.
CC Cytoplasm {ECO:0000269|PubMed:20086240, ECO:0000269|PubMed:8910369}.
CC -!- PTM: Highly phosphorylated on serine and threonine residues but not on
CC tyrosines. {ECO:0000269|PubMed:8910369}.
CC -!- PTM: Cleaved and activated by calpain I/CAPN1.
CC {ECO:0000269|PubMed:8910369}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; M68941; AAA36530.1; -; mRNA.
DR EMBL; AK314836; BAG37355.1; -; mRNA.
DR EMBL; BC010674; AAH10674.1; -; mRNA.
DR CCDS; CCDS2129.1; -.
DR PIR; A41105; A41105.
DR RefSeq; NP_002821.1; NM_002830.3.
DR RefSeq; XP_016860089.1; XM_017004600.1.
DR PDB; 2CS5; NMR; -; A=507-612.
DR PDB; 2I75; X-ray; 2.45 A; A=611-926.
DR PDB; 2VPH; X-ray; 1.90 A; A/B=513-606.
DR PDB; 3NFK; X-ray; 1.43 A; A/B=499-604.
DR PDB; 3NFL; X-ray; 1.91 A; A/B/C/D=499-604.
DR PDB; 5EYZ; X-ray; 2.09 A; A/B/C/D=499-604.
DR PDB; 5EZ0; X-ray; 2.35 A; A/B/C/D=499-604.
DR PDB; 7VZE; X-ray; 2.88 A; A/B/C/D=513-603.
DR PDBsum; 2CS5; -.
DR PDBsum; 2I75; -.
DR PDBsum; 2VPH; -.
DR PDBsum; 3NFK; -.
DR PDBsum; 3NFL; -.
DR PDBsum; 5EYZ; -.
DR PDBsum; 5EZ0; -.
DR PDBsum; 7VZE; -.
DR AlphaFoldDB; P29074; -.
DR BMRB; P29074; -.
DR SMR; P29074; -.
DR BioGRID; 111741; 50.
DR DIP; DIP-34634N; -.
DR IntAct; P29074; 40.
DR MINT; P29074; -.
DR STRING; 9606.ENSP00000263708; -.
DR BindingDB; P29074; -.
DR ChEMBL; CHEMBL3165; -.
DR DrugBank; DB00630; Alendronic acid.
DR DEPOD; PTPN4; -.
DR iPTMnet; P29074; -.
DR PhosphoSitePlus; P29074; -.
DR BioMuta; PTPN4; -.
DR DMDM; 131531; -.
DR EPD; P29074; -.
DR jPOST; P29074; -.
DR MassIVE; P29074; -.
DR PaxDb; P29074; -.
DR PeptideAtlas; P29074; -.
DR PRIDE; P29074; -.
DR ProteomicsDB; 54516; -.
DR Antibodypedia; 18333; 143 antibodies from 22 providers.
DR DNASU; 5775; -.
DR Ensembl; ENST00000263708.7; ENSP00000263708.2; ENSG00000088179.9.
DR GeneID; 5775; -.
DR KEGG; hsa:5775; -.
DR MANE-Select; ENST00000263708.7; ENSP00000263708.2; NM_002830.4; NP_002821.1.
DR UCSC; uc002tmf.3; human.
DR CTD; 5775; -.
DR DisGeNET; 5775; -.
DR GeneCards; PTPN4; -.
DR HGNC; HGNC:9656; PTPN4.
DR HPA; ENSG00000088179; Tissue enhanced (brain).
DR MIM; 176878; gene.
DR neXtProt; NX_P29074; -.
DR OpenTargets; ENSG00000088179; -.
DR PharmGKB; PA34000; -.
DR VEuPathDB; HostDB:ENSG00000088179; -.
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000157211; -.
DR HOGENOM; CLU_001645_7_0_1; -.
DR InParanoid; P29074; -.
DR OMA; MRWLDPS; -.
DR OrthoDB; 96595at2759; -.
DR PhylomeDB; P29074; -.
DR TreeFam; TF315900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P29074; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR SignaLink; P29074; -.
DR BioGRID-ORCS; 5775; 13 hits in 1082 CRISPR screens.
DR ChiTaRS; PTPN4; human.
DR EvolutionaryTrace; P29074; -.
DR GeneWiki; PTPN4; -.
DR GenomeRNAi; 5775; -.
DR Pharos; P29074; Tchem.
DR PRO; PR:P29074; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P29074; protein.
DR Bgee; ENSG00000088179; Expressed in lateral nuclear group of thalamus and 191 other tissues.
DR ExpressionAtlas; P29074; baseline and differential.
DR Genevisible; P29074; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0035254; F:glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR IDEAL; IID00656; -.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041783; PTPN3/4_FERM_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50106; PDZ; 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; Cell membrane; Cytoplasm; Cytoskeleton; Hydrolase; Membrane;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..926
FT /note="Tyrosine-protein phosphatase non-receptor type 4"
FT /id="PRO_0000219434"
FT DOMAIN 29..312
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 517..589
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 655..911
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 380..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 852
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 820
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 852..858
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 896
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU22"
FT VARIANT 924
FT /note="T -> S (in dbSNP:rs3189128)"
FT /id="VAR_061033"
FT CONFLICT 131
FT /note="K -> E (in Ref. 2; BAG37355)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="G -> K (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="I -> V (in Ref. 2; BAG37355)"
FT /evidence="ECO:0000305"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:3NFK"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:2CS5"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:3NFK"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:3NFK"
FT STRAND 540..547
FT /evidence="ECO:0007829|PDB:3NFK"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:2CS5"
FT HELIX 552..555
FT /evidence="ECO:0007829|PDB:3NFK"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:3NFK"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:3NFK"
FT HELIX 579..587
FT /evidence="ECO:0007829|PDB:3NFK"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:3NFK"
FT STRAND 596..602
FT /evidence="ECO:0007829|PDB:3NFK"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:2VPH"
FT HELIX 639..651
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 654..661
FT /evidence="ECO:0007829|PDB:2I75"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 704..713
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 720..726
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 734..743
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 779..783
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 790..801
FT /evidence="ECO:0007829|PDB:2I75"
FT TURN 802..805
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 806..815
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 820..823
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 828..841
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 848..851
FT /evidence="ECO:0007829|PDB:2I75"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 858..873
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 880..888
FT /evidence="ECO:0007829|PDB:2I75"
FT HELIX 898..911
FT /evidence="ECO:0007829|PDB:2I75"
SQ SEQUENCE 926 AA; 105911 MW; 4DAC6A87A675CFB0 CRC64;
MTSRFRLPAG RTYNVRASEL ARDRQHTEVV CNILLLDNTV QAFKVNKHDQ GQVLLDVVFK
HLDLTEQDYF GLQLADDSTD NPRWLDPNKP IRKQLKRGSP YSLNFRVKFF VSDPNKLQEE
YTRYQYFLQI KQDILTGRLP CPSNTAALLA SFAVQSELGD YDQSENLSGY LSDYSFIPNQ
PQDFEKEIAK LHQQHIGLSP AEAEFNYLNT ARTLELYGVE FHYARDQSNN EIMIGVMSGG
ILIYKNRVRM NTFPWLKIVK ISFKCKQFFI QLRKELHESR ETLLGFNMVN YRACKNLWKA
CVEHHTFFRL DRPLPPQKNF FAHYFTLGSK FRYCGRTEVQ SVQYGKEKAN KDRVFARSPS
KPLARKLMDW EVVSRNSISD DRLETQSLPS RSPPGTPNHR NSTFTQEGTR LRPSSVGHLV
DHMVHTSPSE VFVNQRSPSS TQANSIVLES SPSQETPGDG KPPALPPKQS KKNSWNQIHY
SHSQQDLESH INETFDIPSS PEKPTPNGGI PHDNLVLIRM KPDENGRFGF NVKGGYDQKM
PVIVSRVAPG TPADLCVPRL NEGDQVVLIN GRDIAEHTHD QVVLFIKASC ERHSGELMLL
VRPNAVYDVV EEKLENEPDF QYIPEKAPLD SVHQDDHSLR ESMIQLAEGL ITGTVLTQFD
QLYRKKPGMT MSCAKLPQNI SKNRYRDISP YDATRVILKG NEDYINANYI NMEIPSSSII
NQYIACQGPL PHTCTDFWQM TWEQGSSMVV MLTTQVERGR VKCHQYWPEP TGSSSYGCYQ
VTCHSEEGNT AYIFRKMTLF NQEKNESRPL TQIQYIAWPD HGVPDDSSDF LDFVCHVRNK
RAGKEEPVVV HCSAGIGRTG VLITMETAMC LIECNQPVYP LDIVRTMRDQ RAMMIQTPSQ
YRFVCEAILK VYEEGFVKPL TTSTNK
