ID MTMR8_HUMAN Reviewed; 704 AA. AC Q96EF0; Q5JT99; Q9NXP6; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 175. DE RecName: Full=Myotubularin-related protein 8; DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000305}; DE EC=3.1.3.95 {ECO:0000269|PubMed:16959974, ECO:0000269|PubMed:22647598}; DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000305}; DE EC=3.1.3.64 {ECO:0000269|PubMed:22647598}; GN Name=MTMR8; 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 GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary; 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 [LARGE SCALE MRNA] OF 85-704 (ISOFORM 2). RC TISSUE=Colon; 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 [5] RP SUBCELLULAR LOCATION, AND INTERACTION WITH MTMR9. RX PubMed=16787938; DOI=10.1242/jcs.03040; RA Lorenzo O., Urbe S., Clague M.J.; RT "Systematic analysis of myotubularins: heteromeric interactions, RT subcellular localisation and endosome related functions."; RL J. Cell Sci. 119:2953-2959(2006). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH RP MTMR9. RX PubMed=22647598; DOI=10.1073/pnas.1207021109; RA Zou J., Zhang C., Marjanovic J., Kisseleva M.V., Majerus P.W., Wilson M.P.; RT "Myotubularin-related protein (MTMR) 9 determines the enzymatic activity, RT substrate specificity, and role in autophagy of MTMR8."; RL Proc. Natl. Acad. Sci. U.S.A. 109:9539-9544(2012). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 122-505 IN COMPLEX WITH RP PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ALA-253 AND RP LYS-255. RX PubMed=26143924; DOI=10.1107/s139900471500927x; RA Yoo K.Y., Son J.Y., Lee J.U., Shin W., Im D.W., Kim S.J., Ryu S.E., RA Heo Y.S.; RT "Structure of the catalytic phosphatase domain of MTMR8: implications for RT dimerization, membrane association and reversible oxidation."; RL Acta Crystallogr. D 71:1528-1539(2015). RN [8] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-127 AND LYS-454. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol CC headgroup (PubMed:22647598, PubMed:26143924). Has phosphatase activity CC towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5- CC bisphosphate (PubMed:22647598, PubMed:26143924). In complex with MTMR9, CC negatively regulates autophagy (PubMed:22647598). CC {ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:26143924}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3- CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64; CC Evidence={ECO:0000269|PubMed:22647598}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5- CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795, CC ChEBI:CHEBI:57923; EC=3.1.3.95; CC Evidence={ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:26143924}; CC -!- ACTIVITY REGULATION: Interaction with MTMR9 increases phosphatase CC activity. {ECO:0000269|PubMed:22647598}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=16.64 uM for phosphatidylinositol 3,5-biphosphate CC {ECO:0000269|PubMed:26143924}; CC -!- SUBUNIT: Homodimer (PubMed:26143924). Heterodimer with MTMR9 CC (PubMed:16787938, PubMed:22647598). {ECO:0000269|PubMed:16787938, CC ECO:0000269|PubMed:22647598, ECO:0000269|PubMed:26143924}. CC -!- INTERACTION: CC Q96EF0; Q96QG7: MTMR9; NbExp=6; IntAct=EBI-750578, EBI-744593; CC Q96EF0-1; Q96QG7: MTMR9; NbExp=3; IntAct=EBI-15985865, EBI-744593; CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:16787938}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96EF0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96EF0-2; Sequence=VSP_033007; CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class myotubularin subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA90964.1; Type=Erroneous initiation; Evidence={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; AL034408; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356317; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471132; EAX05411.1; -; Genomic_DNA. DR EMBL; BC012399; AAH12399.1; -; mRNA. DR EMBL; AK000133; BAA90964.1; ALT_INIT; mRNA. DR CCDS; CCDS14379.1; -. [Q96EF0-1] DR RefSeq; NP_060147.2; NM_017677.3. [Q96EF0-1] DR PDB; 4Y7I; X-ray; 2.80 A; A/B=122-505. DR PDBsum; 4Y7I; -. DR AlphaFoldDB; Q96EF0; -. DR SMR; Q96EF0; -. DR BioGRID; 120753; 25. DR DIP; DIP-60046N; -. DR IntAct; Q96EF0; 8. DR MINT; Q96EF0; -. DR STRING; 9606.ENSP00000363985; -. DR DEPOD; MTMR8; -. DR GlyGen; Q96EF0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96EF0; -. DR MetOSite; Q96EF0; -. DR PhosphoSitePlus; Q96EF0; -. DR BioMuta; MTMR8; -. DR DMDM; 74751838; -. DR EPD; Q96EF0; -. DR jPOST; Q96EF0; -. DR MassIVE; Q96EF0; -. DR MaxQB; Q96EF0; -. DR PaxDb; 9606-ENSP00000363985; -. DR PeptideAtlas; Q96EF0; -. DR ProteomicsDB; 76401; -. [Q96EF0-1] DR ProteomicsDB; 76402; -. [Q96EF0-2] DR Antibodypedia; 27059; 121 antibodies from 22 providers. DR DNASU; 55613; -. DR Ensembl; ENST00000374852.4; ENSP00000363985.3; ENSG00000102043.16. [Q96EF0-1] DR GeneID; 55613; -. DR KEGG; hsa:55613; -. DR MANE-Select; ENST00000374852.4; ENSP00000363985.3; NM_017677.4; NP_060147.2. DR UCSC; uc004dvs.4; human. [Q96EF0-1] DR AGR; HGNC:16825; -. DR CTD; 55613; -. DR DisGeNET; 55613; -. DR GeneCards; MTMR8; -. DR HGNC; HGNC:16825; MTMR8. DR HPA; ENSG00000102043; Low tissue specificity. DR MIM; 301061; gene. DR neXtProt; NX_Q96EF0; -. DR OpenTargets; ENSG00000102043; -. DR PharmGKB; PA134942633; -. DR VEuPathDB; HostDB:ENSG00000102043; -. DR eggNOG; KOG1089; Eukaryota. DR GeneTree; ENSGT00940000162717; -. DR HOGENOM; CLU_001839_3_2_1; -. DR InParanoid; Q96EF0; -. DR OMA; FRFIGIE; -. DR OrthoDB; 5474662at2759; -. DR PhylomeDB; Q96EF0; -. DR TreeFam; TF315197; -. DR BRENDA; 3.1.3.95; 2681. DR PathwayCommons; Q96EF0; -. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR SignaLink; Q96EF0; -. DR BioGRID-ORCS; 55613; 9 hits in 793 CRISPR screens. DR ChiTaRS; MTMR8; human. DR GenomeRNAi; 55613; -. DR Pharos; Q96EF0; Tbio. DR PRO; PR:Q96EF0; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q96EF0; Protein. DR Bgee; ENSG00000102043; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 138 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0106018; F:phosphatidylinositol-3,5-bisphosphate phosphatase activity; IDA:UniProtKB. DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IDA:UniProtKB. DR GO; GO:0010507; P:negative regulation of autophagy; IPI:UniProtKB. DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB. DR GO; GO:0016241; P:regulation of macroautophagy; IMP:FlyBase. DR CDD; cd13345; PH-GRAM_MTMR8; 1. DR CDD; cd14584; PTP-MTMR8; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR030591; MTMR8_PTP. DR InterPro; IPR010569; Myotubularin-like_Pase_dom. DR InterPro; IPR030564; Myotubularin_fam. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1. DR PANTHER; PTHR10807:SF36; MYOTUBULARIN-RELATED PROTEIN 8; 1. DR Pfam; PF06602; Myotub-related; 1. DR Pfam; PF21098; PH-GRAM_MTMR6-like; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR Genevisible; Q96EF0; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Hydrolase; KW Lipid metabolism; Nucleus; Reference proteome. FT CHAIN 1..704 FT /note="Myotubularin-related protein 8" FT /id="PRO_0000330034" FT DOMAIN 126..500 FT /note="Myotubularin phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669" FT COILED 515..541 FT /evidence="ECO:0000255" FT ACT_SITE 338 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044" FT BINDING 250..253 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16959974" FT BINDING 275..276 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q13614" FT BINDING 338..344 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16959974" FT BINDING 384 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q13614" FT VAR_SEQ 153..265 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033007" FT VARIANT 127 FT /note="W -> R (in a breast cancer sample; somatic mutation; FT dbSNP:rs1406282063)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_042688" FT VARIANT 454 FT /note="E -> K (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_042689" FT MUTAGEN 253 FT /note="A->K: Increases catalytic activity." FT /evidence="ECO:0000269|PubMed:26143924" FT MUTAGEN 255 FT /note="K->A: Decreases catalytic activity." FT /evidence="ECO:0000269|PubMed:26143924" FT CONFLICT 130 FT /note="I -> S (in Ref. 4; BAA90964)" FT /evidence="ECO:0000305" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 134..138 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 142..149 FT /evidence="ECO:0007829|PDB:4Y7I" FT TURN 151..154 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 173..180 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:4Y7I" FT TURN 196..198 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 201..205 FT /evidence="ECO:0007829|PDB:4Y7I" FT TURN 211..213 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 217..227 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 244..252 FT /evidence="ECO:0007829|PDB:4Y7I" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 266..270 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 276..290 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 297..307 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 309..328 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 339..343 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 344..356 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 363..373 FT /evidence="ECO:0007829|PDB:4Y7I" FT TURN 374..378 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 381..384 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 398..412 FT /evidence="ECO:0007829|PDB:4Y7I" FT TURN 414..416 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 421..433 FT /evidence="ECO:0007829|PDB:4Y7I" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 444..449 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 452..455 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 459..465 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:4Y7I" FT HELIX 490..492 FT /evidence="ECO:0007829|PDB:4Y7I" FT TURN 497..501 FT /evidence="ECO:0007829|PDB:4Y7I" SQ SEQUENCE 704 AA; 78919 MW; 515BE817C9AEA961 CRC64; MDHITVPKVE NVKLVDRYVS KKPANGILYL TATHLIYVEA SGAARKETWI ALHHIATVEK LPITSLGCPL TLRCKNFRVA HFVLDSDLVC HEVYISLLKL SQPALPEDLY AFSYNPKSSK EMRESGWKLI DPISDFGRMG IPNRNWTITD ANRNYEICST YPPEIVVPKS VTLGTVVGSS KFRSKERVPV LSYLYKENNA AICRCSQPLS GFYTRCVDDE LLLEAISQTN PGSQFMYVVD TRPKLNAMAN RAAGKGYENE DNYANIRFRF MGIENIHVMR SSLQKLLEVC ELKTPTMSEF LSGLESSGWL RHIKAIMDAG IFITKAVKVE KASVLVHCSD GWDRTAQVCS VASILLDPFY RTFKGLMILI EKEWISMGHK FSQRCGHLDG DSKEVSPIFT QFLDCIWQLM EQFPCAFEFN ENFLLEIHDH VFSCQFGNFL GNCQKDREDL RVYEKTHSVW PFLVQRKPDF RNPLYKGFTM YGVLNPSTVP YNIQFWCGMY NRFDKGLQPK QSMLESLLEI KKQRAMLETD VHELEKKLKV RDEPPEEICT CSQLGNILSQ HLGSPLTNPL GFMGINGDLN TLMENGTLSR EGGLRAQMDQ VKSQGADLHH NCCEIVGSLR AINISGDVGI SEAMGISGDM CTFEATGFSK DLGICGAMDI SEATGISGNL GISEARGFSG DMGILGDTGI SKASTKEADY SKHQ //