MTMR8_HUMAN
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 03-AUG-2022, entry version 166.
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};
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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; 23.
DR DIP; DIP-60046N; -.
DR IntAct; Q96EF0; 8.
DR MINT; Q96EF0; -.
DR STRING; 9606.ENSP00000363985; -.
DR DEPOD; MTMR8; -.
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; Q96EF0; -.
DR PeptideAtlas; Q96EF0; -.
DR PRIDE; Q96EF0; -.
DR ProteomicsDB; 76401; -. [Q96EF0-1]
DR ProteomicsDB; 76402; -. [Q96EF0-2]
DR Antibodypedia; 27059; 113 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 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; CHKERED; -.
DR OrthoDB; 824298at2759; -.
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 707 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 colonic epithelium and 137 other tissues.
DR Genevisible; Q96EF0; HS.
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-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 Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030591; MTMR8.
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; PTHR10807; 1.
DR PANTHER; PTHR10807:SF36; PTHR10807:SF36; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
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
