MIO_HUMAN
ID MIO_HUMAN Reviewed; 875 AA.
AC Q9NXC5; B2RTV6; O75216; Q7L551; Q9H092;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=GATOR complex protein MIOS {ECO:0000305};
DE AltName: Full=Missing oocyte meiosis regulator homolog {ECO:0000312|HGNC:HGNC:21905};
GN Name=MIOS {ECO:0000312|HGNC:HGNC:21905};
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] (ISOFORM 2).
RC TISSUE=Hepatoma;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 464-875 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND SER-766, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND SUBUNIT.
RX PubMed=23723238; DOI=10.1126/science.1232044;
RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A.,
RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.;
RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that
RT signal amino acid sufficiency to mTORC1.";
RL Science 340:1100-1106(2013).
RN [15]
RP INTERACTION WITH SESN1; SESN2 AND SESN3.
RX PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
RA Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
RA Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
RT "The Sestrins interact with GATOR2 to negatively regulate the amino-acid-
RT sensing pathway upstream of mTORC1.";
RL Cell Rep. 9:1-8(2014).
RN [16]
RP FUNCTION.
RX PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
RA Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C., Akopiants K.,
RA Guan K.L., Karin M., Budanov A.V.;
RT "Sestrins inhibit mTORC1 kinase activation through the GATOR complex.";
RL Cell Rep. 9:1281-1291(2014).
RN [17]
RP INTERACTION WITH CASTOR2 AND CASTOR1.
RX PubMed=26972053; DOI=10.1016/j.cell.2016.02.035;
RA Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K., Wyant G.A.,
RA Wang T., Harper J.W., Gygi S.P., Sabatini D.M.;
RT "The CASTOR proteins are arginine sensors for the mTORC1 pathway.";
RL Cell 165:153-164(2016).
RN [18]
RP INTERACTION WITH SESN2.
RX PubMed=26586190; DOI=10.1126/science.aad2087;
RA Saxton R.A., Knockenhauer K.E., Wolfson R.L., Chantranupong L.,
RA Pacold M.E., Wang T., Schwartz T.U., Sabatini D.M.;
RT "Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway.";
RL Science 351:53-58(2016).
RN [19]
RP FUNCTION.
RX PubMed=27487210; DOI=10.1038/nature19079;
RA Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U.,
RA Sabatini D.M.;
RT "Mechanism of arginine sensing by CASTOR1 upstream of mTORC1.";
RL Nature 536:229-233(2016).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=28199306; DOI=10.1038/nature21423;
RA Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K.,
RA Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M.,
RA Frankel W.N., Sabatini D.M.;
RT "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to
RT regulate mTORC1.";
RL Nature 543:438-442(2017).
CC -!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively
CC regulated by the upstream amino acid sensors SESN2 and CASTOR1
CC (PubMed:25457612, PubMed:27487210). {ECO:0000269|PubMed:23723238,
CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
CC -!- SUBUNIT: Within the GATOR complex, component of the GATOR2 subcomplex,
CC made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly
CC interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2
CC complex interacts with CASTOR2 and CASTOR1; the interaction is
CC negatively regulated by arginine (PubMed:26972053). The GATOR2 complex
CC interacts with the sestrins SESN1, SESN2 and SESN3; the interaction is
CC negatively regulated by amino acids (PubMed:25263562, PubMed:25457612,
CC PubMed:26586190). {ECO:0000269|PubMed:23723238,
CC ECO:0000269|PubMed:25263562, ECO:0000269|PubMed:25457612,
CC ECO:0000269|PubMed:26586190, ECO:0000269|PubMed:26972053}.
CC -!- INTERACTION:
CC Q9NXC5; P58004: SESN2; NbExp=5; IntAct=EBI-2515122, EBI-3939642;
CC Q9NXC5; Q96S15: WDR24; NbExp=15; IntAct=EBI-2515122, EBI-746424;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:28199306}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXC5-2; Sequence=VSP_032979, VSP_032980;
CC -!- SIMILARITY: Belongs to the WD repeat mio family. {ECO:0000305}.
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DR EMBL; AK000330; BAA91090.1; -; mRNA.
DR EMBL; AC004982; AAC31788.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471073; EAW93598.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93601.1; -; Genomic_DNA.
DR EMBL; BC005883; AAH05883.2; -; mRNA.
DR EMBL; BC140833; AAI40834.1; -; mRNA.
DR EMBL; BC140834; AAI40835.1; -; mRNA.
DR EMBL; AL136892; CAB66826.2; -; mRNA.
DR CCDS; CCDS43554.1; -. [Q9NXC5-1]
DR RefSeq; NP_061878.3; NM_019005.3. [Q9NXC5-1]
DR RefSeq; XP_005249837.1; XM_005249780.3.
DR RefSeq; XP_005249838.1; XM_005249781.3.
DR RefSeq; XP_005249839.1; XM_005249782.3.
DR RefSeq; XP_016867850.1; XM_017012361.1.
DR AlphaFoldDB; Q9NXC5; -.
DR SMR; Q9NXC5; -.
DR BioGRID; 119974; 59.
DR ComplexPortal; CPX-6227; GATOR2 complex.
DR CORUM; Q9NXC5; -.
DR DIP; DIP-53801N; -.
DR IntAct; Q9NXC5; 32.
DR MINT; Q9NXC5; -.
DR STRING; 9606.ENSP00000339881; -.
DR iPTMnet; Q9NXC5; -.
DR PhosphoSitePlus; Q9NXC5; -.
DR BioMuta; MIOS; -.
DR DMDM; 182662411; -.
DR EPD; Q9NXC5; -.
DR jPOST; Q9NXC5; -.
DR MassIVE; Q9NXC5; -.
DR MaxQB; Q9NXC5; -.
DR PaxDb; Q9NXC5; -.
DR PeptideAtlas; Q9NXC5; -.
DR PRIDE; Q9NXC5; -.
DR ProteomicsDB; 83074; -. [Q9NXC5-1]
DR ProteomicsDB; 83075; -. [Q9NXC5-2]
DR Antibodypedia; 50650; 37 antibodies from 15 providers.
DR DNASU; 54468; -.
DR Ensembl; ENST00000340080.9; ENSP00000339881.4; ENSG00000164654.16. [Q9NXC5-1]
DR Ensembl; ENST00000405785.5; ENSP00000384088.1; ENSG00000164654.16. [Q9NXC5-1]
DR GeneID; 54468; -.
DR KEGG; hsa:54468; -.
DR MANE-Select; ENST00000340080.9; ENSP00000339881.4; NM_019005.4; NP_061878.3.
DR UCSC; uc003srf.4; human. [Q9NXC5-1]
DR CTD; 54468; -.
DR GeneCards; MIOS; -.
DR HGNC; HGNC:21905; MIOS.
DR HPA; ENSG00000164654; Tissue enhanced (skeletal).
DR MIM; 615359; gene.
DR neXtProt; NX_Q9NXC5; -.
DR OpenTargets; ENSG00000164654; -.
DR PharmGKB; PA164722300; -.
DR VEuPathDB; HostDB:ENSG00000164654; -.
DR eggNOG; KOG1008; Eukaryota.
DR GeneTree; ENSGT00390000015038; -.
DR HOGENOM; CLU_005843_1_0_1; -.
DR InParanoid; Q9NXC5; -.
DR OMA; QSHNSTC; -.
DR PhylomeDB; Q9NXC5; -.
DR TreeFam; TF324074; -.
DR PathwayCommons; Q9NXC5; -.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q9NXC5; -.
DR SIGNOR; Q9NXC5; -.
DR BioGRID-ORCS; 54468; 296 hits in 1081 CRISPR screens.
DR GenomeRNAi; 54468; -.
DR Pharos; Q9NXC5; Tdark.
DR PRO; PR:Q9NXC5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NXC5; protein.
DR Bgee; ENSG00000164654; Expressed in tongue squamous epithelium and 208 other tissues.
DR ExpressionAtlas; Q9NXC5; baseline and differential.
DR Genevisible; Q9NXC5; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IC:ComplexPortal.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:UniProtKB.
DR CDD; cd16691; mRING-H2-C3H3C2_Mio; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037593; MIOS/Sea4.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR031488; Zn_ribbon_mio.
DR PANTHER; PTHR16453; PTHR16453; 1.
DR Pfam; PF17034; zinc_ribbon_16; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..875
FT /note="GATOR complex protein MIOS"
FT /id="PRO_0000329404"
FT REPEAT 58..100
FT /note="WD 1"
FT REPEAT 111..155
FT /note="WD 2"
FT REPEAT 182..221
FT /note="WD 3"
FT REPEAT 223..261
FT /note="WD 4"
FT REPEAT 265..306
FT /note="WD 5"
FT REPEAT 395..437
FT /note="WD 6"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 551..567
FT /note="DLNLNVVAMALSGYTDE -> RRSESQCGSNGFIGLYG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032979"
FT VAR_SEQ 568..875
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032980"
SQ SEQUENCE 875 AA; 98584 MW; 481D3AA0C9A3A1CB CRC64;
MSGTKPDILW APHHVDRFVV CDSELSLYHV ESTVNSELKA GSLRLSEDSA ATLLSINSDT
PYMKCVAWYL NYDPECLLAV GQANGRVVLT SLGQDHNSKF KDLIGKEFVP KHARQCNTLA
WNPLDSNWLA AGLDKHRADF SVLIWDICSK YTPDIVPMEK VKLSAGETET TLLVTKPLYE
LGQNDACLSL CWLPRDQKLL LAGMHRNLAI FDLRNTSQKM FVNTKAVQGV TVDPYFHDRV
ASFYEGQVAI WDLRKFEKPV LTLTEQPKPL TKVAWCPTRT GLLATLTRDS NIIRLYDMQH
TPTPIGDETE PTIIERSVQP CDNYIASFAW HPTSQNRMIV VTPNRTMSDF TVFERISLAW
SPITSLMWAC GRHLYECTEE ENDNSLEKDI ATKMRLRALS RYGLDTEQVW RNHILAGNED
PQLKSLWYTL HFMKQYTEDM DQKSPGNKGS LVYAGIKSIV KSSLGMVESS RHNWSGLDKQ
SDIQNLNEER ILALQLCGWI KKGTDVDVGP FLNSLVQEGE WERAAAVALF NLDIRRAIQI
LNEGASSEKG DLNLNVVAMA LSGYTDEKNS LWREMCSTLR LQLNNPYLCV MFAFLTSETG
SYDGVLYENK VAVRDRVAFA CKFLSDTQLN RYIEKLTNEM KEAGNLEGIL LTGLTKDGVD
LMESYVDRTG DVQTASYCML QGSPLDVLKD ERVQYWIENY RNLLDAWRFW HKRAEFDIHR
SKLDPSSKPL AQVFVSCNFC GKSISYSCSA VPHQGRGFSQ YGVSGSPTKS KVTSCPGCRK
PLPRCALCLI NMGTPVSSCP GGTKSDEKVD LSKDKKLAQF NNWFTWCHNC RHGGHAGHML
SWFRDHAECP VSACTCKCMQ LDTTGNLVPA ETVQP
