IML1_YEAST
ID IML1_YEAST Reviewed; 1584 AA.
AC P47170; D6VWV7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Vacuolar membrane-associated protein IML1;
DE AltName: Full=Increased minichromosome loss protein 1;
DE AltName: Full=SEH-associated protein 1;
GN Name=IML1; Synonyms=SEA1; OrderedLocusNames=YJR138W; ORFNames=J2129;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680 AND SER-737, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA Rout M.P., Dargemont C.;
RT "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT associates with the vacuole in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011).
CC -!- FUNCTION: Component of the SEA complex which coats the vacuolar
CC membrane and is involved in intracellular trafficking, autophagy,
CC response to nitrogen starvation, and amino acid biogenesis.
CC {ECO:0000269|PubMed:21454883}.
CC -!- SUBUNIT: Component of the SEA complex composed of at least IML1/SEA1,
CC RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
CC {ECO:0000269|PubMed:21454883}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:21454883}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21454883}.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IML1 family. {ECO:0000305}.
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DR EMBL; Z49638; CAA89670.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08923.1; -; Genomic_DNA.
DR PIR; S57161; S57161.
DR RefSeq; NP_012672.1; NM_001181796.2.
DR AlphaFoldDB; P47170; -.
DR BioGRID; 33894; 235.
DR ComplexPortal; CPX-3231; SEA complex.
DR DIP; DIP-2589N; -.
DR IntAct; P47170; 29.
DR MINT; P47170; -.
DR STRING; 4932.YJR138W; -.
DR iPTMnet; P47170; -.
DR MaxQB; P47170; -.
DR PaxDb; P47170; -.
DR PRIDE; P47170; -.
DR EnsemblFungi; YJR138W_mRNA; YJR138W; YJR138W.
DR GeneID; 853603; -.
DR KEGG; sce:YJR138W; -.
DR SGD; S000003899; IML1.
DR VEuPathDB; FungiDB:YJR138W; -.
DR eggNOG; KOG3572; Eukaryota.
DR GeneTree; ENSGT00390000016559; -.
DR HOGENOM; CLU_000935_1_1_1; -.
DR InParanoid; P47170; -.
DR OMA; RMYDLQM; -.
DR BioCyc; YEAST:G3O-31754-MON; -.
DR PRO; PR:P47170; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47170; protein.
DR GO; GO:0097042; C:extrinsic component of fungal-type vacuolar membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:1990130; C:GATOR1 complex; IDA:SGD.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IC:ComplexPortal.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IGI:SGD.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:SGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:SGD.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR045838; DEPDC5_CTD.
DR InterPro; IPR027244; IML1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13179; PTHR13179; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF19418; DEPDC5_CTD; 1.
DR Pfam; PF12257; IML1; 1.
DR SMART; SM00049; DEP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50186; DEP; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Vacuole.
FT CHAIN 1..1584
FT /note="Vacuolar membrane-associated protein IML1"
FT /id="PRO_0000203123"
FT DOMAIN 1198..1273
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1584 AA; 181949 MW; BB8E73FF5B70CCDF CRC64;
MFAKLHGKKQ RPISSINSQT PRTSNTTHAN SISLSSGNLI VGSNRNLRQK KEQFGSQQRA
SGRKLISNKE NDDNVNNGGD NNYDNGERVH RHHIPGLKIK AYQAELGYHE SRFSENLVML
NLVEFPDIKP GDLVELKTYH KNPSASNGDK KIYFIAKDFD GETKRRAKTS NVSILSGQLQ
TLLDLPSRSR IWIKLKPNKF DLQADVVEFN IKDCLLNRGD MWVLSSKLVD TCVFMDQRLA
FLDSIRGTIK GIYRNGKKIV SGYIGEQTRI IFRSESARLI FLIQITDEMW NFEETGEQLF
QKMVNSFFPK IFKKWKDVDT HHTITIAFAI SMDLSDTSFK DLTPGESLKN SQDYFRIVVD
QVSIIHWVDI METLREEFME IRKDLLNKQT DKGYSVANGR FSPVIKSNFL ELVNFATTIL
TDPFKQLDLR HTTTHVMIIS PGSGLFDVDY SLLRLTGKKL LSLEMTMDLI CLSKAPLHIV
PLFRYRDFEN KLHHCVPLWL SVFFWNDHDK KSNSEWTPRC KIYDLQMMGI TENELIREVD
VEYLQLNKKV KSLSEFMNDY DKNAFEVKIL CAGSNTKQSK KLNSKFDTVF ENDVVVKARK
IPATATTTHG NTKFIWRGPK VALPAIKDIQ KPNVIPDLSI KTIEASFYDD CNTTNDKIST
PTTSNNDNLE MNDSLVSVRS ADNQNTSLAL DSLKGLSKRN SLKDFTQRVI TKFISNIDTS
KNKKIKSTLL RDDVDNSPLG SNTPLPSSES KISGLKLQQK GLADENVISK RGNLIIKKNL
SIFGLPSNEI MSGSPSSYLG SSHTRTSSKL SNMSDKAAFI TEGQKSKHDD SNTYSLTQQL
KHRISETWVD IKSPSIPVSS EFANELLPIR WKDVWPKYVA RKYSKWRSFT TPAELPITIS
DFPSKDDFDR NFIFRNHSVT LNTDQEQYNQ TYKDLLRDMI YMRLLTGFQI CVGRQVEKIE
LSRESGESET VVNKYLDFNQ NDAFKLYLMI DSEIHRITCS SSGIIDVERY LRKDEANLFD
QVPSYIPLVK TRYESSFRDA MIDPLHVKRE SLNWNQIDQV LAGYGDNLID RKWHGFRAKY
VVLPTDIPPN TYSMVINGKS ETLNPEEIRV EGLRRLIGSI TRSRLRTEKE KKGRKTKREE
IQPEVMFYTG PLYNFINEQQ TSLESSAINF KDSIFVNDNN LLNRNVELSK LAYQIQRGED
RITLVNRKWH WKKHEKCFVG SEMVNWLIRN FSDIDTREDA IKYGQKVMKE GLFVHVLNKH
NFLDGHYFYQ FSPEYVMDTN KLEKTNSHRS TLSDPKQMLR KASTGSSNDP SAMTPFSSVV
PAISASNASV ADAKEPSRPI LMLSNSLVID VDPAGKSSKQ ESCTVHYDRV HNPDHCFHIR
LEWLTTTPKL IDDLVGNWSR LCERYGLKMI EIPWEELCTI PSVNPFHSFV EIKLAINPWE
DPEFKDRELF AKSKFYYHVY LLKASGFLLD NRASKFLQNQ DIEFDIMYSW GKPQFKYVQY
IHHTGAYVAE LRENGCLFLA PNNIYISRVN PGNIIGKIHS ASSSSLDAQK VILNFKSTCL
DYQKLRSIFL DAKEMWITGK IVED
