ID   AIM3_YEAST              Reviewed;         947 AA.
AC   P38266; D6VQA7;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Altered inheritance of mitochondria protein 3;
GN   Name=AIM3; OrderedLocusNames=YBR108W; ORFNames=YBR0901;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7900426; DOI=10.1002/yea.320101014;
RA   Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT   "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL   Yeast 10:1363-1381(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 515.
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   [4]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [5]
RP   INTERACTION WITH RVS167, AND SUBCELLULAR LOCATION.
RX   PubMed=15561700; DOI=10.1074/jbc.m412454200;
RA   Germann M., Swain E., Bergman L., Nickels J.T. Jr.;
RT   "Characterizing the sphingolipid signaling pathway that remediates defects
RT   associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and
RT   Rvs167p.";
RL   J. Biol. Chem. 280:4270-4278(2005).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-729, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; THR-729 AND THR-861, 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   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA   Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA   Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA   Troyanskaya O.G., Caudy A.A.;
RT   "Computationally driven, quantitative experiments discover genes required
RT   for mitochondrial biogenesis.";
RL   PLoS Genet. 5:E1000407-E1000407(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-58 AND SER-64, AND
RP   IDENTIFICATION BY 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).
CC   -!- SUBUNIT: Interacts with RVS167. {ECO:0000269|PubMed:15561700}.
CC   -!- INTERACTION:
CC       P38266; P38822: BZZ1; NbExp=2; IntAct=EBI-21584, EBI-3889;
CC       P38266; P53281: LSB1; NbExp=3; IntAct=EBI-21584, EBI-23329;
CC       P38266; P43603: LSB3; NbExp=4; IntAct=EBI-21584, EBI-22980;
CC       P38266; P39743: RVS167; NbExp=6; IntAct=EBI-21584, EBI-14500;
CC       P38266; P32793: YSC84; NbExp=5; IntAct=EBI-21584, EBI-24460;
CC   -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000269|PubMed:15561700};
CC       Peripheral membrane protein {ECO:0000269|PubMed:15561700}.
CC       Note=Localize within detergent-insoluble glycolipid-enriched membranes.
CC   -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC       {ECO:0000269|PubMed:19300474}.
CC   -!- SIMILARITY: Belongs to the AIM3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA55611.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA85063.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X78993; CAA55611.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z35977; CAA85063.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006936; DAA07227.2; -; Genomic_DNA.
DR   PIR; S48273; S48273.
DR   RefSeq; NP_009666.3; NM_001178456.2.
DR   AlphaFoldDB; P38266; -.
DR   SMR; P38266; -.
DR   BioGRID; 32812; 206.
DR   DIP; DIP-1602N; -.
DR   IntAct; P38266; 16.
DR   MINT; P38266; -.
DR   STRING; 4932.YBR108W; -.
DR   GlyGen; P38266; 25 sites, 1 O-linked glycan (25 sites).
DR   iPTMnet; P38266; -.
DR   MaxQB; P38266; -.
DR   PaxDb; 4932-YBR108W; -.
DR   PeptideAtlas; P38266; -.
DR   EnsemblFungi; YBR108W_mRNA; YBR108W; YBR108W.
DR   GeneID; 852405; -.
DR   KEGG; sce:YBR108W; -.
DR   AGR; SGD:S000000312; -.
DR   SGD; S000000312; AIM3.
DR   VEuPathDB; FungiDB:YBR108W; -.
DR   eggNOG; ENOG502S02E; Eukaryota.
DR   HOGENOM; CLU_324433_0_0_1; -.
DR   InParanoid; P38266; -.
DR   OMA; DNPFRRY; -.
DR   OrthoDB; 1969643at2759; -.
DR   BioCyc; YEAST:G3O-29070-MONOMER; -.
DR   BioGRID-ORCS; 852405; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P38266; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38266; Protein.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0000147; P:actin cortical patch assembly; IGI:SGD.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IMP:SGD.
DR   InterPro; IPR031370; Aim3.
DR   Pfam; PF17096; AIM3; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..947
FT                   /note="Altered inheritance of mitochondria protein 3"
FT                   /id="PRO_0000202486"
FT   REGION          1..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..300
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..399
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..707
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..874
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         729
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         861
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        515
FT                   /note="V -> A (in Ref. 1; CAA55611 and 2; CAA85063)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   947 AA;  103863 MW;  CD624428B29DA272 CRC64;
     MGFWENNKDS ITSGLKSAGK YGYQGTKYVA KTGYKASKKH YNNSKARRER KSGKKNSSDE
     EYDSEDEMEY ERKPTDIRSL KDPKSFPPPP LKPGQKTYTG QQQQQMPNGQ ASYAFQGAYQ
     GQPGAGSTEQ SQYAQPQYNQ YPQQQLQQGV MPQQQQLQQG VVPQQPPIYG EQVPPYGSNS
     NATSYQSLPQ QNQPQNAIPS QVSLNSASQQ STGFVSQNLQ YGTQSSNPAP SPSFQNGLQC
     HQQPQYVSHG STNLGQSQFP SGQQQQPTTQ FGQQVLPSPA QPQQQQQGQP LPPPRGQVIL
     PAPGEPLSNG FGQQQQQQQQ QQQPLNQNNA LLPQMNVEGV SGMAAVQPVY GQAMSSTTNM
     QDSNPSYGAS PMQGQPPVGG QPPVPVRMQP QPPQPMQQGN IYPIEPSLDS TGSTPHFEVT
     PFDPDAPAPK PKIDIPTVDV SSLPPPPTHR DRGAVVHQEP APSGKIQPNT TSSAASLPAK
     HSRTTTADNE RNSGNKENDE STSKSSILGH YDVDVNIMPP PKPFRHGLDS VPSEHTTKNA
     PERAVPILPP RNNVEPPPPP SRGNFERTES VLSTNAANVQ EDPISNFLPP PKPFRHTETK
     QNQNSKASPV EMKGEVLPGH PSEEDRNVEP SLVPQSKPQS QSQFRRAHME TQPIQNFQPP
     PKPFRRSQSS NSSDSSYTID GPEANHGRGR GRIAKHHDGD EYNPKSENST ENGRLGDAPN
     SFIRKRAPTP PAPSRSEKLH EGTITSEVDS SKDANKYEKS IPPVTSSIQA QQSTKKAPPP
     VVKPKPRNFS LKANEYPKEL TREATGQDEV LNSITNELSH IKLRKTNVNL EKLGGSKKVK
     DSSPVPSDLD EKYVSASGSI TPPRPPPSRS SPKKVPPVVP KKNDNLKKKP PVVPKKKPLL
     KSLEPRPIEM ERAYSGDISA ADDNLNPFER YKRNVVPQED DRLHKLK
//