ID   AIM21_YEAST             Reviewed;         679 AA.
AC   P40563; D6VVT3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 174.
DE   RecName: Full=Altered inheritance of mitochondria protein 21;
GN   Name=AIM21; OrderedLocusNames=YIR003W; ORFNames=YIB3W;
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=7762303; DOI=10.1002/yea.320110109;
RA   Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA   Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT   "Nucleotide sequence and analysis of the centromeric region of yeast
RT   chromosome IX.";
RL   Yeast 11:61-78(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870; DOI=10.1038/387s084;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
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   [4]
RP   INTERACTION WITH ABP1.
RX   PubMed=11668184; DOI=10.1074/jbc.m109848200;
RA   Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K.,
RA   Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.;
RT   "Unusual binding properties of the SH3 domain of the yeast actin-binding
RT   protein Abp1: structural and functional analysis.";
RL   J. Biol. Chem. 277:5290-5298(2002).
RN   [5]
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   [6]
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   [7]
RP   INTERACTION WITH ABP1.
RX   PubMed=14737190; DOI=10.1371/journal.pbio.0020014;
RA   Landgraf C., Panni S., Montecchi-Palazzi L., Castagnoli L.,
RA   Schneider-Mergener J., Volkmer-Engert R., Cesareni G.;
RT   "Protein interaction networks by proteome peptide scanning.";
RL   PLoS Biol. 2:94-103(2004).
RN   [8]
RP   COPURIFICATION WITH RIBOSOMAL COMPLEXES, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16702403; DOI=10.1101/gad.1422006;
RA   Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT   "Systematic identification and functional screens of uncharacterized
RT   proteins associated with eukaryotic ribosomal complexes.";
RL   Genes Dev. 20:1294-1307(2006).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17164236; DOI=10.1074/jbc.m610575200;
RA   Fairn G.D., Macdonald K., McMaster C.R.;
RT   "A chemogenomic screen in Saccharomyces cerevisiae uncovers a primary role
RT   for the mitochondria in farnesol toxicity and its regulation by the Pkc1
RT   pathway.";
RL   J. Biol. Chem. 282:4868-4874(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-36; THR-58; THR-85;
RP   SER-183; THR-277; SER-625 AND SER-678, AND IDENTIFICATION BY MASS
RP   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   [11]
RP   IDENTIFICATION BY 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-231; THR-277;
RP   SER-324; SER-576; SER-620 AND SER-671, AND IDENTIFICATION BY MASS
RP   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   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19053807; DOI=10.1021/pr800524g;
RA   Narayanaswamy R., Moradi E.K., Niu W., Hart G.T., Davis M., McGary K.L.,
RA   Ellington A.D., Marcotte E.M.;
RT   "Systematic definition of protein constituents along the major polarization
RT   axis reveals an adaptive reuse of the polarization machinery in pheromone-
RT   treated budding yeast.";
RL   J. Proteome Res. 8:6-19(2009).
RN   [14]
RP   FUNCTION.
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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-36; THR-58; SER-70;
RP   THR-85; SER-104; SER-183; SER-206; THR-277; SER-284; THR-552; SER-576;
RP   SER-620; SER-623; SER-627; SER-667; SER-671; SER-675 AND SER-678, 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   -!- FUNCTION: Involved in mitochondrial migration along actin filaments.
CC       {ECO:0000269|PubMed:19300474}.
CC   -!- SUBUNIT: Interacts with ribosomes. Interacts with ABP1.
CC       {ECO:0000269|PubMed:11668184, ECO:0000269|PubMed:14737190}.
CC   -!- INTERACTION:
CC       P40563; P15891: ABP1; NbExp=10; IntAct=EBI-25376, EBI-2036;
CC       P40563; P47068: BBC1; NbExp=9; IntAct=EBI-25376, EBI-3437;
CC       P40563; P38822: BZZ1; NbExp=7; IntAct=EBI-25376, EBI-3889;
CC       P40563; P13517: CAP2; NbExp=3; IntAct=EBI-25376, EBI-4013;
CC       P40563; P38753: HSE1; NbExp=4; IntAct=EBI-25376, EBI-1382;
CC       P40563; P53281: LSB1; NbExp=5; IntAct=EBI-25376, EBI-23329;
CC       P40563; P43603: LSB3; NbExp=2; IntAct=EBI-25376, EBI-22980;
CC       P40563; P36006: MYO3; NbExp=3; IntAct=EBI-25376, EBI-11670;
CC       P40563; Q04439: MYO5; NbExp=2; IntAct=EBI-25376, EBI-11687;
CC       P40563; Q12163: NBP2; NbExp=4; IntAct=EBI-25376, EBI-34713;
CC       P40563; P32790: SLA1; NbExp=4; IntAct=EBI-25376, EBI-17313;
CC       P40563; P40045: TDA2; NbExp=3; IntAct=EBI-25376, EBI-22573;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19053807}.
CC       Note=Cortical actin patches. Localizes at the shmoo tip.
CC   -!- DISRUPTION PHENOTYPE: Increases the sensitivity to farnesol.
CC       {ECO:0000269|PubMed:17164236}.
CC   -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the AIM21 family. {ECO:0000305}.
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DR   EMBL; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z38062; CAA86205.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08549.1; -; Genomic_DNA.
DR   PIR; S48437; S48437.
DR   RefSeq; NP_012268.3; NM_001179525.3.
DR   AlphaFoldDB; P40563; -.
DR   SMR; P40563; -.
DR   BioGRID; 34994; 149.
DR   ComplexPortal; CPX-3541; AIM21-TDA2 actin assembly regulator complex.
DR   DIP; DIP-5096N; -.
DR   FunCoup; P40563; 134.
DR   IntAct; P40563; 23.
DR   STRING; 4932.YIR003W; -.
DR   GlyGen; P40563; 1 site.
DR   iPTMnet; P40563; -.
DR   PaxDb; 4932-YIR003W; -.
DR   PeptideAtlas; P40563; -.
DR   EnsemblFungi; YIR003W_mRNA; YIR003W; YIR003W.
DR   GeneID; 854819; -.
DR   KEGG; sce:YIR003W; -.
DR   AGR; SGD:S000001442; -.
DR   SGD; S000001442; AIM21.
DR   VEuPathDB; FungiDB:YIR003W; -.
DR   eggNOG; ENOG502S25J; Eukaryota.
DR   HOGENOM; CLU_418608_0_0_1; -.
DR   InParanoid; P40563; -.
DR   OMA; AFHNMLQ; -.
DR   OrthoDB; 3995855at2759; -.
DR   BioCyc; YEAST:G3O-31424-MONOMER; -.
DR   BioGRID-ORCS; 854819; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P40563; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40563; protein.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0015629; C:actin cytoskeleton; HDA:SGD.
DR   GO; GO:0110131; C:Aim21-Tda2 complex; IPI:SGD.
DR   GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR   GO; GO:0034642; P:mitochondrion migration along actin filament; IMP:SGD.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:SGD.
DR   GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IDA:ComplexPortal.
DR   InterPro; IPR021582; Aim21.
DR   Pfam; PF11489; Aim21; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..679
FT                   /note="Altered inheritance of mitochondria protein 21"
FT                   /id="PRO_0000203003"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..396
FT                   /note="Interaction with SH3 domain of ABP1"
FT   REGION          549..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..119
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..512
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         58
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         85
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         277
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         552
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         576
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         620
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         623
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         627
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   679 AA;  74763 MW;  9DF79500375339E7 CRC64;
     MPSEVTPKVP ERPSRRKTSE LFPLSGSESG DIKANSEPPT PAGTPNVPTR RPILKAKTMT
     SFESGMDQES LPKVPLQRPV RRSTTEELNN VMNNTSKELE EIESLISKHN IHNVSRKKSP
     TSVEEGKVAA IHQNGQRSAS DNKTSTNPSP LEKNEHEGAE GNESAISPSN LVNKSNNEVT
     EHSDSEDLTE KQKVHAALDN EAGDRSHFEE KLIPGDMKVQ VDVSKDVEEG SLNALPPSGI
     TESDDKAEKF TKHPESSLEE LQKHQEQQEE KIFQNPTDEE STTSLNEKQE GKDNMEVNSQ
     PQGPSDTETV IAATSSNVPS QIASEEENDV PVIPRSRPKK DFEAHVQKEE LPNTQEKRVS
     EECDSTLIST EEESKIPKIP SERPKRRAPP PVPKKPSSRI AAFQEMLQKQ QQQDLHNNGN
     SSATTASADI AKKHTDSSIT SDTTKADFTS KLNGLFALPG MVNPGQLPPS LEKKLSSPDT
     ESKLGPQDQS QAKTGPLGGT RRGRGPRGRK LPSKVASVEK IEEDDNTNKI EIFNNWNVSS
     SFSKEKVLID TTPGEQAERA LDEKSKSIPE EQREQSPNKM EAALCPFELD EKEKLPANAE
     SDPLSQLPQT NAVGNRKAIS EESLSPSEAI ANRDQNDTTE IQEQQMEDQM EVDMERELSG
     GYEDVDSALH SEEASFHSL
//