AIM21_YEAST
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 03-AUG-2022, entry version 157.
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;
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=8; IntAct=EBI-25376, EBI-3437;
CC P40563; P38822: BZZ1; NbExp=7; IntAct=EBI-25376, EBI-3889;
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 -!- 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 BioGRID; 34994; 130.
DR ComplexPortal; CPX-3541; AIM21-TDA2 actin assembly regulator complex.
DR DIP; DIP-5096N; -.
DR IntAct; P40563; 20.
DR MINT; P40563; -.
DR STRING; 4932.YIR003W; -.
DR iPTMnet; P40563; -.
DR MaxQB; P40563; -.
DR PaxDb; P40563; -.
DR PRIDE; P40563; -.
DR EnsemblFungi; YIR003W_mRNA; YIR003W; YIR003W.
DR GeneID; 854819; -.
DR KEGG; sce:YIR003W; -.
DR SGD; S000001442; AIM21.
DR VEuPathDB; FungiDB:YIR003W; -.
DR eggNOG; ENOG502S25J; Eukaryota.
DR HOGENOM; CLU_418608_0_0_1; -.
DR InParanoid; P40563; -.
DR OMA; FQQMFNQ; -.
DR BioCyc; YEAST:G3O-31424-MON; -.
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 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..671
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
