AIM21_YEAS7
ID AIM21_YEAS7 Reviewed; 679 AA.
AC A6ZVS1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Altered inheritance of mitochondria protein 21;
GN Name=AIM21; ORFNames=SCY_2787;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Involved in mitochondrial migration along actin filaments.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ribosomes. Interacts with ABP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Cortical actin patches. Localizes at the shmoo tip.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AIM21 family. {ECO:0000305}.
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DR EMBL; AAFW02000124; EDN61496.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZVS1; -.
DR EnsemblFungi; EDN61496; EDN61496; SCY_2787.
DR HOGENOM; CLU_418608_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR InterPro; IPR021582; Aim21.
DR Pfam; PF11489; Aim21; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Phosphoprotein.
FT CHAIN 1..679
FT /note="Altered inheritance of mitochondria protein 21"
FT /id="PRO_0000399526"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..396
FT /note="Interaction with SH3 domain of ABP1"
FT /evidence="ECO:0000250"
FT REGION 548..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 116..149
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..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..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:0000250|UniProtKB:P40563"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
SQ SEQUENCE 679 AA; 74587 MW; 8F3E1E5EF029495A CRC64;
MPSEVTPKVP ERPSRRKTSE LFPLSGSESG DIKANSEPPT PAGTPNVPTR RPILKAKTMT
SFESGMDQES LPKVPLQRPV RRSTTEELNN VMNNTSKELE EIESLISKHN IHSVSRKKSP
TSVQEGKAAA IHQNGQRSAS DNKTSTNPSP LEKNEHKGDE GNESAISPSN SVNKSNNEVT
EHSDSEDLTE KQKVHAALDN EAGDGSHFEE KLIPGDMKVP VDVSKDVEEG SLNALPPSGI
TESDDKAEKF TKHPESSLEE LQKHQEQQEE KIFQNPTDEE STTSLNEKQE GKDNMEVNSQ
PQGPSDTETV IAATSSNVPS QIASEEENDV PVIPRSRPKK DFEAHVQKEE LPNTQEKLVS
EECDSTLIST EEESKIPKIP SERPKRRAPP PVPKKPSSRI AAFQEMLQKQ QQQDLHNNGN
SSATTASADI AKKHTDSSIT SDTTKADFTS KLNGLFALPG MVNPGQLPPS LEKKLSSPDT
ESKLGTQDQS QAKTGPLGGT RRGRGPRGRK LPSKVASVEK IEEDDNTNKI EIFNNWNVSS
SFSKEKILMD TTPGEQAERA LDEKSKSIPE EQREQSPNKM EAALCPFELD EQEKLPANAE
SDPLSQLPQT NAVGNRKAIS EESLSPSEAI ANRDQNDTTE IQEQQMEDQM EVDMERELSG
GYEDVDSALH SEEASFHSL
