AIM21_YEAS1
ID AIM21_YEAS1 Reviewed; 651 AA.
AC B3LTK6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Altered inheritance of mitochondria protein 21;
GN Name=AIM21; ORFNames=SCRG_05176;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408055; EDV09487.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LTK6; -.
DR EnsemblFungi; EDV09487; EDV09487; SCRG_05176.
DR HOGENOM; CLU_418608_0_0_1; -.
DR Proteomes; UP000008335; 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..651
FT /note="Altered inheritance of mitochondria protein 21"
FT /id="PRO_0000399524"
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 /evidence="ECO:0000250"
FT REGION 549..651
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..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..643
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 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40563"
SQ SEQUENCE 651 AA; 71620 MW; 9E39C171D08CEF07 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 LDEKEKLPAN AESDPLSQLP QTNTVGNRKA ISEESLSPSE
AITNRDQNDT TEIQEQQMEE QMEVDMEREL SGGYEDVDSA LHSEEASFHS L
