ID   AIM3_VANPO              Reviewed;         915 AA.
AC   A7TRW3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Altered inheritance of mitochondria protein 3;
GN   Name=AIM3; ORFNames=Kpol_376p13;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Note=Localizes within detergent-insoluble
CC       glycolipid-enriched membranes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AIM3 family. {ECO:0000305}.
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DR   EMBL; DS480489; EDO15000.1; -; Genomic_DNA.
DR   RefSeq; XP_001642858.1; XM_001642808.1.
DR   AlphaFoldDB; A7TRW3; -.
DR   STRING; 436907.A7TRW3; -.
DR   PRIDE; A7TRW3; -.
DR   EnsemblFungi; EDO15000; EDO15000; Kpol_376p13.
DR   GeneID; 5543044; -.
DR   KEGG; vpo:Kpol_376p13; -.
DR   eggNOG; ENOG502S02E; Eukaryota.
DR   HOGENOM; CLU_324433_0_0_1; -.
DR   InParanoid; A7TRW3; -.
DR   OMA; DNPFRRY; -.
DR   OrthoDB; 1315070at2759; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0030479; C:actin cortical patch; IEA:InterPro.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR   InterPro; IPR031370; Aim3.
DR   Pfam; PF17096; AIM3; 1.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome.
FT   CHAIN           1..915
FT                   /note="Altered inheritance of mitochondria protein 3"
FT                   /id="PRO_0000399607"
FT   REGION          30..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..244
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..416
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..690
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..852
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..915
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   915 AA;  100922 MW;  0C87255ADB127C65 CRC64;
     MSDFWDKNKG SIASGFKSAG KYTYQGAKYV GKSGYNASKN HYNKSKEQRD KRDKKKGKKK
     NGDDEYSGDD SYSDDDSSYS TASIPVSSMK DPNSFPPPPL KPQQVQATSS SHSVEQYPAS
     AGVPQQQLRQ LPPQPISATQ QPAWPQQPAA NQYDGQVSAP DQSQMQYGGQ TQYQQPPAMQ
     QPPAMQQHPA MQQPPDMQQP PDMQQPPAMQ QPPAMQQPPA MQQPPAMQQP PAMQQPPAMQ
     QPPAMQQPPN MVGQPSNQFQ LPEPQQRQTP PLPPVTSQPY GEAQNQAQNQ GQFQATPLSQ
     LQNMQQEETT RSVPNAYDPQ QTYSQPPSIP QRHTPQPVVN QVQYQESQSS IPQVNQDYYG
     QQPEVNQQNN LMNRSIPPPM QQQPPMQQQP PMQQQPPMQQ QPPMQQQPPM PPRGPSLAAP
     AYGGTPNINA NAQLPASSGI TVKPYNPDEV QTREPLALKV DIGNLPPPPT HRDRGTETRP
     PSEPKPSPAI RNPISAVPAV SRASTLDSSS VPVNSIPAHQ NQPIYMQDNS SSVESFPDEE
     TSDFNNLPPP PPPNRRVTEQ NLEKSAKSST IGQEQRNDSK TEPPRAAIVG SFNSNPTINF
     EPPPKPFRPV VNSDRKSESP VQPQPLARSA NGPPALPSRR GTQTSFESHP TPPSMESSTP
     SLPNRLNRNE PPIAEKPVSS FPPPPKPFRR VEAESPSHSQ VNDSNKESSA PRTHNFGNDE
     DEDISAPVKW NPPAELLERK SEIDVKKGKK APPPVVKPKP KNLSSVNKVN PEYEGHKPVG
     SMNQNQNQNQ NQNSLNSITD ELTHVHLRKT GISLEDEGKK FGGNDTSIDD IPPKFEKIET
     SRKPKAPPAV PKKKDSIRGA PPPVPAKKKN LNATPQPPPS RRNNNVNNDN DDDDSNPFEK
     YMRDAVPAEE NRLRK