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AIM21_VANPO
ID   AIM21_VANPO             Reviewed;         655 AA.
AC   A7TSV6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Altered inheritance of mitochondria protein 21;
GN   Name=AIM21; ORFNames=Kpol_328p3;
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   -!- FUNCTION: Involved in mitochondrial migration along actin filaments.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000250}. Note=Cortical actin patches. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AIM21 family. {ECO:0000305}.
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DR   EMBL; DS480526; EDO14651.1; -; Genomic_DNA.
DR   RefSeq; XP_001642509.1; XM_001642459.1.
DR   AlphaFoldDB; A7TSV6; -.
DR   STRING; 436907.A7TSV6; -.
DR   EnsemblFungi; EDO14651; EDO14651; Kpol_328p3.
DR   GeneID; 5542674; -.
DR   KEGG; vpo:Kpol_328p3; -.
DR   eggNOG; ENOG502S25J; Eukaryota.
DR   HOGENOM; CLU_418608_0_0_1; -.
DR   InParanoid; A7TSV6; -.
DR   OMA; FQQMFNQ; -.
DR   OrthoDB; 1635202at2759; -.
DR   PhylomeDB; A7TSV6; -.
DR   Proteomes; UP000000267; 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; Reference proteome.
FT   CHAIN           1..655
FT                   /note="Altered inheritance of mitochondria protein 21"
FT                   /id="PRO_0000399523"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   655 AA;  72848 MW;  3551E6763FFA4373 CRC64;
     MSEEDIPIIP SRPKKRATDS SLSSYTPNAS ADNLISPSPP IIPTSRPLSR AKTTDNINTD
     PVTTTGIATK EEVELPKVPT NRPTRRTTTQ ELNDLIDNTN HELEEIEAMV FKDDPNKMST
     GTNDDDIPHV PGNRPKITSK TTTTITKESL NDSDAAINNK NPSDEQTDSK VRPEVFKENL
     NEAKIAKTYD IMDMNNDIKE FVDNGNKTLS ENEDTVSTEH LDKVTTSDAS RVDEPPDTTL
     MKEPNTILDS EEVLASNDGQ VSINEKEITP TIPNRPSRKK EEQSESTSNV ESTPVIPVRP
     AKVKEIQSES STRLESSSSD EQEKANMVDS VSAVAERSTN SKDQIYTNSE RASKESLSEA
     KEPEIEKNDN QVHIETKHIP VIPERPKKNG PPPIPKKPSS RIAAFQKMIQ EQQAQSFNSL
     ASDVPTSERT ISEIEKDGDK LKTEQTMEEK NQINRSNAER TKFASSLNGL FALPGMAPLQ
     NLPAALTKKL SQPSESGFND SKEVNGGENI SNIRQKRARG PRGRKLPSKV AAVEKVNDSN
     NSNEIEVFRA WRIDSKPVTP SEEIVITQNQ LSDKQSVISS EDIITESETD KQITSSTEEF
     HKYTEQETDI TDRNQDVTAE VLEHDIEVQI EKEMEEQILA EDEPYEEVFS AETIG
 
 
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