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KTU_DROWI
ID   KTU_DROWI               Reviewed;         828 AA.
AC   P0CU29; B4MPK3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Protein kintoun {ECO:0000255|HAMAP-Rule:MF_03069};
DE   AltName: Full=Dynein assembly factor 2, axonemal homolog {ECO:0000255|HAMAP-Rule:MF_03069};
DE   AltName: Full=PP1-interacting protein 20 {ECO:0000255|HAMAP-Rule:MF_03069};
GN   Name=Nop17l {ECO:0000255|HAMAP-Rule:MF_03069};
GN   Synonyms=Ppi20 {ECO:0000255|HAMAP-Rule:MF_03069}; ORFNames=GK27737;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Required for cytoplasmic pre-assembly of axonemal dyneins,
CC       thereby playing a central role in motility in cilia and flagella.
CC       Involved in pre-assembly of dynein arm complexes in the cytoplasm
CC       before intraflagellar transport loads them for the ciliary compartment.
CC       {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   -!- SUBUNIT: Interacts with Pp1alpha-96A, Pp1-87B, Pp1-13C and flw.
CC       {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW74042.1; Type=Erroneous gene model prediction; Note=The predicted gene GK21583 has been split into 2 genes: GK21583 and GK27737.; Evidence={ECO:0000305};
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DR   EMBL; CH963849; EDW74042.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015034407.1; XM_015178921.1.
DR   AlphaFoldDB; P0CU29; -.
DR   SMR; P0CU29; -.
DR   STRING; 7260.FBpp0250726; -.
DR   EnsemblMetazoa; FBtr0416438; FBpp0374625; FBgn0279603.
DR   GeneID; 26529739; -.
DR   KEGG; dwi:26529739; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   eggNOG; KOG4356; Eukaryota.
DR   OrthoDB; 943252at2759; -.
DR   PhylomeDB; P0CU29; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IEA:EnsemblMetazoa.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0060285; P:cilium-dependent cell motility; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03069; Kintoun; 1.
DR   InterPro; IPR034727; Kintoun.
DR   InterPro; IPR012981; PIH1_N.
DR   InterPro; IPR041442; PIH1D1/2/3_CS-like.
DR   Pfam; PF08190; PIH1; 1.
DR   Pfam; PF18201; PIH1_CS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..828
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365813"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          741..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..412
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..767
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..828
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
FT   MOD_RES         759
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ   SEQUENCE   828 AA;  94728 MW;  919D355364441D47 CRC64;
     MSGSTASARN KHSKGNLKHN NNKNKNNDEP IDITKDEFER IREALGKEEF RKLFFEYVDE
     IQDPANRKIY EDEITQLEKE RGVEVTFIHP QPGFVVKTSI DGEQKCFINI AGSPEIARPE
     SKLDINPDTG DRGLSWSIPM AQTASRDDCD AKNQQCKVFD VVFHPDALHL GQKNSQFRKC
     LIDTALDAVE REYEVNLDRT NLKYPKLDYK GIARPTVIRK LSKNPTDEEL EPHPLEHSFP
     TKPTAGEGEP KVLPMKVQKE QPKAPKFTEP KYSIKYSHDV DLSEYTNELD AKLQVTKPRA
     LVVEIELPLL RSTAECELDV TSKSIYLLSE RAGAKYRLKL DLPYTVDDKS GRARFDTDKR
     RLNIHLPVIR SNEPNLRLLS REDSGVELHS NSESPVEEEE DGEDEIEAEE EEEEVKTKVK
     PTSNPPSFLK SSLHYQLPGK FDCNLLDNCM AFTLHVANVQ PDSIEYVQEK RSLHLQFASM
     GNGYYPTHYA FYVALPAKES QLIIENVEAE AWDNNVILKL DLNKSSESIE SYLAGLDDQD
     LQDYAIHGQF KALKEAPVQE DKPGDIQFKR NDQEPSLEIT VSGLNAVEQQ EREEGEIEEA
     EEQQHKKSAS KKQRGKRNKK ERSLSESACV SLPTSVDSQP MATLKLPQRK QRSFSECHEQ
     QHHHHRGILK RFSRYDGNDS CSSIDDCSSS YPCSVEASRS FGGIPEEDSS LSESCKKTVR
     FNDHIMKQVF RLDSSILGQR KKNQKRRDCK LRAQQRRLSE GDSADYEEST ANKTQYCKYN
     KKHHHHHDSG LDLTRHNKKR ELAEEADNKN SLMFEMDDDD DDEDEDLI
 
 
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