位置:首页 > 蛋白库 > KTU_CHLRE
KTU_CHLRE
ID   KTU_CHLRE               Reviewed;         675 AA.
AC   B5BUZ8; B5U305;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 39.
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=Paralyzed flagella protein 13;
GN   Name=pf13;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-580,
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19052621; DOI=10.1038/nature07471;
RA   Omran H., Kobayashi D., Olbrich H., Tsukahara T., Loges N.T., Hagiwara H.,
RA   Zhang Q., Leblond G., O'Toole E., Hara C., Mizuno H., Kawano H.,
RA   Fliegauf M., Yagi T., Koshida S., Miyawaki A., Zentgraf H., Seithe H.,
RA   Reinhardt R., Watanabe Y., Kamiya R., Mitchell D.R., Takeda H.;
RT   "Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal dyneins.";
RL   Nature 456:611-616(2008).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=2974040; DOI=10.1083/jcb.107.6.2253;
RA   Kamiya R.;
RT   "Mutations at twelve independent loci result in absence of outer dynein
RT   arms in Chylamydomonas reinhardtii.";
RL   J. Cell Biol. 107:2253-2258(1988).
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, ECO:0000269|PubMed:19052621}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069,
CC       ECO:0000269|PubMed:19052621}. Note=Localizes exclusively in the
CC       cytoplasm but not in flagella. {ECO:0000269|PubMed:19052621}.
CC   -!- DISRUPTION PHENOTYPE: Paralyzed flagella, leading to a loss of
CC       motility. Electron microscopy image averages show that a density is
CC       missing from the inner dynein arms region in axonemes, which probably
CC       accounts for the paralyzed phenotype. {ECO:0000269|PubMed:19052621}.
CC   -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03069}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB455237; BAG69288.1; -; mRNA.
DR   EMBL; FJ160770; ACI01704.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5BUZ8; -.
DR   SMR; B5BUZ8; -.
DR   STRING; 3055.EDP00902; -.
DR   eggNOG; KOG4356; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IMP:GO_Central.
DR   GO; GO:0036158; P:outer dynein arm assembly; IMP:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm.
FT   CHAIN           1..675
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365815"
FT   REGION          98..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        409
FT                   /note="P -> A (in Ref. 1; ACI01704)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   675 AA;  69211 MW;  73121E2511B9E31F CRC64;
     MPGKEENDTL EKSLKELNLT SDEMTKFEKA FKDPEFIKLF EEYAKEVSDP KVKAETDAYL
     RQIEQQGRAE DVYGAGTQLI VPDPAGAVIK TKVVSSSASK KQQQEQEKQE KEQQQQAAGA
     GKPEGPGKQG ALPVGQKVFI NICTCDKLER YSLTDAQDPA TGRLRPKLTI PLSLGPVRQG
     ADKQGAPAAV YDFVVHPDSW TFAAGNAAGL ATLADTALDH VEQVGRCRLV RAWKRLNCRY
     KGTEGAAEPP VQCIRTSAAA AAGAAGEGAG GRVRPRPDVP GVPDLPGAKT APPAAAGAAA
     TAAAAAGAAE GGAGSSSRST FSFDKSRKAG GTEAAGAVAK QEATITDPAR PGYRHPDGAV
     TPEWGLLHRG EADLGEAWGD AGKGLAAGGR VPKELVVRVT LPDVSSAAPV DLDVGARCLA
     LTVPNRYRLS VQLPYGVDDA KGRAKFDKAR KVLEVTLPVV PPPAPPPGAA AAARAGLALI
     QELGGSEEAA EVKAEVEVEV ADVMGRDQEA AHAKSEAGAG AGVKSPHTAA AASSGAAPAP
     AAASEEEEEE DKEDGGPAAG SGGDPAAAAA AAGASSGREL TENERKWREL HARQQQEEQE
     QQEAAEAAAA AAAAAAEPSS RSQLTGTVAQ GGAAAAAESV AAAKQQVQQQ PVAAAAAPTA
     VLRPRLNREL AMELD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025