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MUPS1_ARATH
ID   MUPS1_ARATH             Reviewed;         377 AA.
AC   F4KDF5; C9X3W2; Q9FJM6;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 2.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Protein MULTIPOLAR SPINDLE 1 {ECO:0000303|PubMed:19500302};
DE   AltName: Full=Protein PUTATIVE RECOMBINATION INITIATION DEFECTS 2 {ECO:0000303|PubMed:19763177};
DE            Short=AtPRD2 {ECO:0000303|PubMed:19763177};
GN   Name=MPS1 {ECO:0000303|PubMed:19500302};
GN   Synonyms=PRD2 {ECO:0000303|PubMed:19763177};
GN   OrderedLocusNames=At5g57880 {ECO:0000312|Araport:AT5G57880};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia, and cv. Wassilewskija; TISSUE=Flower bud;
RX   PubMed=19763177; DOI=10.1371/journal.pgen.1000654;
RA   De Muyt A., Pereira L., Vezon D., Chelysheva L., Gendrot G., Chambon A.,
RA   Laine-Choinard S., Pelletier G., Mercier R., Nogue F., Grelon M.;
RT   "A high throughput genetic screen identifies new early meiotic
RT   recombination functions in Arabidopsis thaliana.";
RL   PLoS Genet. 5:E1000654-E1000654(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=19500302; DOI=10.1111/j.1365-313x.2009.03929.x;
RA   Jiang H., Wang F.-F., Wu Y.-T., Zhou X., Huang X.-Y., Zhu J., Gao J.-F.,
RA   Dong R.-B., Cao K.-M., Yang Z.-N.;
RT   "MULTIPOLAR SPINDLE 1 (MPS1), a novel coiled-coil protein of Arabidopsis
RT   thaliana, is required for meiotic spindle organization.";
RL   Plant J. 59:1001-1010(2009).
CC   -!- FUNCTION: Involved in meiotic spindle organization in meiocytes thus
CC       regulating chromosome segregation (PubMed:19500302). Required for
CC       formation of meiotic DNA double-strand breaks (DSBs) during early
CC       recombination processes (PubMed:19763177).
CC       {ECO:0000269|PubMed:19500302, ECO:0000269|PubMed:19763177}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000305|PubMed:19500302}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, inflorescences
CC       and seedlings. Strongly expressed in meiocytes.
CC       {ECO:0000269|PubMed:19500302}.
CC   -!- DEVELOPMENTAL STAGE: In anthers, predominantly detected in meiocytes
CC       and tapetal cells from stage 5 to early stage 7, with highest levels at
CC       stage 6, the time of male meiosis. In ovules, present in female
CC       meiocytes and embryo sacs. {ECO:0000269|PubMed:19500302}.
CC   -!- DISRUPTION PHENOTYPE: Defective in early recombination processes
CC       leading to the absence of meiotic DNA double-strand break (DSB)
CC       formation (PubMed:19763177). Reduced silique elongation associated with
CC       fertility defects involving both male and female gametophyte abortion
CC       due to aberrant meiotic products (PubMed:19763177, PubMed:19500302).
CC       Produced multiple uneven spores aborted in later stages during anther
CC       development, due to abnormal chromosome segregation and unequal bipolar
CC       or multipolar spindles in meiocytes (PubMed:19500302).
CC       {ECO:0000269|PubMed:19500302, ECO:0000269|PubMed:19763177}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB08858.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FN356233; CAX83745.1; -; mRNA.
DR   EMBL; AB013396; BAB08858.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96966.2; -; Genomic_DNA.
DR   RefSeq; NP_001318822.1; NM_001345277.1.
DR   AlphaFoldDB; F4KDF5; -.
DR   SMR; F4KDF5; -.
DR   STRING; 3702.AT5G57880.1; -.
DR   PaxDb; F4KDF5; -.
DR   PRIDE; F4KDF5; -.
DR   ProteomicsDB; 238904; -.
DR   EnsemblPlants; AT5G57880.1; AT5G57880.1; AT5G57880.
DR   GeneID; 835898; -.
DR   Gramene; AT5G57880.1; AT5G57880.1; AT5G57880.
DR   KEGG; ath:AT5G57880; -.
DR   Araport; AT5G57880; -.
DR   TAIR; locus:2174363; AT5G57880.
DR   eggNOG; ENOG502QVCM; Eukaryota.
DR   HOGENOM; CLU_044141_0_0_1; -.
DR   InParanoid; F4KDF5; -.
DR   OMA; SNMFIMI; -.
DR   OrthoDB; 965665at2759; -.
DR   PRO; PR:F4KDF5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KDF5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0051026; P:chiasma assembly; IMP:TAIR.
DR   GO; GO:0007059; P:chromosome segregation; IMP:TAIR.
DR   GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR   GO; GO:0007140; P:male meiotic nuclear division; IMP:TAIR.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:TAIR.
DR   GO; GO:0000212; P:meiotic spindle organization; IMP:TAIR.
DR   GO; GO:0048236; P:plant-type sporogenesis; IMP:TAIR.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
DR   InterPro; IPR037500; Msp1.
DR   PANTHER; PTHR35768; PTHR35768; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Developmental protein; DNA recombination; Meiosis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..377
FT                   /note="Protein MULTIPOLAR SPINDLE 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000438412"
FT   MOTIF           117..124
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   CONFLICT        31
FT                   /note="Q -> H (in Ref. 1; CAX83745)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="V -> F (in Ref. 1; CAX83745)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305
FT                   /note="A -> AE (in Ref. 1; CAX83745)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  43661 MW;  6B50594A96D19E8D CRC64;
     MSSSVAEANH TEKEESLRLA IAVSLLRSKF QNHQSSSSTS RCYVSSESDA LRWKQKAKER
     KKEIIRLQED LKDAESSFHR DLFPANASCK CYFFDNLGVF SGRRIGEASE SRFNDVLRRR
     FLRLARRRSR RKLTRSSQRL QPSEPDYEEE AEHLRISIDF LLELSEADSN DSNFSNWSHQ
     AVDFIFASLK KLISMGRNLE SVEESISFMI TQLITRMCTP VKGNEVKQLE TSVGFYVQHL
     IRKLGSEPFI GQRAIFAISQ RISILAENLL FMDPFDESFP EMDECMFILI QLIEFLICDY
     LLPWANEAFD NVMFEEWIAS VVHARKAVKA LEERNGLYLL YMDRVTGELA KRVGQITSFR
     EVEPAILDKI LAYQEIE
 
 
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