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CD48B_ARATH
ID   CD48B_ARATH             Reviewed;         603 AA.
AC   Q9ZPR1;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cell division control protein 48 homolog B;
DE            Short=AtCDC48b;
GN   Name=CDC48B; OrderedLocusNames=At2g03670; ORFNames=F19B11.12;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Probably functions in cell division and growth processes.
CC       Interacts with certain SNAREs as part of specialized membrane fusion
CC       events where vesicles from the same organelle fuse (homotypic fusion)
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       phragmoplast {ECO:0000250}. Note=Primarily localized to the nucleus
CC       and, during cytokinesis, to the phragmoplast, a site where membrane
CC       vesicles are targeted in the deposition of new cell wall materials.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; AC006836; AAD20084.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05734.1; -; Genomic_DNA.
DR   EMBL; AY062443; AAL32521.1; -; mRNA.
DR   EMBL; BT008371; AAP37730.1; -; mRNA.
DR   PIR; A84451; A84451.
DR   RefSeq; NP_178463.1; NM_126415.6.
DR   AlphaFoldDB; Q9ZPR1; -.
DR   SMR; Q9ZPR1; -.
DR   BioGRID; 296; 7.
DR   STRING; 3702.AT2G03670.1; -.
DR   TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR   PaxDb; Q9ZPR1; -.
DR   PRIDE; Q9ZPR1; -.
DR   ProteomicsDB; 223908; -.
DR   EnsemblPlants; AT2G03670.1; AT2G03670.1; AT2G03670.
DR   GeneID; 814895; -.
DR   Gramene; AT2G03670.1; AT2G03670.1; AT2G03670.
DR   KEGG; ath:AT2G03670; -.
DR   Araport; AT2G03670; -.
DR   TAIR; locus:2044209; AT2G03670.
DR   eggNOG; KOG0730; Eukaryota.
DR   HOGENOM; CLU_000688_12_3_1; -.
DR   InParanoid; Q9ZPR1; -.
DR   OMA; CTRHPND; -.
DR   OrthoDB; 194195at2759; -.
DR   PhylomeDB; Q9ZPR1; -.
DR   PRO; PR:Q9ZPR1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZPR1; baseline and differential.
DR   Genevisible; Q9ZPR1; AT.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding; Nucleus; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..603
FT                   /note="Cell division control protein 48 homolog B"
FT                   /id="PRO_0000084580"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         327..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   603 AA;  65909 MW;  A3035450B30DB39D CRC64;
     MLETESSVCD NIAGNEKWRA EAEIGGNERA LQALRELIIF PFRYPLEART LGLKWPRGLL
     LYGPPGTGKT SLVRAVVQEC DAHLIVLSPH SVHRAHAGES EKVLREAFAE ASSHAVSDKP
     SVIFIDEIDV LCPRRDARRE QDVRIASQLF TLMDSNKPSS SAPRVVVVAS TNRVDAIDPA
     LRRAGRFDAL VEVSTPNEED RLKILQLYTK KVNLDPSVDL QAIAISCNGY VGADLEALCR
     EATISASKRS SDSLILTSQD FKIAKSVVGP SINRGITVEI PKVTWDDVGG LKDLKKKLQQ
     AVEWPIKHSA AFVKMGISPM RGILLHGPPG CSKTTLAKAA ANAAQASFFS LSCAELFSMY
     VGEGEALLRN TFQRARLASP SIIFFDEADV VACKRGDESS SNSSTVGERL LSTLLTEMDG
     LEEAKGILVL AATNRPYAID AALMRPGRFD LVLYVPPPDL EARFEILQVH TRNMTLGDDV
     DLRKIAEETD LFTGAELEGL CRESGTVSLR ENIAATAVFN RHFQTAKSSL KPALTIEEVE
     TYSSFRKAAK RSDSKPIPIN KKKATSTVFG FSWQLGVLSL LLLATGNYYF NHTKHELLVA
     SAT
 
 
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