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ARP6_ARATH
ID   ARP6_ARATH              Reviewed;         421 AA.
AC   Q8LGE3; Q8GZL0; Q8GZL1; Q8GZL2; Q8GZL3; Q8GZL4; Q8GZL5; Q8GZL6; Q8GZL7;
AC   Q8GZL8; Q8GZL9; Q8GZM0; Q8GZM1; Q8GZM2; Q8GZM3; Q8GZM4; Q8LKR0; Q949Z7;
AC   Q9SRK2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Actin-related protein 6;
DE   AltName: Full=Protein EARLY IN SHORT DAYS 1;
DE   AltName: Full=Protein SUPPRESSOR OF FRIGIDA 3;
GN   Name=ARP6; Synonyms=ESD1, SUF3; OrderedLocusNames=At3g33520;
GN   ORFNames=T4P3.8;
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], IDENTIFICATION, TISSUE SPECIFICITY, AND GENE
RP   FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11891255; DOI=10.1104/pp.010906;
RA   McKinney E.C., Kandasamy M.K., Meagher R.B.;
RT   "Arabidopsis contains ancient classes of differentially expressed actin-
RT   related protein genes.";
RL   Plant Physiol. 128:997-1007(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 230-312, AND VARIANTS 230-PRO-PRO-231;
RP   PRO-231; SER-248; ARG-250; GLU-253; ARG-263; GLU-271; ASP-280; GLU-290;
RP   ILE-301; 308-SER--ILE-311; SER-310 AND VAL-311.
RC   STRAIN=cv. Aa-0, cv. Ba-1, cv. Cl-0, cv. Columbia, cv. Di-0, cv. En-2,
RC   cv. Goe-2, cv. Gre-0, cv. Hi-0, cv. Kas-1, cv. Kil-0, cv. Lip-0, cv. Oy-0,
RC   cv. Ri-0, and cv. Yo-0;
RX   PubMed=12566397; DOI=10.1101/gr.593403;
RA   Hall S.E., Kettler G., Preuss D.;
RT   "Centromere satellites from Arabidopsis populations: maintenance of
RT   conserved and variable domains.";
RL   Genome Res. 13:195-205(2003).
RN   [7]
RP   REVIEW, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15063870; DOI=10.1016/j.tplants.2004.02.004;
RA   Kandasamy M.K., Deal R.B., McKinney E.C., Meagher R.B.;
RT   "Plant actin-related proteins.";
RL   Trends Plant Sci. 9:196-202(2004).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16141450; DOI=10.1105/tpc.105.035196;
RA   Deal R.B., Kandasamy M.K., McKinney E.C., Meagher R.B.;
RT   "The nuclear actin-related protein ARP6 is a pleiotropic developmental
RT   regulator required for the maintenance of FLOWERING LOCUS C expression and
RT   repression of flowering in Arabidopsis.";
RL   Plant Cell 17:2633-2646(2005).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16155178; DOI=10.1105/tpc.105.035485;
RA   Choi K., Kim S., Kim S.Y., Kim M., Hyun Y., Lee H., Choe S., Kim S.-G.,
RA   Michaels S., Lee I.;
RT   "SUPPRESSOR OF FRIGIDA3 encodes a nuclear ACTIN-RELATED PROTEIN6 required
RT   for floral repression in Arabidopsis.";
RL   Plant Cell 17:2647-2660(2005).
RN   [10]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16495307; DOI=10.1242/dev.02301;
RA   Martin-Trillo M., Lazaro A., Poethig R.S., Gomez-Mena C., Pineiro M.A.,
RA   Martinez-Zapater J.M., Jarillo J.A.;
RT   "EARLY IN SHORT DAYS 1 (ESD1) encodes ACTIN-RELATED PROTEIN 6 (AtARP6), a
RT   putative component of chromatin remodelling complexes that positively
RT   regulates FLC accumulation in Arabidopsis.";
RL   Development 133:1241-1252(2006).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SWC6 AND PIE1, AND
RP   SUBUNIT.
RX   PubMed=17470967; DOI=10.1242/dev.001891;
RA   Choi K., Park C., Lee J., Oh M., Noh B., Lee I.;
RT   "Arabidopsis homologs of components of the SWR1 complex regulate flowering
RT   and plant development.";
RL   Development 134:1931-1941(2007).
RN   [12]
RP   FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN THE SWR1 COMPLEX, AND
RP   INTERACTION WITH H2A.F/Z PROTEINS.
RX   PubMed=17220196; DOI=10.1105/tpc.106.048447;
RA   Deal R.B., Topp C.N., McKinney E.C., Meagher R.B.;
RT   "Repression of flowering in Arabidopsis requires activation of FLOWERING
RT   LOCUS C expression by the histone variant H2A.Z.";
RL   Plant Cell 19:74-83(2007).
RN   [13]
RP   INTERACTION WITH PIE1 AND SWC6.
RX   PubMed=17142478; DOI=10.1104/pp.106.092270;
RA   March-Diaz R., Garcia-Dominguez M., Florencio F.J., Reyes J.C.;
RT   "SEF, a new protein required for flowering repression in Arabidopsis,
RT   interacts with PIE1 and ARP6.";
RL   Plant Physiol. 143:893-901(2007).
RN   [14]
RP   FUNCTION.
RX   PubMed=17988222; DOI=10.1111/j.1365-313x.2007.03361.x;
RA   March-Diaz R., Garcia-Dominguez M., Lozano-Juste J., Leon J.,
RA   Florencio F.J., Reyes J.C.;
RT   "Histone H2A.Z and homologues of components of the SWR1 complex are
RT   required to control immunity in Arabidopsis.";
RL   Plant J. 53:475-487(2008).
CC   -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant H2A.F/Z leading
CC       to transcriptional regulation of selected genes (e.g. FLC) by chromatin
CC       remodeling. Binds to the promoter region of FLC chromatin. Required for
CC       the activation of FLC and FLC/MAF genes expression to levels that
CC       inhibit flowering, through both histone H3 and H4 acetylation and
CC       methylation mechanisms. Involved in several developmental processes
CC       including organization of plant organs, leaves formation, flowering
CC       time repression, and fertility. Modulates photoperiod-dependent
CC       epidermal leaves cell development; promotes cell division in long days,
CC       and cell expansion/division in short days. May be involved in the
CC       regulation of pathogenesis-related proteins (PRs).
CC       {ECO:0000269|PubMed:16141450, ECO:0000269|PubMed:16155178,
CC       ECO:0000269|PubMed:16495307, ECO:0000269|PubMed:17220196,
CC       ECO:0000269|PubMed:17470967, ECO:0000269|PubMed:17988222}.
CC   -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex composed of
CC       at least ARP6/ESD1/SUF3, PIE1, SWC6, SWC2 and H2AZs (HTA8, HTA9,
CC       HTA11). Interacts directly with SWC6/SEF and PIE1. Also interacts with
CC       H2A.F/Z proteins. {ECO:0000269|PubMed:17142478,
CC       ECO:0000269|PubMed:17220196, ECO:0000269|PubMed:17470967}.
CC   -!- INTERACTION:
CC       Q8LGE3; Q7X9V2: PIE1; NbExp=4; IntAct=EBI-1537316, EBI-1537462;
CC       Q8LGE3; Q9FHW2: SWC6; NbExp=6; IntAct=EBI-1537316, EBI-1537353;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16141450,
CC       ECO:0000269|PubMed:16155178, ECO:0000269|PubMed:17470967}. Cytoplasm
CC       {ECO:0000269|PubMed:16141450}. Note=Localized in the nucleus during the
CC       interphase, but is released into the cytoplasm during the mitotic phase
CC       (PubMed:16141450). Associated to heterochromatin (PubMed:16141450).
CC       Localized at the nuclear periphery when interacting with SWC6
CC       (PubMed:16155178, PubMed:17470967).
CC   -!- TISSUE SPECIFICITY: Mostly expressed in flowers, and, to a lower
CC       extent, in seedlings, shoot apex, stems, siliques, seeds, and roots (at
CC       protein level). {ECO:0000269|PubMed:11891255,
CC       ECO:0000269|PubMed:16141450, ECO:0000269|PubMed:16155178,
CC       ECO:0000269|PubMed:16495307}.
CC   -!- DISRUPTION PHENOTYPE: Early flowering, leaf serration, production of
CC       extra petals and weak apical dominance. {ECO:0000269|PubMed:17220196}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP6 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF03459.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF507914; AAM53246.1; -; mRNA.
DR   EMBL; AC009992; AAF03459.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77716.1; -; Genomic_DNA.
DR   EMBL; AY050786; AAK92721.1; -; mRNA.
DR   EMBL; AY150426; AAN12968.1; -; mRNA.
DR   EMBL; AY084321; AAM60907.1; -; mRNA.
DR   EMBL; AF494760; AAN77933.1; -; Genomic_DNA.
DR   EMBL; AF494761; AAN77934.1; -; Genomic_DNA.
DR   EMBL; AF494765; AAN77938.1; -; Genomic_DNA.
DR   EMBL; AF494766; AAN77939.1; -; Genomic_DNA.
DR   EMBL; AF494767; AAN77940.1; -; Genomic_DNA.
DR   EMBL; AF494770; AAN77943.1; -; Genomic_DNA.
DR   EMBL; AF494772; AAN77945.1; -; Genomic_DNA.
DR   EMBL; AF494773; AAN77946.1; -; Genomic_DNA.
DR   EMBL; AF494774; AAN77947.1; -; Genomic_DNA.
DR   EMBL; AF494776; AAN77949.1; -; Genomic_DNA.
DR   EMBL; AF494777; AAN77950.1; -; Genomic_DNA.
DR   EMBL; AF494782; AAN77955.1; -; Genomic_DNA.
DR   EMBL; AF494789; AAN77962.1; -; Genomic_DNA.
DR   EMBL; AF494792; AAN77965.1; -; Genomic_DNA.
DR   EMBL; AF494796; AAN77969.1; -; Genomic_DNA.
DR   EMBL; BK000425; DAA00030.1; -; Genomic_DNA.
DR   RefSeq; NP_566861.1; NM_114070.4.
DR   AlphaFoldDB; Q8LGE3; -.
DR   SMR; Q8LGE3; -.
DR   BioGRID; 8476; 3.
DR   IntAct; Q8LGE3; 2.
DR   STRING; 3702.AT3G33520.1; -.
DR   PaxDb; Q8LGE3; -.
DR   PRIDE; Q8LGE3; -.
DR   ProteomicsDB; 246921; -.
DR   EnsemblPlants; AT3G33520.1; AT3G33520.1; AT3G33520.
DR   GeneID; 823150; -.
DR   Gramene; AT3G33520.1; AT3G33520.1; AT3G33520.
DR   KEGG; ath:AT3G33520; -.
DR   Araport; AT3G33520; -.
DR   TAIR; locus:2102202; AT3G33520.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_1_1_1; -.
DR   InParanoid; Q8LGE3; -.
DR   OMA; FFEEYEC; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; Q8LGE3; -.
DR   PRO; PR:Q8LGE3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8LGE3; baseline and differential.
DR   Genevisible; Q8LGE3; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0000812; C:Swr1 complex; IDA:TAIR.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:TAIR.
DR   GO; GO:0030029; P:actin filament-based process; TAS:TAIR.
DR   GO; GO:0051301; P:cell division; IMP:TAIR.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:TAIR.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IMP:TAIR.
DR   GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR   GO; GO:0016571; P:histone methylation; IMP:TAIR.
DR   GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR   GO; GO:0009266; P:response to temperature stimulus; IMP:TAIR.
DR   GO; GO:0009845; P:seed germination; IMP:TAIR.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR030054; Arp6.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF47; PTHR11937:SF47; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Developmental protein; Nucleus;
KW   Plant defense; Reference proteome.
FT   CHAIN           1..421
FT                   /note="Actin-related protein 6"
FT                   /id="PRO_0000320535"
FT   VARIANT         230..231
FT                   /note="RL -> PP (in strain: cv. Lip-0)"
FT   VARIANT         231
FT                   /note="L -> P (in strain: cv. Aa-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         248
FT                   /note="G -> S (in strain: cv. Goe-2)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         250
FT                   /note="T -> R (in strain: cv. Ri-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         253
FT                   /note="K -> E (in strain: cv. Gre-0 and cv. Kas-1)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         263
FT                   /note="K -> R (in strain: cv. Di-0 and cv. Kil-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         271
FT                   /note="K -> E (in strain: cv. Cl-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         280
FT                   /note="V -> D (in strain: cv. Yo-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         290
FT                   /note="K -> E (in strain: cv. Kil-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         301
FT                   /note="L -> I (in strain: cv. Yo-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         308..311
FT                   /note="QPAD -> SLQI (in strain: cv. Ba-1)"
FT   VARIANT         310
FT                   /note="A -> S (in strain: cv. En-2)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   VARIANT         311
FT                   /note="D -> V (in strain: cv. Oy-0)"
FT                   /evidence="ECO:0000269|PubMed:12566397"
FT   CONFLICT        1
FT                   /note="M -> MG (in Ref. 1; AAM53246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        6
FT                   /note="V -> F (in Ref. 1; AAM53246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        250
FT                   /note="T -> I (in Ref. 4; AAK92721 and 6; AAN77965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        291
FT                   /note="N -> I (in Ref. 6; AAN77939)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  46944 MW;  9854EDAB8630030F CRC64;
     MSNIVVLDNG GGLIKAGQGG ERDPTTVIPN CLYKPLSSKK FIHPSPLTTL SDEIDLTSAA
     VRRPIDRGYL INSDLQREIW SHLFTSLLHI APSSSSLLLT EAPLSIPSVQ RTTDELVFED
     FGFSSLYIAH PQSLVHLYEA SRQPDSILSK TQCSLVVDCG FSFTHAVPVL HNFTLNHAIK
     RIDLGGKAFT NYLKELVSYR SINVMDETFL VDDAKEKLCF VSLDLLRDLR LARNGNTLIK
     STYVLPDGVT HTKGYVKDPQ AAKRFLSLSE KESVVVMDKV GERKKADMNK NEIDLTNERF
     LVPETLFQPA DLGMNQAGLA ECIVRAINSC HSYLQPVLYQ SIILTGGSTL FPQLKERLEG
     ELRPLVPDHF DVKITTQEDP ILGVWRGGSL LASSPDFESM CVTKAEYEEL GSARCRRRFF
     H
 
 
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