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AP1_SCHPO
ID   AP1_SCHPO               Reviewed;         552 AA.
AC   Q01663; Q9US23; Q9UU69;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=AP-1-like transcription factor;
DE   AltName: Full=Caffeine resistance protein 3;
GN   Name=pap1; Synonyms=caf3; ORFNames=SPAC1783.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=1899230; DOI=10.1101/gad.5.1.60;
RA   Toda T., Shimanuki M., Yanagida M.;
RT   "Fission yeast genes that confer resistance to staurosporine encode an AP-
RT   1-like transcription factor and a protein kinase related to the mammalian
RT   ERK1/MAP2 and budding yeast FUS3 and KSS1 kinases.";
RL   Genes Dev. 5:60-73(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-143.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [4]
RP   PROTEIN SEQUENCE OF 514-525, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12100563; DOI=10.1046/j.1365-2958.2002.03020.x;
RA   Castillo E.A., Ayte J., Chiva C., Moldon A., Carrascal M., Abian J.,
RA   Jones N., Hidalgo E.;
RT   "Diethylmaleate activates the transcription factor Pap1 by covalent
RT   modification of critical cysteine residues.";
RL   Mol. Microbiol. 45:243-254(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=1448080; DOI=10.1128/mcb.12.12.5474-5484.1992;
RA   Toda T., Shimanuki M., Saka Y., Yamano H., Adachi Y., Shirakawa M.,
RA   Kyogoku Y., Yanagida M.;
RT   "Fission yeast pap1-dependent transcription is negatively regulated by an
RT   essential nuclear protein, crm1.";
RL   Mol. Cell. Biol. 12:5474-5484(1992).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=9585505; DOI=10.1101/gad.12.10.1453;
RA   Toone W.M., Kuge S., Samuels M., Morgan B.A., Toda T., Jones N.;
RT   "Regulation of the fission yeast transcription factor Pap1 by oxidative
RT   stress: requirement for the nuclear export factor Crm1 (Exportin) and the
RT   stress-activated MAP kinase Sty1/Spc1.";
RL   Genes Dev. 12:1453-1463(1998).
RN   [7]
RP   ERRATUM OF PUBMED:9585505.
RA   Toone W.M., Kuge S., Samuels M., Morgan B.A., Toda T., Jones N.;
RL   Genes Dev. 12:2650-2650(1998).
RN   [8]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-517; ILE-519; LEU-522;
RP   CYS-523; LEU-526 AND CYS-532.
RX   PubMed=10329722; DOI=10.1074/jbc.274.21.15151;
RA   Kudo N., Taoka H., Toda T., Yoshida M., Horinouchi S.;
RT   "A novel nuclear export signal sensitive to oxidative stress in the fission
RT   yeast transcription factor Pap1.";
RL   J. Biol. Chem. 274:15151-15158(1999).
RN   [9]
RP   SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-278 AND
RP   CYS-501.
RX   PubMed=15165244; DOI=10.1111/j.1365-2958.2004.04065.x;
RA   Vivancos A.P., Castillo E.A., Jones N., Ayte J., Hidalgo E.;
RT   "Activation of the redox sensor Pap1 by hydrogen peroxide requires
RT   modulation of the intracellular oxidant concentration.";
RL   Mol. Microbiol. 52:1427-1435(2004).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15824112; DOI=10.1074/jbc.m502757200;
RA   Bozonet S.M., Findlay V.J., Day A.M., Cameron J., Veal E.A., Morgan B.A.;
RT   "Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch
RT   controlling the transcriptional response to increasing levels of hydrogen
RT   peroxide.";
RL   J. Biol. Chem. 280:23319-23327(2005).
RN   [11]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [12]
RP   INTERACTION WITH TPX1.
RX   PubMed=24316080; DOI=10.1016/j.celrep.2013.11.027;
RA   Calvo I.A., Boronat S., Domenech A., Garcia-Santamarina S., Ayte J.,
RA   Hidalgo E.;
RT   "Dissection of a redox relay: H2O2-dependent activation of the
RT   transcription factor Pap1 through the peroxidatic Tpx1-thioredoxin cycle.";
RL   Cell Rep. 5:1413-1424(2013).
RN   [13]
RP   FUNCTION, AND MUTAGENESIS OF CYS-259; CYS-278; CYS-285; CYS-501; CYS-523
RP   AND CYS-532.
RX   PubMed=23525001; DOI=10.1242/jcs.124370;
RA   Calvo I.A., Ayte J., Hidalgo E.;
RT   "Reversible thiol oxidation in the H2O2-dependent activation of the
RT   transcription factor Pap1.";
RL   J. Cell Sci. 126:2279-2284(2013).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 71-140, SUBUNIT, AND DNA-BINDING.
RX   PubMed=11017199; DOI=10.1038/82822;
RA   Fujii Y., Shimizu T., Toda T., Yanagida M., Hakoshima T.;
RT   "Structural basis for the diversity of DNA recognition by bZIP
RT   transcription factors.";
RL   Nat. Struct. Biol. 7:889-893(2000).
CC   -!- FUNCTION: Transcription activator involved in multidrug resistance,
CC       oxidative stress response, and redox homeostasis. Regulates the
CC       transcription of genes encoding antioxidant enzymes like catalase ctt1
CC       and components of the cellular thiol-reducing pathways, including the
CC       thioredoxin system (trx2, trr1), ABC tansporters involved in multidrug
CC       resistance like bfr1/hba2 and pmd1 as well as the gene obr1/apt1.
CC       Preferentially binds to promoters with the core binding site 5'-
CC       TTA[CG]TAA-3'. Activity of the transcription factor is controlled
CC       through oxidation of specific cysteine residues resulting in the
CC       alteration of its subcellular location. Oxidative stress induces
CC       nuclear accumulation and as a result pap1 transcriptional activity.
CC       Required for sty1/spc1-confered staurosporine resistance.
CC       {ECO:0000269|PubMed:11017199, ECO:0000269|PubMed:1448080,
CC       ECO:0000269|PubMed:1899230, ECO:0000269|PubMed:23525001,
CC       ECO:0000269|PubMed:9585505}.
CC   -!- SUBUNIT: Homodimer (PubMed:11017199). The reduced form of pap1
CC       interacts in the nucleus with the nuclear export protein crm1, and in
CC       the cytoplasm with the peroxiredoxin tpx1 (PubMed:12100563,
CC       PubMed:24316080). {ECO:0000269|PubMed:11017199,
CC       ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:24316080}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10329722,
CC       ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:15165244,
CC       ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:9585505}. Cytoplasm
CC       {ECO:0000269|PubMed:10329722, ECO:0000269|PubMed:12100563,
CC       ECO:0000269|PubMed:15165244, ECO:0000269|PubMed:15824112,
CC       ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9585505}. Note=Oxidized
CC       pap1 is found predominantly in the nucleus, while reduced pap1 is
CC       continuously exported to the cytoplasm by crm1/exportin 1.
CC       {ECO:0000269|PubMed:10329722, ECO:0000269|PubMed:9585505}.
CC   -!- DOMAIN: Contains two cysteine rich domains (CRD), referred to as the
CC       N- and C-terminal CRD's, n-CRD (Cys-259, Cys-278, Cys-285 and Cys-290)
CC       and c-CRD (Cys-501, Cys-523 and Cys-532), respectively. Cys-259 and
CC       Cys-290 are not conserved in orthologs in other yeast species. A
CC       nuclear export signal is embedded in the c-CRD, with which the nuclear
CC       export protein crm1/exportin 1 interacts only in the absence of
CC       disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or
CC       between the c-CRD and the n-CRD. {ECO:0000269|PubMed:12100563,
CC       ECO:0000269|PubMed:23525001}.
CC   -!- PTM: Depending on the oxidative stress inducing agent, pap1 can undergo
CC       two distinct conformational changes, both masking the nuclear export
CC       signal, thus abolishing nuclear export by crm1/exportin 1. The
CC       glutathione-depleting agent diethylmaleate (DEM) leads to the non-
CC       reversible modification of at least 2 cysteine residues in the c-CRD.
CC       Peroxide stress induces the formation of a tpx1-dependent interdomain
CC       disulfide bond between Cys-278 and Cys-501.
CC       {ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:15165244,
CC       ECO:0000269|PubMed:15824112}.
CC   -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR   EMBL; X57078; CAA40363.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB66170.1; -; Genomic_DNA.
DR   EMBL; AB027778; BAA87082.1; -; Genomic_DNA.
DR   PIR; S15664; S15664.
DR   PIR; T50109; T50109.
DR   RefSeq; NP_593662.1; NM_001019094.2.
DR   PDB; 1GD2; X-ray; 2.00 A; E/F/G/H/I/J=71-140.
DR   PDBsum; 1GD2; -.
DR   AlphaFoldDB; Q01663; -.
DR   SMR; Q01663; -.
DR   BioGRID; 278616; 75.
DR   IntAct; Q01663; 1.
DR   MINT; Q01663; -.
DR   STRING; 4896.SPAC1783.07c.1; -.
DR   iPTMnet; Q01663; -.
DR   MaxQB; Q01663; -.
DR   PaxDb; Q01663; -.
DR   PRIDE; Q01663; -.
DR   EnsemblFungi; SPAC1783.07c.1; SPAC1783.07c.1:pep; SPAC1783.07c.
DR   GeneID; 2542140; -.
DR   KEGG; spo:SPAC1783.07c; -.
DR   PomBase; SPAC1783.07c; pap1.
DR   VEuPathDB; FungiDB:SPAC1783.07c; -.
DR   eggNOG; ENOG502RPD7; Eukaryota.
DR   HOGENOM; CLU_492711_0_0_1; -.
DR   InParanoid; Q01663; -.
DR   OMA; DFFTPYN; -.
DR   PhylomeDB; Q01663; -.
DR   EvolutionaryTrace; Q01663; -.
DR   PRO; PR:Q01663; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:PomBase.
DR   GO; GO:0140463; F:chromatin-protein adaptor; IMP:PomBase.
DR   GO; GO:0008301; F:DNA binding, bending; IDA:PomBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:PomBase.
DR   GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR013910; TF_PAP1.
DR   InterPro; IPR023167; Yap1_redox_dom_sf.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF08601; PAP1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF111430; SSF111430; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..552
FT                   /note="AP-1-like transcription factor"
FT                   /id="PRO_0000076532"
FT   DOMAIN          76..139
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..102
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          104..111
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          213..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..290
FT                   /note="n-CRD"
FT                   /evidence="ECO:0000305|PubMed:23525001"
FT   REGION          460..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..532
FT                   /note="c-CRD"
FT                   /evidence="ECO:0000305|PubMed:23525001"
FT   MOTIF           81..88
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           515..533
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000305|PubMed:10329722"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        278..501
FT                   /note="In nuclear retained form"
FT                   /evidence="ECO:0000269|PubMed:12100563,
FT                   ECO:0000269|PubMed:15165244"
FT   DISULFID        285..532
FT                   /note="In nuclear retained form"
FT                   /evidence="ECO:0000250|UniProtKB:P19880"
FT   MUTAGEN         259
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:23525001"
FT   MUTAGEN         278
FT                   /note="C->A: Constitutively cytoplasmic."
FT                   /evidence="ECO:0000269|PubMed:15165244,
FT                   ECO:0000269|PubMed:23525001"
FT   MUTAGEN         285
FT                   /note="C->S: Constitutively cytoplasmic."
FT                   /evidence="ECO:0000269|PubMed:23525001"
FT   MUTAGEN         501
FT                   /note="C->A: Constitutively cytoplasmic."
FT                   /evidence="ECO:0000269|PubMed:15165244,
FT                   ECO:0000269|PubMed:23525001"
FT   MUTAGEN         517
FT                   /note="F->A: Impairs nuclear export; when associated with
FT                   A-519."
FT                   /evidence="ECO:0000269|PubMed:10329722"
FT   MUTAGEN         519
FT                   /note="I->A: Weakens nuclear export. Impairs nuclear
FT                   export; when associated with A-517."
FT                   /evidence="ECO:0000269|PubMed:10329722"
FT   MUTAGEN         522
FT                   /note="L->A: Impairs nuclear export."
FT                   /evidence="ECO:0000269|PubMed:10329722"
FT   MUTAGEN         523
FT                   /note="C->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:23525001"
FT   MUTAGEN         523
FT                   /note="C->S: Impairs nuclear export; when associated with
FT                   S-532."
FT                   /evidence="ECO:0000269|PubMed:10329722"
FT   MUTAGEN         526
FT                   /note="L->A: Impairs nuclear export."
FT                   /evidence="ECO:0000269|PubMed:10329722"
FT   MUTAGEN         532
FT                   /note="C->S: Weakens nuclear export. Impairs nuclear
FT                   export; when associated with S-523."
FT                   /evidence="ECO:0000269|PubMed:10329722"
FT   MUTAGEN         532
FT                   /note="C->T: Constitutively cytoplasmic."
FT                   /evidence="ECO:0000269|PubMed:23525001"
FT   CONFLICT        166
FT                   /note="S -> P (in Ref. 1; CAA40363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280..281
FT                   /note="KL -> NV (in Ref. 1; CAA40363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        543..552
FT                   /note="DVEAALNQFN -> RC (in Ref. 1; CAA40363)"
FT                   /evidence="ECO:0000305"
FT   HELIX           80..125
FT                   /evidence="ECO:0007829|PDB:1GD2"
FT   HELIX           128..138
FT                   /evidence="ECO:0007829|PDB:1GD2"
SQ   SEQUENCE   552 AA;  61532 MW;  D9E7FEA0A286B4BE CRC64;
     MSGQTETLSS TSNIPIAKAE PEQSADFSAS HKKRGPVSDR SSRRTSSEEV DLMPNVDDEV
     DGDVKPKKIG RKNSDQEPSS KRKAQNRAAQ RAFRKRKEDH LKALETQVVT LKELHSSTTL
     ENDQLRQKVR QLEEELRILK DGSFTFEMSL PHRNPSLSSL PTTGFSSNFA HMKDGISPQS
     NLHLSPNSIE KPNMHQNVLH NDRSADNLNH RYQVPPTLVD SNSAQGTLSP ETPSSSDSPS
     NLYLNYPKRK SITHLHHDCS ALSNGENGED VADGKQFCQK LSTACGSIAC SMLTKTTPHR
     ASVDILSNLH ESTVSPPMAD ESVQRSSEVS KSIPNVELSL NVNQQFVSPF GGTDSFPLPT
     DTGLDSLFEP DSAIENSHLK NVVMEPELFQ AWREPAESLD KEFFNDEGEI DDVFHNYFHN
     SNENGDLITN SLHGLDFLEN ANESFPEQMY PFIKHNKDYI SNHPDEVPPD GLPQKGKHDT
     SSQMPSENEI VPAKERAYLS CPKVWSKIIN HPRFESFDID DLCSKLKNKA KCSSSGVLLD
     ERDVEAALNQ FN
 
 
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