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LVSB_DICDI
ID   LVSB_DICDI              Reviewed;        4118 AA.
AC   Q86JF2; Q55AT1; Q8IHL0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   23-FEB-2022, entry version 110.
DE   RecName: Full=BEACH domain-containing protein lvsB;
GN   Name=lvsB; ORFNames=DDB_G0271504;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 416-4118, AND FUNCTION.
RC   STRAIN=NC4A2;
RX   PubMed=12210762; DOI=10.1002/jcb.10254;
RA   Wang N., Wu W.I., De Lozanne A.;
RT   "BEACH family of proteins: phylogenetic and functional analysis of six
RT   Dictyostelium BEACH proteins.";
RL   J. Cell. Biochem. 86:561-570(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=11854420; DOI=10.1091/mbc.01-09-0454;
RA   Harris E., Wang N., Wu Wl W.L., Weatherford A., De Lozanne A., Cardelli J.;
RT   "Dictyostelium LvsB mutants model the lysosomal defects associated with
RT   Chediak-Higashi syndrome.";
RL   Mol. Biol. Cell 13:656-669(2002).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17488289; DOI=10.1111/j.1600-0854.2007.00567.x;
RA   Kypri E., Schmauch C., Maniak M., De Lozanne A.;
RT   "The BEACH protein LvsB is localized on lysosomes and postlysosomes and
RT   limits their fusion with early endosomes.";
RL   Traffic 8:774-783(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=17606989; DOI=10.1242/jcs.009001;
RA   Charette S.J., Cosson P.;
RT   "A LYST/beige homolog is involved in biogenesis of Dictyostelium secretory
RT   lysosomes.";
RL   J. Cell Sci. 120:2338-2343(2007).
CC   -!- FUNCTION: Involved in negative regulation of lysosome biogenesis, by
CC       limiting the heterotypic fusion of early endosomes and postlysosomal
CC       compartments. {ECO:0000269|PubMed:11854420,
CC       ECO:0000269|PubMed:12210762, ECO:0000269|PubMed:17488289,
CC       ECO:0000269|PubMed:17606989}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Lysosome {ECO:0000269|PubMed:17488289}. Endosome
CC       {ECO:0000269|PubMed:17488289}. Note=Also found in post-lysosome.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN38985.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAFI02000006; EAL71616.2; -; Genomic_DNA.
DR   EMBL; AY159038; AAN38985.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_645615.2; XM_640523.2.
DR   SMR; Q86JF2; -.
DR   STRING; 44689.DDB0185107; -.
DR   PaxDb; Q86JF2; -.
DR   PRIDE; Q86JF2; -.
DR   EnsemblProtists; EAL71616; EAL71616; DDB_G0271504.
DR   GeneID; 8618070; -.
DR   KEGG; ddi:DDB_G0271504; -.
DR   dictyBase; DDB_G0271504; lvsB.
DR   eggNOG; KOG1786; Eukaryota.
DR   HOGENOM; CLU_223969_0_0_1; -.
DR   InParanoid; Q86JF2; -.
DR   OMA; MSITKKW; -.
DR   PRO; PR:Q86JF2; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:dictyBase.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; HMP:dictyBase.
DR   GO; GO:0006887; P:exocytosis; IMP:dictyBase.
DR   GO; GO:0007041; P:lysosomal transport; IMP:dictyBase.
DR   GO; GO:0007040; P:lysosome organization; IMP:dictyBase.
DR   GO; GO:1905362; P:negative regulation of endosomal vesicle fusion; IMP:dictyBase.
DR   GO; GO:0001845; P:phagolysosome assembly; IMP:dictyBase.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:dictyBase.
DR   CDD; cd06071; Beach; 1.
DR   Gene3D; 1.10.1540.10; -; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 2.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000409; BEACH_dom.
DR   InterPro; IPR036372; BEACH_dom_sf.
DR   InterPro; IPR023362; PH-BEACH_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF02138; Beach; 1.
DR   Pfam; PF14844; PH_BEACH; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM01026; Beach; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF81837; SSF81837; 1.
DR   PROSITE; PS50197; BEACH; 1.
DR   PROSITE; PS51783; PH_BEACH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   4: Predicted;
KW   Coiled coil; Endosome; Lysosome; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; WD repeat.
FT   CHAIN           1..4118
FT                   /note="BEACH domain-containing protein lvsB"
FT                   /id="PRO_0000327708"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        827..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3303..3479
FT                   /note="BEACH-type PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT   DOMAIN          3491..3782
FT                   /note="BEACH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT   REPEAT          3868..3907
FT                   /note="WD 1"
FT   REPEAT          3924..3963
FT                   /note="WD 2"
FT   REPEAT          3984..4027
FT                   /note="WD 3"
FT   REPEAT          4029..4073
FT                   /note="WD 4"
FT   REPEAT          4075..4114
FT                   /note="WD 5"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1599..1622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1643..1681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1928..1968
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2015..2044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2537..2574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2702..2741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2754..2791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2902..3007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3245..3265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3348..3418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2705..2738
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        236..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1190..1204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2537..2573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2704..2737
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3348..3417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        2030
FT                   /note="N -> T (in Ref. 3; AAN38985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4104
FT                   /note="L -> W (in Ref. 3; AAN38985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   4118 AA;  463997 MW;  E87919A55B1B0EBC CRC64;
     MNRNFNNINN NNNNNNNYHG YQYHQQQQQQ NQQQQQQQYN NNVIKYLWNT YTQTVVYQDS
     LFNLVEFLQF FTLNYYNDTI GDLLFLSNGT LTDITRHLSK HLIEEIGYSC TLLNQQQQTQ
     QTQTQTQSKQ QTIPQLSLNN SIPTSFTTTA SSTNTTPNAG LKLAEYEIYQ YLIGYSTAGE
     GPLVLAALDI LSRQSPNGIP LSFLNFLITI LLRILSLPPE LLYNNNNNDN NNNINNFSGN
     NNNNFNNNNH YFNNNHNNHN HHYQHHQLKE KKKNVNKQHF KPIESFFYLQ PLPSSLSDMF
     RDDDYASLSS SYGGGGNLTP LSLSSNHAFS PPLSSLKNSS SNTFTKPSSS TTTTTTTTTQ
     TPTPNSNTDS KQNKDNNNSK NNNKEVSSVV LLGYQILKIV ENLVKDKLFL YELVTSDCFS
     QLLNIFYKLP ILSTTASSLP PNSSFSIIYQ QLSQIFAQIM SKSCLSSDTI VLIHNFKLIK
     NLLNIMDKLK EKDEYNMNLI IELNKIILFS IKSSTSITKL LHDDFTKANG YSILLNSMIF
     ISDYGTLKNK IDYIQTTTNL LFIGHRSSYL DKANTKMFEI YLNVFSISTS EETKTELLKC
     IKGVFYTSLI EESSSSSSLI ISSSDNNNNN NNNSDGVNDD KNNNNNNRDN IIFEDVIDMD
     GNDSYLIFHQ FQPFTILFSQ FDTLNINNRR MILDMMDVLL TKNRISLNEL KEYCNLFKSE
     LPSTVLLVSQ HLTELLTKGK VSCDVLGRDL SLTQKLLEFL VNDPTTLRFS SILLQNETEL
     QLCFSILSTN NNNNNSSSKY YSNNIQQQQQ QQQQQQQQQK KRHVSRYLVL YMIVTEILSL
     LLELLVPPSI QTIFIQECQG LKLLYPMLLD EYLIQPALKV IASIAIGGLQ LESRIIPDLI
     MELQNNGGGA TNLDSKVLTM RKNIFSSMCY IFHNNPNSKN SFRNFQGFTW SLSILDGISR
     YLISIDNNNN NSSNNNSNDN LNDFKESLDH SCNGVLNSNN SSNNSNLNGG IGNEIKKSSF
     NEIFYFLKVL IDMLSAAMKN NSINQEYFRK EIIIISRSLK QCKYMEGIHA ISLCDSLLNM
     AITGSWPPSC ENHSLEEGSL FSLYSPITSF FPINTTLSKN FDISFILKFE KKEQMEQQLK
     QQILLNSNNN INNGNGGSIS PSSIINNMNS PGGGSSSSND SLKSPTRRSR SYTNDFHLDK
     SSRIPHPPDF NNNNDTMNYD YNFQDDYIES LNSKSSSSFS LDLASVTGDS EIVYYGGSTT
     SRMIHSPGLP SSSLQALSSN STKLPEKSSL QLAQERYICC QSCRDTLTLE MPEIFKLIIE
     LMSSDDDISQ TEIKSSCYII RELIFLTNCS LANQKRLSSL LIDIITHFKP LLLSIILYQK
     QQQQQQQQQQ QSNSNSNSNS TIILKKKINN ETSTKLKPLL LDLIQTLAGH NLTLIEFRKY
     FELLKVKDSN NQFIYPIDLL NLLLKISSNR DNIPLYYAEL SKHGLEYIDF PSWGERTWPP
     TKGFGISFWF RYSLPCLNIN KSPIYLLSIE GSIGNSSTKS CECQLILENG KLVYKIYHFS
     GICETYHFSD HKFEPDQFYH ISISHSSLLS TTTTTATTAN TTTNSTTAST TTTTTNSTTA
     VSSTTNSIST TAAVAAITTS DGNSGISREN SLGGRDSIGS NSSSSSSSSN SGVSSGSSTN
     LNKKSPVKLY VNGCLRGQIL ANYPKSNSMT LYIRFGGVNA ASSVISNNQD VQSFNVNNSW
     NLGNAYFFEE VPLDKEIFYL YLLGPNHFRG LKVDLSAVDS IQPSLDKVSN LHPFLIDHLL
     NPTVQPLLSL HEKIMYIFTA KCLYVTTHRI TNKTESVTHA SALPQLSTIL FQQQQLQQQQ
     LQQQITNSTT SILNELNLSN SINLIRRGSE NSLITSSSSS SLSLSLSSNT NNNNNNNTRS
     SLERSISGNF LQSPSSSNNN LRERSINNNN NNNNNSNNNN NNNSISSSTS SLSSSVISLV
     AGAMAVPSPP SPNKLGSGIN GSSILNASLT TLSISTNNNS NNSNNSNSNN NNNNNNTNYN
     SNSLNNSLNH QALSLLHTGL PIALPRGVIS QIGVKDAIMN SGGVSVIIYL IAMAEDKEYQ
     RSGLKLLQSI IHNSQLNLKD MKEISGYQLV SFLIRKKNWV LDDQLLSILF SFVGIQSTRT
     SIHYVDGVVQ DVLALKHFLL ERSIWRRASL IDQKKLFESL EKLVNVLHEN HEFNIIKFRQ
     AGAYETILKM CREDDLPLEL LSTLTKILRS ITTNKSNKLK DDLQLILSWL LETMPKQQIF
     KKYNSFNGLN STNNSNNNNN NPISLFRKGR KTLLQVQFDN HQLYLQQQQQ QNLIPQVNSN
     NNNEESNNGI EGIIRINILN LLLDILSKTE LSVVEDFHSI CSLETIFGLL TCESMVSRVM
     FLKIIDIFLH SQMIFGHFQK MKGFHLLGHQ LLPFETSEKI FGVLFCILFG KPSNSDILEG
     LSMRMYFLSH LSDAEMKYPG AIVTILIILC NSNSTTQHNV IKMIHNIFLQ NDQFKQSLLD
     NELIPRLVDI LSSNYQRRGS SSSSTNSTTN NNNNNSSTTT TSNNNNNNNE NNNEDDWVAE
     ESILSLLKEI ALYGAKSQDG SAALLRDILV VLHLNTRMDY DYICCLQRRV LFDVISFFND
     NIHSFSSIDS LVSSFEKLCV LTIHTLSYQE KLLLTNGTGT GGGTGGSGGG LLTKKSFRSN
     LFSPSRSKEK EKEKEKEKEK EKEKEKERER ERETTNVTSD SDNILSANDI FYGDQSNEES
     STTDSDSTSD NNNNNNRNSY SGRNIRGNGI NNNNNKNKFI PIWIKEGNLL DQEEFIRSLL
     KVLSKSKIPQ SNTTYRNLFS TQYSARSLLC KFIFILLTFD EFKDYYLMVL QELSNMVPSL
     SNTPISSSPI ISPINNNNNY YNTNSNTNSN SSTPSLFSIT SNNNNNNNNN NNNNNNNNNN
     NNTNSTNQTI TDTTLSPASS NVSISNQSTP ISNNNNNNNS SGGGSGGSNI NIPPTINISD
     SNSNSNEQQG ISSVLSEIIM EEDFILVLLH ITHKFLQSGN DYEIQRNSFR LWVSIIQHCS
     QVDYVKKAFD TTTTSLAVLS SSQEIRDLLI RYQQIYVENE FKKWEEKFNQ SKKEWKLQYF
     ETQKNKQSMI TKNQDITKST KKLSDSLIQL KSEYEKSNYQ YLIENRESKR FFQSQWKLLI
     KKVTHEKAIW SPNYEISNSS STNITTTTTT TTTAKKWKLD PTEGLNRMRM RLKVISDNTS
     NSHIPLIPDL STPSTPPSPQ NTKDQLLFNF NNYNNNNNNN NNNGLNAPPL HGSLDYSSFD
     NLKLGEKVNE VFKCSCISPF YQRDGELLIG DQNVYFLDEL LTSADRKKTT ASTVGGSNNN
     NNNNNNNNNN NNNNNNNSND TTSSINSTTA TNTNTTNTTT TNTTTTTTTT NGLSNIVKPP
     QRGKHITWSY DDIIEIHKRR HVLKNNAIEI FLGSGVPHKT YLFAFNKPSD RDIVYDLIMS
     KPLPNRVDYA AEVHGNILKM SITKKWQSGL ISNFEYLMHL NTLAGRSFND LTQYPIFPFI
     LRDYESEVLD LENPNTFRDF TKPMGAQDPK RLEKFIEKYN DLLEMNEKPY HYGSHYSNIG
     SVLHFLVRLQ PFTSYFIDFQ GGRFDVPDRA FHSIAQSWNL SSSISNSDVK ELIPEFFYLS
     DFLVNSNKFF MGIKQNGVKV DDVILPPWAH NDPRLFIKKH NEALECKYVS ENLHHWIDLL
     FGYKQQGEAA VKAHNMFFPL TYEGAVDIDS IEDQLNRDAA VAQIHSYGQT PKQIFTKPHP
     KKNWSKTIRL TQDSIFTKPE RLTSYIMFQY RSPIGSITIA NDSSPIHLTP QRILFFPDNN
     KSISWGHWDQ NLRVNSIDTG KVLSIIEVLN DDIICGDITK NGRLFVTGGT AGTVKVWKRC
     NNDGTIMTRK ERGDNLSLWS TLYGHTNSIL CVTVSQEYSI IVSGSKDSNC IIWDLNRLTY
     INSLQHDHPV TCVQVSPTFG YIATFETNIY NKQNNNSGGG GSKNDNSING SGCLRLWSIN
     GTLLAKQNFV NDRVNCMIFT STIQGVNTNL LITGMESGTI ILWNAWNLQK IRTLVSKSTI
     TALAVSKDNT QLISGDINGL IECLSSRSFD GYSSIVLG
 
 
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