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PI4KA_MOUSE
ID   PI4KA_MOUSE             Reviewed;        2105 AA.
AC   E9Q3L2; Q3UVT5; Q6DIC7; Q7TNG2; Q80Y45;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Phosphatidylinositol 4-kinase alpha;
DE            Short=PI4-kinase alpha;
DE            Short=PI4K-alpha;
DE            Short=PtdIns-4-kinase alpha;
DE            EC=2.7.1.67 {ECO:0000250|UniProtKB:P42356};
GN   Name=Pi4ka {ECO:0000312|MGI:MGI:2448506}; Synonyms=Pik4, Pik4ca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-2105.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH75629.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH75629.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1441-2105.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23184.1};
RC   TISSUE=Diencephalon {ECO:0000312|EMBL:BAE23184.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-263 AND SER-1439,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-260; SER-262;
RP   SER-263; SER-268 AND SER-1439, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   GENE STRUCTURE, AND DISRUPTION PHENOTYPE.
RX   PubMed=23229899; DOI=10.1083/jcb.201206095;
RA   Nakatsu F., Baskin J.M., Chung J., Tanner L.B., Shui G., Lee S.Y.,
RA   Pirruccello M., Hao M., Ingolia N.T., Wenk M.R., De Camilli P.;
RT   "PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its impact
RT   on plasma membrane identity.";
RL   J. Cell Biol. 199:1003-1016(2012).
CC   -!- FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed
CC       step in the production of the second messenger inositol-1,4,5,-
CC       trisphosphate. {ECO:0000250|UniProtKB:P42356}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC         1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:P42356};
CC   -!- ACTIVITY REGULATION: Activated by Triton X-100, insensitive to
CC       inhibition by adenosine and inhibited by wortmannin (By similarity).
CC       The PI4K complex acts as a regulator of phosphatidylinositol 4-
CC       phosphate (PtdIns(4)P) synthesis. Interaction with TMEM150A regulates
CC       PtdIns(4)P synthesis (By similarity). {ECO:0000250|UniProtKB:O08662,
CC       ECO:0000250|UniProtKB:P42356}.
CC   -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex,
CC       composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and
CC       FAM126 (FAM126A or FAM126B). Interacts with TMEM150A; regulating
CC       recruitment to the plasma membrane. Interacts with TTC7A.
CC       {ECO:0000250|UniProtKB:P42356}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42356}. Cell
CC       membrane {ECO:0000250|UniProtKB:P42356}. Note=Localization to the
CC       plasma membrane is mediated by the PI4K complex and association with
CC       EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and FAM126 (FAM126A or
CC       FAM126B). Localization to the plasma membrane is regulated by TMEM150A.
CC       {ECO:0000250|UniProtKB:P42356}.
CC   -!- DISRUPTION PHENOTYPE: Early embryonic lethality. Conditional knockout
CC       mice show a dramatic depletion of cellular phosphatidylinositol 4-
CC       phosphate (PtdIns(4)P). {ECO:0000269|PubMed:23229899}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AC110573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC049252; AAH49252.1; -; mRNA.
DR   EMBL; BC055479; AAH55479.1; -; mRNA.
DR   EMBL; BC075629; AAH75629.1; -; mRNA.
DR   EMBL; AK136942; BAE23184.1; -; mRNA.
DR   RefSeq; NP_001001983.2; NM_001001983.2.
DR   RefSeq; XP_006522097.1; XM_006522034.1.
DR   AlphaFoldDB; E9Q3L2; -.
DR   SMR; E9Q3L2; -.
DR   IntAct; E9Q3L2; 9.
DR   MINT; E9Q3L2; -.
DR   STRING; 10090.ENSMUSP00000036162; -.
DR   iPTMnet; E9Q3L2; -.
DR   PhosphoSitePlus; E9Q3L2; -.
DR   EPD; E9Q3L2; -.
DR   jPOST; E9Q3L2; -.
DR   PaxDb; E9Q3L2; -.
DR   PeptideAtlas; E9Q3L2; -.
DR   PRIDE; E9Q3L2; -.
DR   ProteomicsDB; 289418; -.
DR   DNASU; 224020; -.
DR   GeneID; 224020; -.
DR   KEGG; mmu:224020; -.
DR   UCSC; uc007ykq.2; mouse.
DR   UCSC; uc007ykr.2; mouse.
DR   CTD; 5297; -.
DR   MGI; MGI:2448506; Pi4ka.
DR   eggNOG; KOG0902; Eukaryota.
DR   HOGENOM; CLU_000893_2_0_1; -.
DR   InParanoid; E9Q3L2; -.
DR   OrthoDB; 1147978at2759; -.
DR   TreeFam; TF102041; -.
DR   Reactome; R-MMU-1483248; Synthesis of PIPs at the ER membrane.
DR   Reactome; R-MMU-1660514; Synthesis of PIPs at the Golgi membrane.
DR   BioGRID-ORCS; 224020; 19 hits in 75 CRISPR screens.
DR   ChiTaRS; Pi4ka; mouse.
DR   PRO; PR:E9Q3L2; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; E9Q3L2; protein.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IMP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; ISO:MGI.
DR   GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR   GO; GO:0044788; P:modulation by host of viral process; ISO:MGI.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; ISO:MGI.
DR   GO; GO:0140754; P:reorganization of cellular membranes to establish viral sites of replication; ISO:MGI.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 1.25.40.70; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR045495; PI4K_N.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   Pfam; PF19274; PI4K_N; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipid metabolism; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..2105
FT                   /note="Phosphatidylinositol 4-kinase alpha"
FT                   /id="PRO_0000435632"
FT   DOMAIN          1533..1721
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          1811..2089
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1817..1823
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1957..1965
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1976..2000
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42356"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         260
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         262
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42356"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42356"
FT   MOD_RES         1439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   CONFLICT        861
FT                   /note="P -> L (in Ref. 2; AAH75629)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2105 AA;  237042 MW;  25EB66874330ED51 CRC64;
     MAAAGARGGG GGGGGGGGGG SGSSSGSSTS RGFYFNTVLS LARSLAVQRP ASLEKVQKLL
     CMCPVDFHGI FQLDERRRDA VIALGIFLIE SDLQHKDCVV PYLLRLLRGL PKVYWVEEST
     ARKGRGNLPV AESFSFCLVT LLSDVACRDP SLRDEILEAI LQVLHVLLGM CQALEIQEKE
     YLCKYAIPCL IGISRSFGRY SNSEESLLSK LFPKVSPHSL RIPEELEGVR RRSFNDFRSI
     LPSNLLTVCQ EGTLKRKTSS VSSISQVSPE RGIPPPSSPG GSAFHYFEAS CLPDGTALEP
     EYYFSTISSS FSISPLFNGI TYKEFCIPLE MLRELLNLVK KIVEEPVLKS LDAIVAGVME
     ANPSADLYYT TFSDPLYLTM FKMLRDTLYY MKDLPTSFVK EIHDFVLEQF NMSQGELQKI
     LHDADRIHSE MSPLKLRCQA NAACVDLMVW AVKDEQGAEN LCIKLSEKLQ SKTSSKVIIA
     HLPLLICCLQ GLGRLCERFP VVVHSVTPSL RDFLVIPSPV LVKLYKYHSQ YHTVAGSDIK
     ISVTNEHSES TLNVLPGKKN QPSMYEQLRD IAIDNICRCL KAGLTVDPVI VEAFLASLSN
     RLYISQESDK DAHLIPDHTI RALGHIAVAL RDTPKVMEPI LQILQQKFCQ PPSPLDVLII
     DQLGCLVITG NQYIYQEVWN LFQQISVKAS SVVYSATKDY KDHGYRHCSL AVINALANIA
     ANIQEEHLVD ELLMNLLELF VQLGLEGKRA SERASEKGPA LKASSSAGNL GVLIPVIAVL
     TRRLPPIKEA KPRLQKLFRD FWLYSVLMGF AVEGSGLWPE EWYEGVCEIA TKSPLLTFPS
     KEPLRSVLQY NSAMKNDTVT PAELSELRST IINLLDPPPE VSALINKLDF AMSTYLLSVY
     RLEYMRVLRS TDPDRFQVMF CYFEDKAIQK DKSGMMQCVI AVADKVFDAF LNMMAEKAKT
     KENEEELERH AQFLLVNFNH IHKRIRRVAD KYLSGLVDKF PHLLWSGTVL KTMLDILQTL
     SLSLSADIHK DQPYYDIPDA PYRITVPDTY EARESIVKDF AARCGMILQE AMKWAPTVTK
     SHLQEYLNKH QNWVSGLSQH TGLAMATESI LHFAGYNKQN TTLGATQLTE RPACVKKDYS
     NFMASLNLRN RYAGEVHGMI RFSGATGQMS DLNKMMVQDL ITALDHSHPQ HYTQAMFKLT
     AMLISSKDCD PQLLHHLCWG PLRMFNEHGM ETALACWEWL LAGKNGVEVP FMREMAGAWH
     MTVEQKFGLF SVETKEADPL AASEASQPRP CPPEVTPHYI WIDFLVQRFE IAKYCSSDQV
     EIFSSLLQRS MSLNIGGARG SMNRHVAAIG PRFKLLTLGL SLLHADVVPN ATIRNVLREK
     IYSTAFDYFS CPPKFPTQGE KRLREDISIM IKFWTAMFSD KKYLTASQLV PPDNQDTRSN
     LDITVGSRQQ ATQGWINTYP LSSGMSTISK KSGMSKKTNR GSQLHKYYMK RRTLLLSLLA
     TEIERLITWY NPLSAPELEL DQAGENSVAN WRSKYISLSE KQWKDNVNLA WSISPYLAVQ
     LPARFKNTEA IGNEVTRLVR LDPGAVSDVP EAIKFLVTWH TIDADAPELS HVLCWAPTDP
     PTGLSYFSSM YPPHPLTAQY GVKVLRSFPP DAILFYIPQI VQALRYDKMG YVREYILWAA
     AKSQLLAHQF IWNMKTNIYL DEEGHQKDPD IGDLLEQLVE EITGSLSGPA KDFYQREFDF
     FNKITNVSAI IKPYPKGDER KKACLSALSE VKVQPGCYLP SNPEAIVLDI DYKSGTPMQS
     AAKAPYLAKF KVKRCGVSEL EKEGLQCRSD AEDECFSQEA DGKKICWQAA IFKVGDDCRQ
     DMLALQIIDL FKNIFQLVGL DLFVFPYRVV ATAPGCGVIE CIPDCTSRDQ LGRQTDFGMY
     DYFTRQYGDE STLAFQQARY NFIRSMAAYS LLLFLLQIKD RHNGNIMLDK KGHIIHIDFG
     FMFESSPGGN LGWEPDIKLT DEMVMIMGGK MEATPFKWFM EMCVRGYLAV RPYMDAVVSL
     VTLMLDTGLP CFRGQTIKLL KHRFSPNMTE REAANFIMKV IQNCFLSNRS RTYDMIQYYQ
     NDIPY
 
 
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