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YTDC2_MOUSE
ID   YTDC2_MOUSE             Reviewed;        1445 AA.
AC   B2RR83;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=3'-5' RNA helicase YTHDC2 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000269|PubMed:29360036};
DE   AltName: Full=Keen to exit meiosis leaving testes under-populated protein {ECO:0000303|PubMed:29360036};
DE            Short=Ketu {ECO:0000303|PubMed:29360036};
DE   AltName: Full=YTH domain-containing protein C2 {ECO:0000303|PubMed:28809393};
DE            Short=mYTHDC2 {ECO:0000303|PubMed:29033321};
GN   Name=Ythdc2 {ECO:0000303|PubMed:28809393, ECO:0000312|MGI:MGI:2448561};
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 MRNA].
RC   TISSUE=Brain;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1278 AND SER-1282, AND
RP   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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1104; SER-1105; SER-1107;
RP   SER-1278; SER-1282 AND SER-1296, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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   [4]
RP   FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=28809393; DOI=10.1038/cr.2017.99;
RA   Hsu P.J., Zhu Y., Ma H., Guo Y., Shi X., Liu Y., Qi M., Lu Z., Shi H.,
RA   Wang J., Cheng Y., Luo G., Dai Q., Liu M., Guo X., Sha J., Shen B., He C.;
RT   "Ythdc2 is an N(6)-methyladenosine binding protein that regulates mammalian
RT   spermatogenesis.";
RL   Cell Res. 27:1115-1127(2017).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH MEIOC.
RX   PubMed=28380054; DOI=10.1371/journal.pgen.1006704;
RA   Soh Y.Q.S., Mikedis M.M., Kojima M., Godfrey A.K., de Rooij D.G.,
RA   Page D.C.;
RT   "Meioc maintains an extended meiotic prophase I in mice.";
RL   PLoS Genet. 13:E1006704-E1006704(2017).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   RNA-BINDING, AND INTERACTION WITH MEIOC.
RX   PubMed=29087293; DOI=10.7554/elife.26116;
RA   Bailey A.S., Batista P.J., Gold R.S., Chen Y.G., de Rooij D.G., Chang H.Y.,
RA   Fuller M.T.;
RT   "The conserved RNA helicase YTHDC2 regulates the transition from
RT   proliferation to differentiation in the germline.";
RL   Elife 6:0-0(2017).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   AND INTERACTION WITH XRN1 AND MEIOC.
RX   PubMed=29033321; DOI=10.1016/j.molcel.2017.09.021;
RA   Wojtas M.N., Pandey R.R., Mendel M., Homolka D., Sachidanandam R.,
RA   Pillai R.S.;
RT   "Regulation of m6A transcripts by the 3'-5' RNA helicase YTHDC2 is
RT   essential for a successful meiotic program in the mammalian germline.";
RL   Mol. Cell 68:374-387(2017).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF HIS-327.
RX   PubMed=29360036; DOI=10.7554/elife.30919;
RA   Jain D., Puno M.R., Meydan C., Lailler N., Mason C.E., Lima C.D.,
RA   Anderson K.V., Keeney S.;
RT   "Ketu mutant mice uncover an essential meiotic function for the ancient RNA
RT   helicase YTHDC2.";
RL   Elife 7:0-0(2018).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=32470506; DOI=10.1016/j.gene.2020.144810;
RA   Zeng M., Dai X., Liang Z., Sun R., Huang S., Luo L., Li Z.;
RT   "Critical roles of mRNA m6A modification and YTHDC2 expression for meiotic
RT   initiation and progression in female germ cells.";
RL   Gene 753:144810-144810(2020).
CC   -!- FUNCTION: 3'-5' RNA helicase that plays a key role in the male and
CC       female germline by promoting transition from mitotic to meiotic
CC       divisions in stem cells (PubMed:28380054, PubMed:28809393,
CC       PubMed:29033321, PubMed:29087293, PubMed:29360036, PubMed:32470506).
CC       Specifically recognizes and binds N6-methyladenosine (m6A)-containing
CC       RNAs, a modification present at internal sites of mRNAs and some non-
CC       coding RNAs that plays a role in the efficiency of RNA processing and
CC       stability (PubMed:29360036). Essential for ensuring a successful
CC       progression of the meiotic program in the germline by regulating the
CC       level of m6A-containing RNAs (PubMed:29033321). Acts by binding and
CC       promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase
CC       activity is required for this process and RNA degradation may be
CC       mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both
CC       spermatogenesis and oogenesis (PubMed:28809393, PubMed:29033321).
CC       {ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:28809393,
CC       ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293,
CC       ECO:0000269|PubMed:29360036, ECO:0000269|PubMed:32470506}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000269|PubMed:29360036};
CC   -!- SUBUNIT: Interacts with MEIOC; binds transcripts that regulate the
CC       mitotic cell cycle inhibiting progression into metaphase, thereby
CC       allowing meiotic prophase to proceed normally (PubMed:28380054,
CC       PubMed:29087293). Interacts (via ANK repeats) with XRN1 (By
CC       similarity). Interacts with ZCCHC4 (By similarity). Associates with the
CC       small ribosomal subunit (By similarity). {ECO:0000250|UniProtKB:Q9H6S0,
CC       ECO:0000269|PubMed:28380054, ECO:0000269|PubMed:29087293}.
CC   -!- INTERACTION:
CC       B2RR83; A2AG06: Meioc; NbExp=4; IntAct=EBI-8572369, EBI-11664020;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29033321,
CC       ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036}. Cytoplasm,
CC       perinuclear region {ECO:0000250|UniProtKB:Q9H6S0}.
CC   -!- TISSUE SPECIFICITY: Present in male and female germ cells (at protein
CC       level) (PubMed:29033321, PubMed:32470506). Highly expressed in testis
CC       (PubMed:28809393, PubMed:29033321, PubMed:29087293, PubMed:29360036).
CC       Not detected in spermatogonia next to the tubule wall but is strongly
CC       expressed in spermatocytes, suggesting that it is up-regulated in germ
CC       cells upon entry into meiosis (at protein level) (PubMed:29087293).
CC       {ECO:0000269|PubMed:28809393, ECO:0000269|PubMed:29033321,
CC       ECO:0000269|PubMed:29087293, ECO:0000269|PubMed:29360036,
CC       ECO:0000269|PubMed:32470506}.
CC   -!- DEVELOPMENTAL STAGE: Expression rises between 7 and 12 d.p.p. and
CC       remains steady through adulthood. {ECO:0000269|PubMed:28809393}.
CC   -!- DOMAIN: The YTH domain mediates RNA-binding. It recognizes and binds
CC       N6-methyladenosine (m6A)-containing RNAs.
CC       {ECO:0000250|UniProtKB:Q9H6S0}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and reach adulthood
CC       (PubMed:28809393, PubMed:29087293, PubMed:29033321). However, both male
CC       and female mice are infertile; male mice have smaller testes, and
CC       female mice have smaller ovaries and show progressive loss of germ
CC       cells (PubMed:28809393, PubMed:29087293, PubMed:29033321). Mutant germ
CC       cells enter meiosis but proceed prematurely to aberrant metaphase and
CC       apoptosis, and display defects in transitioning from spermatogonial to
CC       meiotic gene expression programs (PubMed:29087293, PubMed:29033321).
CC       Mutant testes reveal an up-regulation of N6-methyladenosine (m6A)-
CC       enriched transcripts (PubMed:29033321). {ECO:0000269|PubMed:28809393,
CC       ECO:0000269|PubMed:29033321, ECO:0000269|PubMed:29087293,
CC       ECO:0000269|PubMed:29360036}.
CC   -!- MISCELLANEOUS: 'Ketu' is a harbinger of misfortune in Vedic mythology
CC       (PubMed:29360036). {ECO:0000303|PubMed:29360036}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC138263; AAI38264.1; -; mRNA.
DR   EMBL; BC171951; AAI71951.1; -; mRNA.
DR   CCDS; CCDS50278.1; -.
DR   RefSeq; NP_001156485.1; NM_001163013.1.
DR   AlphaFoldDB; B2RR83; -.
DR   SMR; B2RR83; -.
DR   BioGRID; 232185; 7.
DR   IntAct; B2RR83; 4.
DR   MINT; B2RR83; -.
DR   STRING; 10090.ENSMUSP00000048340; -.
DR   iPTMnet; B2RR83; -.
DR   PhosphoSitePlus; B2RR83; -.
DR   EPD; B2RR83; -.
DR   MaxQB; B2RR83; -.
DR   PaxDb; B2RR83; -.
DR   PeptideAtlas; B2RR83; -.
DR   PRIDE; B2RR83; -.
DR   ProteomicsDB; 275234; -.
DR   Antibodypedia; 48855; 39 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000037763; ENSMUSP00000048340; ENSMUSG00000034653.
DR   GeneID; 240255; -.
DR   KEGG; mmu:240255; -.
DR   UCSC; uc008evb.2; mouse.
DR   CTD; 64848; -.
DR   MGI; MGI:2448561; Ythdc2.
DR   VEuPathDB; HostDB:ENSMUSG00000034653; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   eggNOG; KOG0922; Eukaryota.
DR   eggNOG; KOG1902; Eukaryota.
DR   GeneTree; ENSGT00940000155826; -.
DR   HOGENOM; CLU_001832_1_6_1; -.
DR   InParanoid; B2RR83; -.
DR   OMA; WQNLFIK; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; B2RR83; -.
DR   TreeFam; TF318311; -.
DR   BioGRID-ORCS; 240255; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Ythdc2; mouse.
DR   PRO; PR:B2RR83; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; B2RR83; protein.
DR   Bgee; ENSMUSG00000034653; Expressed in secondary oocyte and 222 other tissues.
DR   ExpressionAtlas; B2RR83; baseline and differential.
DR   Genevisible; B2RR83; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; ISO:MGI.
DR   GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR   GO; GO:0051729; P:germline cell cycle switching, mitotic to meiotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0048599; P:oocyte development; IMP:UniProtKB.
DR   GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:MGI.
DR   GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR   GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR   CDD; cd06007; R3H_DEXH_helicase; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 3.30.1370.50; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR034083; R3H_DEXH_helicase.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR007275; YTH_domain.
DR   InterPro; IPR031083; YTHDC2-like.
DR   PANTHER; PTHR18934:SF100; PTHR18934:SF100; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF01424; R3H; 1.
DR   Pfam; PF04146; YTH; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF82708; SSF82708; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS50882; YTH; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; ATP-binding; Cytoplasm; Differentiation; Helicase; Hydrolase;
KW   Meiosis; Nucleotide-binding; Oogenesis; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding; Spermatogenesis.
FT   CHAIN           1..1445
FT                   /note="3'-5' RNA helicase YTHDC2"
FT                   /id="PRO_0000378275"
FT   DOMAIN          53..121
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT   DOMAIN          218..384
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REPEAT          521..553
FT                   /note="ANK 1"
FT   REPEAT          554..586
FT                   /note="ANK 2"
FT   DOMAIN          627..799
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1303..1433
FT                   /note="YTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1179..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           331..334
FT                   /note="DEAH box"
FT   COMPBIAS        1179..1193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1247..1267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1309..1311
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT                   /ligand_part_id="ChEBI:CHEBI:74449"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT   BINDING         1325
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT                   /ligand_part_id="ChEBI:CHEBI:74449"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT   BINDING         1375
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT                   /ligand_part_id="ChEBI:CHEBI:74449"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT   MOD_RES         1104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MUTAGEN         327
FT                   /note="H->R: In ketu; homozygotes mice are both male- and
FT                   female-sterile. In the testis, mutant germ cells carry out
FT                   an abortive attempt at meiosis: They express hallmark
FT                   meiotic proteins and initiate recombination, but fail to
FT                   fully extinguish the spermatogonial mitotic division
FT                   program, proceed prematurely to an aberrant metaphase-like
FT                   state, and undergo apoptosis. The mutation probably causes
FT                   misfolding or protein aggregation. Slightly reduced
FT                   helicase activity."
FT                   /evidence="ECO:0000269|PubMed:29360036"
SQ   SEQUENCE   1445 AA;  161092 MW;  A693BF57FEAF7511 CRC64;
     MSRPSSVSPR PPAPSGGGTG GGGGGSGGGG GGGGGGPASC GPGGGGRAKG LKDIRIDEEV
     KIAVNIALER FRYGDQREME FPSSLTSTER AFIHRLSQSL GLVSKSKGKG ANRYLTVKKK
     DGSETAHAMM TCNLTHNTKH AVRSLIQRFP VTNKERTELL PKTERGNVFA VEAENREMSK
     TSGRLNNGIP QVPVKRGESE FDSFRQSLPV FEKQEEIVKI IKENKVVLIV GETGSGKTTQ
     IPQFLLDDCF KNGIPCRIFC TQPRRLAAIA VAERVAAERR ERIGQTIGYQ IRLESRVSPK
     TLLTFCTNGV LLRTLMAGDS TLSTVTHVIV DEVHERDRFS DFLLTKLRDL LQKHPTLKLI
     LSSAALDVNL FIRYFGSCPV IYIQGRPFEV KEMFLEDILR TTGYTNKEML KYKKEKQREE
     KQQTTLTEWY SAQENTFKPE SQRQRAVASV SEEYDLLDDG GDAVFSQLTE KDVNCLEPWL
     IKEMDACLSD IWLHKDVDAF AQVFHLILTE NVSVDYRHSE TSATALMVAA GRGFTSQVEQ
     LISMGANVHS KASNGWMALD WAKHFGQTEI VDLLESYSAS LEFGNLDESS LVQTNGNDLS
     AEDRELLKAY HHSFDDEKVD LDLIMHLLYN ICHSCDAGAI LIFLPGYDEI VGLRDRILFD
     DKRFADNTHR YQVFMLHSNM QTSDQKKVLK NPPAGVRKII LSTNIAETSI TVNDVVFVID
     SGKVKEKSFD ALNFVTMLKM VWISKASAIQ RKGRAGRCRP GICFRLFSRL RFQNMLEFQT
     PELLRMPLQE LCLHTKLLAP VNCTIADFLM KAPEPPPALI VRNAVQMLKT IDAMDAWEDL
     TELGYHLADL PVEPHLGKMV LCAVVLKCLD PILTIACTLA YRDPFVLPTQ ASQKRAAMLC
     RKRFTAGTFS DHMALLRAFQ AWQKARSDGW ERAFCEKNFL SQATMEIIIG MRTQLLGQLR
     ASGFVRARGG GDIRDVNTNS ENWAVVKAAL VAGMYPNLVH VDRENVILTG PKEKKVRFHP
     TSVLSQPQYK KIPPANGQAA AIQALPTDWL IYDEMTRAHR IANIRCCSAV TPVTVLVFCG
     PARLASNALQ EPSSFRADGI PNDSSDSEME DRTTANLAAL KLDEWLNFKL EPEAASLLLQ
     LRQKWHSLFL RRMRAPSKPW SQVDEATIRA IIAVLSTEEQ SAGLQQPSGI GQRPRPMSSE
     ELPLASSWRS NNSRKSTADT EFADGSTTGE RVLMKSPSPA LHPPQKYKDR GILHPKRSTD
     DRSDQSSVKS TDSSSYPSPC ASPSPPSSGK GSKSPSPRPN MPIRYFIMKS SNLRNLEISQ
     QKGIWSTTPS NERKLNRAFW ESSMVYLVFS VQGSGHFQGF SRMSSEIGRE KSQDWGSAGL
     GGVFKVEWIR KESLPFQFAH HLLNPWNDNK KVQISRDGQE LEPQVGEQLL QLWERLPLGE
     KTTSD
 
 
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