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PANG1_DROME
ID   PANG1_DROME             Reviewed;         751 AA.
AC   P91943; A0AVW4; A4V148; B5RJS3; O02548; Q0KIE9; Q59DP5; Q5BHZ3; Q6W492;
AC   Q6W493; Q6W494; Q6W495; Q6W4A6; Q6W4B4; Q9V4B0;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 196.
DE   RecName: Full=Protein pangolin, isoforms A/H/I/S;
DE   AltName: Full=dTCF;
GN   Name=pan; Synonyms=TCF; ORFNames=CG34403;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9118222; DOI=10.1016/s0092-8674(00)81925-x;
RA   van de Wetering M., Cavallo R.A., Dooijes D., van Beest M., van Es J.,
RA   Loureiro J., Ypma A., Hursh D., Jones T., Bejsovec A., Peifer M.,
RA   Mortin M., Clevers H.;
RT   "Armadillo coactivates transcription driven by the product of the
RT   Drosophila segment polarity gene dTCF.";
RL   Cell 88:789-799(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RX   PubMed=9039917; DOI=10.1038/385829a0;
RA   Brunner E., Peter O., Schweizer L., Basler K.;
RT   "Pangolin encodes a Lef-1 homologue that acts downstream of Armadillo to
RT   transduce the Wingless signal in Drosophila.";
RL   Nature 385:829-833(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 363-751 (ISOFORM J).
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-751.
RC   STRAIN=Crete24, Crete26, Crete30, Crete31, Crete35, Crete40, Crete42,
RC   Crete43, Crete44, Crete8, FTF1, FTF105, FTF14, FTF2, FTF20, FTF23, FTF26,
RC   FTF28, FTF5, FTF6, Zim11, Zim2, Zim30, and Zim53;
RX   PubMed=14668375; DOI=10.1093/genetics/165.3.1195;
RA   Sheldahl L.A., Weinreich D.M., Rand D.M.;
RT   "Recombination, dominance and selection on amino acid polymorphism in the
RT   Drosophila genome: contrasting patterns on the X and fourth chromosomes.";
RL   Genetics 165:1195-1208(2003).
RN   [7]
RP   FUNCTION, INTERACTION WITH ARM AND GRO, AND SUBCELLULAR LOCATION.
RX   PubMed=9783586; DOI=10.1038/26982;
RA   Cavallo R.A., Cox R.T., Moline M.M., Roose J., Polevoy G.A., Clevers H.,
RA   Peifer M., Bejsovec A.;
RT   "Drosophila Tcf and Groucho interact to repress Wingless signalling
RT   activity.";
RL   Nature 395:604-608(1998).
CC   -!- FUNCTION: Segment polarity protein. Functions together with arm to
CC       transduce the Wingless (Wg) signal in embryos and in developing adult
CC       tissues. Acts as a transcriptional activator, but in the absence of
CC       arm, it binds to gro and acts as a transcriptional repressor of wg-
CC       responsive genes. {ECO:0000269|PubMed:9039917,
CC       ECO:0000269|PubMed:9118222, ECO:0000269|PubMed:9783586}.
CC   -!- SUBUNIT: Binds to the beta-catenin homolog arm or to gro.
CC   -!- INTERACTION:
CC       P91943; P18824: arm; NbExp=2; IntAct=EBI-147301, EBI-216128;
CC       P91943; Q9W0N9: ebd1; NbExp=4; IntAct=EBI-147301, EBI-141287;
CC       P91943; P16371: gro; NbExp=2; IntAct=EBI-147301, EBI-153866;
CC       P91943-5; Q6NP72: Dmel\CG13220; NbExp=4; IntAct=EBI-15112213, EBI-146896;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:9783586}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=A; Synonyms=C, D, E, F, G;
CC         IsoId=P91943-3; Sequence=Displayed;
CC       Name=H;
CC         IsoId=P91943-4; Sequence=VSP_021967;
CC       Name=S;
CC         IsoId=P91943-6; Sequence=VSP_047713;
CC       Name=I;
CC         IsoId=P91943-5; Sequence=VSP_021967, VSP_021968, VSP_021969;
CC       Name=J;
CC         IsoId=Q8IMA8-1; Sequence=External;
CC   -!- DISRUPTION PHENOTYPE: Flies exhibit a segment polarity phenotype and
CC       altered expression of the wg target genes en and Ubx.
CC       {ECO:0000269|PubMed:9118222}.
CC   -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR   EMBL; Y09125; CAA70343.1; -; mRNA.
DR   EMBL; U88538; AAC47464.1; -; mRNA.
DR   EMBL; AE014135; AAF59371.2; -; Genomic_DNA.
DR   EMBL; AE014135; AAN06545.1; -; Genomic_DNA.
DR   EMBL; AE014135; AAN06548.2; -; Genomic_DNA.
DR   EMBL; AE014135; AFH06766.1; -; Genomic_DNA.
DR   EMBL; AE014135; AAX52517.1; -; Genomic_DNA.
DR   EMBL; AE014135; ABC65830.1; -; Genomic_DNA.
DR   EMBL; BT021431; AAX33579.1; -; mRNA.
DR   EMBL; BT029282; ABK30919.1; -; mRNA.
DR   EMBL; BT044547; ACI03583.1; -; mRNA.
DR   EMBL; BT053747; ACK77665.1; -; mRNA.
DR   EMBL; AY312729; AAQ67543.1; -; Genomic_DNA.
DR   EMBL; AY312730; AAQ67544.1; -; Genomic_DNA.
DR   EMBL; AY312731; AAQ67545.1; -; Genomic_DNA.
DR   EMBL; AY312732; AAQ67546.1; -; Genomic_DNA.
DR   EMBL; AY312733; AAQ67547.1; -; Genomic_DNA.
DR   EMBL; AY312734; AAQ67548.1; -; Genomic_DNA.
DR   EMBL; AY312735; AAQ67549.1; -; Genomic_DNA.
DR   EMBL; AY312736; AAQ67550.1; -; Genomic_DNA.
DR   EMBL; AY312737; AAQ67551.1; -; Genomic_DNA.
DR   EMBL; AY312738; AAQ67552.1; -; Genomic_DNA.
DR   EMBL; AY312739; AAQ67553.1; -; Genomic_DNA.
DR   EMBL; AY312740; AAQ67554.1; -; Genomic_DNA.
DR   EMBL; AY312741; AAQ67555.1; -; Genomic_DNA.
DR   EMBL; AY312742; AAQ67556.1; -; Genomic_DNA.
DR   EMBL; AY312743; AAQ67557.1; -; Genomic_DNA.
DR   EMBL; AY312744; AAQ67558.1; -; Genomic_DNA.
DR   EMBL; AY312745; AAQ67559.1; -; Genomic_DNA.
DR   EMBL; AY312746; AAQ67560.1; -; Genomic_DNA.
DR   EMBL; AY312747; AAQ67561.1; -; Genomic_DNA.
DR   EMBL; AY312748; AAQ67562.1; -; Genomic_DNA.
DR   EMBL; AY312749; AAQ67563.1; -; Genomic_DNA.
DR   EMBL; AY312750; AAQ67564.1; -; Genomic_DNA.
DR   EMBL; AY312751; AAQ67565.1; -; Genomic_DNA.
DR   EMBL; AY312752; AAQ67566.1; -; Genomic_DNA.
DR   RefSeq; NP_001014685.1; NM_001014685.3. [P91943-4]
DR   RefSeq; NP_001033798.1; NM_001038709.3. [P91943-5]
DR   RefSeq; NP_001245406.1; NM_001258477.2. [P91943-3]
DR   RefSeq; NP_524619.3; NM_079880.6. [P91943-3]
DR   RefSeq; NP_726522.1; NM_166718.3. [P91943-3]
DR   RefSeq; NP_726524.1; NM_166720.3. [P91943-3]
DR   RefSeq; NP_726527.2; NM_166723.3. [P91943-6]
DR   AlphaFoldDB; P91943; -.
DR   SMR; P91943; -.
DR   BioGRID; 68607; 71.
DR   DIP; DIP-19970N; -.
DR   IntAct; P91943; 35.
DR   MINT; P91943; -.
DR   DNASU; 43769; -.
DR   EnsemblMetazoa; FBtr0089159; FBpp0088226; FBgn0085432. [P91943-3]
DR   EnsemblMetazoa; FBtr0089161; FBpp0088228; FBgn0085432. [P91943-3]
DR   EnsemblMetazoa; FBtr0089162; FBpp0088229; FBgn0085432. [P91943-3]
DR   EnsemblMetazoa; FBtr0100245; FBpp0099631; FBgn0085432. [P91943-4]
DR   EnsemblMetazoa; FBtr0100246; FBpp0099632; FBgn0085432. [P91943-5]
DR   EnsemblMetazoa; FBtr0309803; FBpp0301556; FBgn0085432. [P91943-3]
DR   EnsemblMetazoa; FBtr0334301; FBpp0306416; FBgn0085432. [P91943-6]
DR   GeneID; 43769; -.
DR   KEGG; dme:Dmel_CG34403; -.
DR   CTD; 43769; -.
DR   FlyBase; FBgn0085432; pan.
DR   VEuPathDB; VectorBase:FBgn0085432; -.
DR   GeneTree; ENSGT00940000168653; -.
DR   OMA; YMEAING; -.
DR   Reactome; R-DME-209421; Transcription activation by ARM.
DR   Reactome; R-DME-209441; WG ligand not bound to FZ receptors.
DR   SignaLink; P91943; -.
DR   BioGRID-ORCS; 43769; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; pan; fly.
DR   GenomeRNAi; 43769; -.
DR   Proteomes; UP000000803; Chromosome 4.
DR   Bgee; FBgn0085432; Expressed in brain and 32 other tissues.
DR   ExpressionAtlas; P91943; baseline and differential.
DR   Genevisible; P91943; DM.
DR   GO; GO:1990907; C:beta-catenin-TCF complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005667; C:transcription regulator complex; IPI:FlyBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR   GO; GO:0019900; F:kinase binding; IPI:FlyBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:FlyBase.
DR   GO; GO:0007507; P:heart development; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0007500; P:mesodermal cell fate determination; TAS:FlyBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEP:FlyBase.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0072091; P:regulation of stem cell proliferation; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR   GO; GO:0007367; P:segment polarity determination; IEA:UniProtKB-KW.
DR   GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR013558; CTNNB1-bd_N.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR028782; Pangolin-like.
DR   InterPro; IPR024940; TCF/LEF.
DR   PANTHER; PTHR10373; PTHR10373; 1.
DR   PANTHER; PTHR10373:SF38; PTHR10373:SF38; 1.
DR   Pfam; PF08347; CTNNB1_binding; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Developmental protein; DNA-binding;
KW   Nucleus; Reference proteome; Repressor; Segmentation polarity protein;
KW   Transcription; Transcription regulation; Wnt signaling pathway.
FT   CHAIN           1..751
FT                   /note="Protein pangolin, isoforms A/H/I/S"
FT                   /id="PRO_0000048601"
FT   DNA_BIND        273..341
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..53
FT                   /note="Beta-catenin binding site"
FT                   /evidence="ECO:0000250"
FT   REGION          46..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           351..357
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        48..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         313..364
FT                   /note="ELSREEQSKYYEKARQERQLHMELYPGWSARDNYGYVSKKKKRKKDRSTTDS
FT                   -> ALGREEQAKYYELARRERQLHMQMYPDWSSRTNASRGKKRKRKQDTND (in
FT                   isoform H and isoform I)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_021967"
FT   VAR_SEQ         390..414
FT                   /note="RKKKCIRYMEALNGNGPAEDGSCFD -> YVLPLFLFTMLYILLQMDLQDSR
FT                   KN (in isoform I)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_021968"
FT   VAR_SEQ         415..751
FT                   /note="Missing (in isoform I)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_021969"
FT   VAR_SEQ         713..730
FT                   /note="Missing (in isoform S)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047713"
SQ   SEQUENCE   751 AA;  81892 MW;  1C6E5A0B36017143 CRC64;
     MPHTHSRHGS SGDDLCSTDE VKIFKDEGDR EDEKISSENL LVEEKSSLID LTESEEKGHK
     ISRPDHSPVF NKLDTHAPSF NMGYLVSPYS YANGSPSGLP VTMANKIGLP PFFCHNADPL
     STPPPAHCGI PPYQLDPKMG LTRPALYPFA GGQYPYPMLS SDMSQVASWH TPSVYSASSF
     RTPYPSSLPI NTTLASDFPF RFSPSLLPSV HATSHHVINA HSAIVGVSSK QECGVQDPTT
     NNRYPRNLEA KHTSNAQSNE SKETTNDKKK PHIKKPLNAF MLYMKEMRAK VVAECTLKES
     AAINQILGRR WHELSREEQS KYYEKARQER QLHMELYPGW SARDNYGYVS KKKKRKKDRS
     TTDSGGNNMK KCRARFGLDQ QSQWCKPCRR KKKCIRYMEA LNGNGPAEDG SCFDEHGSQL
     SDDDEDDYDD DKLGGSCGSA DETNKIEDED SESLNQSMPS PGCLSGLSSL QSPSTTMSLA
     SPLNMNANSA TNVIFPASSN ALLIVGADQP TAQQRPTLVS TSGSSSGSTS SISTTPNTSS
     TVSPVTCMTG PCLGSSQERA MMLGNRFSHL GMGLSPPVVS TSTSKSEPFF KPHPTVCNNP
     IFALPSIGNC SLNISSMPNT SRNPIGANPR DINNPLSINQ LTKRREYKNV ELIEASESKT
     IVAHAATSII QHVAVNGYHA NHSLLNSNLG HLHHQLNNRT ENPNRSEQTM LSVSNHSVNS
     SECHKESDSQ AIVSSNPPNA GSSDNGVISV S
 
 
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