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FOSLA_DROME
ID   FOSLA_DROME             Reviewed;         755 AA.
AC   P21525; A8MPI0; Q400M6; Q400M7; Q53YJ8; Q8T9E2; Q9BH37; Q9NBW7; Q9VAH5;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 4.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Transcription factor kayak, isoforms A/B/F;
DE   AltName: Full=AP-1;
DE   AltName: Full=Fos-related antigen;
DE            Short=Dfos;
DE            Short=dFra;
GN   Name=kay; Synonyms=Fra; ORFNames=CG15509;
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), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   INTERACTION WITH JRA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=2116361; DOI=10.1101/gad.4.5.822;
RA   Perkins K.K., Admon A., Patel N., Tjian R.;
RT   "The Drosophila Fos-related AP-1 protein is a developmentally regulated
RT   transcription factor.";
RL   Genes Dev. 4:822-834(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC   TISSUE=Embryo;
RA   Nairz K., Hafen E.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX   PubMed=11470538; DOI=10.1016/s0378-1119(01)00514-5;
RA   Rousseau E., Goldstein E.S.;
RT   "The gene structure of the Drosophila melanogaster homolog of the human
RT   proto-oncogene fos.";
RL   Gene 272:315-322(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), ALTERNATIVE PROMOTER USAGE,
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=18571877; DOI=10.1016/j.gene.2008.05.001;
RA   Hudson S.G., Goldstein E.S.;
RT   "The gene structure of the Drosophila melanogaster proto-oncogene, kayak,
RT   and its nested gene, fos-intronic gene.";
RL   Gene 420:76-81(2008).
RN   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Developmentally regulated transcription factor AP-1 binds and
CC       recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role
CC       in the function or determination of a particular subset of cells in the
CC       developing embryo. It is able to carry out its function either
CC       independently of or in conjunction with Jra.
CC       {ECO:0000269|PubMed:2116361}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with Jra. The kay-Jra heterodimer binds
CC       more stably to the AP-1 site than either of the two proteins alone.
CC   -!- INTERACTION:
CC       P21525; P18289: Jra; NbExp=3; IntAct=EBI-195448, EBI-159948;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC       ECO:0000269|PubMed:2116361}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC       Name=F;
CC         IsoId=P21525-5; Sequence=Displayed;
CC       Name=A; Synonyms=beta;
CC         IsoId=P21525-2; Sequence=VSP_017891;
CC       Name=B; Synonyms=gamma;
CC         IsoId=P21525-3; Sequence=VSP_017892;
CC       Name=D; Synonyms=alpha;
CC         IsoId=A8MPH9-1; Sequence=External;
CC       Name=sro; Synonyms=shroud;
CC         IsoId=A8MPH9-2; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Early expression in the embryo is mesodermal and
CC       some of this expression is localized to a region surrounding the
CC       cephalic furrow. Later in embryonic development expression is
CC       ectodermal, corresponding to muscle attachment sites. Also observed in
CC       part of the mid- and hindgut and in the anal pad.
CC       {ECO:0000269|PubMed:2116361}.
CC   -!- DEVELOPMENTAL STAGE: Isoform A and isoform B are expressed both
CC       maternally and zygotically. Zygotically expressed throughout
CC       embryogenesis, until second larval instar. Isoform A is more highly
CC       expressed than isoform B. {ECO:0000269|PubMed:18571877,
CC       ECO:0000269|PubMed:2116361}.
CC   -!- DISRUPTION PHENOTYPE: Loss of isoform A causes embryonic lethality.
CC       {ECO:0000269|PubMed:18571877}.
CC   -!- MISCELLANEOUS: Mammals typically have four copies of fos, Drosophila
CC       has a single gene with multiple transcription start sites giving rise
CC       to multiple protein isoforms.
CC   -!- MISCELLANEOUS: [Isoform A]: Produced by alternative promoter usage.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform B]: Produced by alternative promoter usage.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR   EMBL; X54143; CAA38082.1; -; mRNA.
DR   EMBL; AF238310; AAF69496.1; -; mRNA.
DR   EMBL; AY574373; AAS87366.1; -; mRNA.
DR   EMBL; AH010388; AAK11268.2; -; mRNA.
DR   EMBL; AF332660; AAK11267.2; -; mRNA.
DR   EMBL; DQ858476; ABI74758.1; -; mRNA.
DR   EMBL; AE014297; AAZ83992.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAZ83993.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAZ83994.2; -; Genomic_DNA.
DR   EMBL; AY069805; AAL39950.1; -; mRNA.
DR   PIR; A35847; A35847.
DR   RefSeq; NP_001027577.2; NM_001032405.4. [P21525-5]
DR   RefSeq; NP_001027578.1; NM_001032406.2. [P21525-3]
DR   RefSeq; NP_001027579.1; NM_001032407.3. [P21525-2]
DR   AlphaFoldDB; P21525; -.
DR   SMR; P21525; -.
DR   BioGRID; 533679; 67.
DR   DIP; DIP-22245N; -.
DR   IntAct; P21525; 2.
DR   STRING; 7227.FBpp0288515; -.
DR   iPTMnet; P21525; -.
DR   PaxDb; P21525; -.
DR   PRIDE; P21525; -.
DR   DNASU; 3772082; -.
DR   EnsemblMetazoa; FBtr0099989; FBpp0084844; FBgn0001297. [P21525-2]
DR   EnsemblMetazoa; FBtr0099990; FBpp0084846; FBgn0001297. [P21525-3]
DR   EnsemblMetazoa; FBtr0290076; FBpp0288515; FBgn0001297. [P21525-5]
DR   GeneID; 3772082; -.
DR   KEGG; dme:Dmel_CG33956; -.
DR   CTD; 3772082; -.
DR   FlyBase; FBgn0001297; kay.
DR   VEuPathDB; VectorBase:FBgn0001297; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   InParanoid; P21525; -.
DR   OMA; YQNGHIM; -.
DR   PhylomeDB; P21525; -.
DR   Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
DR   Reactome; R-DME-209409; Formation of the nuclear AP-1 transcription factor 'scaffolding complex'.
DR   Reactome; R-DME-209425; Transcriptional activtion by AP-1 transcription factor.
DR   Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-DME-450341; Activation of the AP-1 family of transcription factors.
DR   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   SignaLink; P21525; -.
DR   BioGRID-ORCS; 3772082; 2 hits in 3 CRISPR screens.
DR   ChiTaRS; kay; fly.
DR   GenomeRNAi; 3772082; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0001297; Expressed in wing disc and 50 other tissues.
DR   ExpressionAtlas; P21525; baseline and differential.
DR   Genevisible; P21525; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0035976; C:transcription factor AP-1 complex; IPI:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA: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:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0048674; P:collateral sprouting of injured axon; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:BHF-UCL.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:FlyBase.
DR   GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR   GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR   GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR   GO; GO:0007297; P:ovarian follicle cell migration; IMP:FlyBase.
DR   GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR   GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; HMP:FlyBase.
DR   GO; GO:1903688; P:positive regulation of border follicle cell migration; IGI:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0007464; P:R3/R4 cell fate commitment; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009611; P:response to wounding; IMP:FlyBase.
DR   GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR   GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR   GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR23351; PTHR23351; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative promoter usage; Alternative splicing;
KW   Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..755
FT                   /note="Transcription factor kayak, isoforms A/B/F"
FT                   /id="PRO_0000076478"
FT   DOMAIN          418..481
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          23..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..439
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          446..453
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          510..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         1..234
FT                   /note="MKNLNGRTHNACYHPYYHQSLHFAQQQQQQQQHHLQQQQQHMQQQQQQQQAP
FT                   QQQLRHQQRQLPTQPAYQQSQSVAHNAFPLRSSSNNYGHVASSAYAASSGSHNSNNAAA
FT                   MAAVCQMQNFFNQQQQQQQQLEFNNNCMPINYYQQQQQQHYPSESQSSASGWNPETPGQ
FT                   AQLALTATTCNTTAAATCNTTAAATTSTTATSAAAGSDNNHSDNFAMDASEIATFLANE
FT                   LFLQQ -> MKVKVERTTKKPAIRKPEDPDPAEEDRVKMVQDDPEDQENQAVDEEELDF
FT                   LPADLSAAISTATTKIATPTRNLI (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:11470538,
FT                   ECO:0000303|PubMed:2116361, ECO:0000303|Ref.2"
FT                   /id="VSP_017891"
FT   VAR_SEQ         1..234
FT                   /note="MKNLNGRTHNACYHPYYHQSLHFAQQQQQQQQHHLQQQQQHMQQQQQQQQAP
FT                   QQQLRHQQRQLPTQPAYQQSQSVAHNAFPLRSSSNNYGHVASSAYAASSGSHNSNNAAA
FT                   MAAVCQMQNFFNQQQQQQQQLEFNNNCMPINYYQQQQQQHYPSESQSSASGWNPETPGQ
FT                   AQLALTATTCNTTAAATCNTTAAATTSTTATSAAAGSDNNHSDNFAMDASEIATFLANE
FT                   LFLQQ -> MTLDSYNIFNDEYLFNMPLSPLPKV (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569,
FT                   ECO:0000303|PubMed:18571877"
FT                   /id="VSP_017892"
FT   CONFLICT        613
FT                   /note="A -> P (in Ref. 1; CAA38082)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        P21525-2:19
FT                   /note="D -> N (in Ref. 3; AAK11267/AAK11268)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   755 AA;  80579 MW;  6E21F0460B626DAA CRC64;
     MKNLNGRTHN ACYHPYYHQS LHFAQQQQQQ QQHHLQQQQQ HMQQQQQQQQ APQQQLRHQQ
     RQLPTQPAYQ QSQSVAHNAF PLRSSSNNYG HVASSAYAAS SGSHNSNNAA AMAAVCQMQN
     FFNQQQQQQQ QLEFNNNCMP INYYQQQQQQ HYPSESQSSA SGWNPETPGQ AQLALTATTC
     NTTAAATCNT TAAATTSTTA TSAAAGSDNN HSDNFAMDAS EIATFLANEL FLQQLGNFET
     GQSVLTLTTP TLTPTTTRNI EDTLGHLLSD TQTDRVAGCA GFAVPKVLPN AIDVLGMGIP
     TGVSSLPLQQ TFDLSLGQGS ESEDSNASYN DTQMNEEQDT TDTSSAHTDS TSYQAGHIMA
     GSVNGGGVNN FSNVLAAVSS SRGSASVGSS NANTSNTPAR RGGGRRPNRS TNMTPEEEQK
     RAVRRERNKQ AAARCRKRRV DQTNELTEEV EQLEKRGESM RKEIEVLTNS KNQLEYLLAT
     HRATCQKIRS DMLSVVTCNG LIAPAGLLSA GSSGSGASSH HNHNSNDSSN GTITGMDATL
     NSTGRSNSPL DLKPAANIDS LLMHIKDEPL DGAIDSGSSL DQDGPPPSKR ITLPPMSTMP
     HVHLSTILTP TGASSGSLQT PITSTAPGGF GSAFPVTSNG SSINNINSIG NNMNSPTLNA
     HNKVPKERPN TLAFQRPLGQ MHLTMANNKA GGPTQIQGVP IQTPSTGTFN FDSLMDGGTG
     LTPVSGPLVP NSSSTNKHPL ELPTPTAEPS KLVSL
 
 
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