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A4_DROME
ID   A4_DROME                Reviewed;         887 AA.
AC   P14599; Q9TVV0; Q9U4H3; Q9W5F1;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 182.
DE   RecName: Full=Amyloid-beta-like protein;
DE   Flags: Precursor;
GN   Name=Appl; ORFNames=CG7727;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=2494667; DOI=10.1073/pnas.86.7.2478;
RA   Rosen D.R., Martin-Morris L., Luo L., White K.;
RT   "A Drosophila gene encoding a protein resembling the human beta-amyloid
RT   protein precursor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:2478-2482(1989).
RN   [2]
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   [3]
RP   GENOME REANNOTATION.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Ovary;
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=2127912; DOI=10.1242/dev.110.1.185;
RA   Martin-Morris L.E., White K.;
RT   "The Drosophila transcript encoded by the beta-amyloid protein precursor-
RT   like gene is restricted to the nervous system.";
RL   Development 110:185-195(1990).
RN   [7]
RP   FUNCTION, INTERACTION WITH APP-BP1, AND DISRUPTION PHENOTYPE.
RX   PubMed=16628230; DOI=10.1038/sj.cdd.4401935;
RA   Kim H.J., Kim S.H., Shim S.O., Park E., Kim C., Kim K., Tanouye M.A.,
RA   Yim J.;
RT   "Drosophila homolog of APP-BP1 (dAPP-BP1) interacts antagonistically with
RT   APPL during Drosophila development.";
RL   Cell Death Differ. 14:103-115(2007).
CC   -!- FUNCTION: During development, plays a role in the regulation of the
CC       neddylation pathway. Appl and APP-BP1 interact antagonistically during
CC       development. {ECO:0000269|PubMed:16628230}.
CC   -!- SUBUNIT: Interacts (via the intracellular domain, ICD) with APP-BP1.
CC       {ECO:0000269|PubMed:16628230}.
CC   -!- INTERACTION:
CC       P14599; Q9W0K0: Aplip1; NbExp=6; IntAct=EBI-74135, EBI-74120;
CC       P14599; P34082: Fas2; NbExp=3; IntAct=EBI-74135, EBI-868243;
CC       P14599; Q9GQQ6: X11L; NbExp=3; IntAct=EBI-74135, EBI-2027617;
CC       P14599; Q9VX41: X11L; NbExp=3; IntAct=EBI-74135, EBI-74153;
CC       P14599; Q9ERE9: Mapk8ip2; Xeno; NbExp=2; IntAct=EBI-74135, EBI-74576;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in postmitotic neurons in the central and
CC       peripheral nervous systems. Within the nervous system, transcripts are
CC       not observed in neuroblasts, newly generated neurons and at least one
CC       class of presumed glial cells. {ECO:0000269|PubMed:2127912,
CC       ECO:0000269|PubMed:2494667}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages.
CC       {ECO:0000269|PubMed:2127912, ECO:0000269|PubMed:2494667}.
CC   -!- DOMAIN: The NPTY motif mediates the interaction with clathrin (By
CC       similarity). The clathrin-binding site is essential for its association
CC       with X11-alpha, -beta, and -gamma. The sequence specific recognition
CC       extends to peptide residues that are C-terminal to the NPXY motif. This
CC       interaction appears to be independent of phosphorylation (By
CC       similarity). {ECO:0000250, ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Overexpression inhibits the Nedd8 conjugation
CC       pathway, disrupts the normal bristle pattern in the fly thorax, and
CC       induces apoptosis in wing imaginal disks.
CC       {ECO:0000269|PubMed:16628230}.
CC   -!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01217}.
CC   -!- CAUTION: Was originally (PubMed:2494667) thought to be vnd but further
CC       analysis (PubMed:2127912) has clearly shown that it corresponds to
CC       Appl. {ECO:0000305|PubMed:2127912, ECO:0000305|PubMed:2494667}.
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DR   EMBL; J04516; AAA28874.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAF45520.2; -; Genomic_DNA.
DR   EMBL; AL031883; CAA21409.1; -; Genomic_DNA.
DR   EMBL; AL022139; CAA21409.1; JOINED; Genomic_DNA.
DR   EMBL; AL022139; CAA18093.1; -; Genomic_DNA.
DR   EMBL; AL031883; CAA18093.1; JOINED; Genomic_DNA.
DR   EMBL; AF181628; AAD55414.1; -; mRNA.
DR   EMBL; X55774; CAA39294.1; -; Genomic_DNA.
DR   EMBL; X55775; CAA39294.1; JOINED; Genomic_DNA.
DR   PIR; A32758; A32758.
DR   RefSeq; NP_476626.2; NM_057278.5.
DR   AlphaFoldDB; P14599; -.
DR   SMR; P14599; -.
DR   BioGRID; 57571; 22.
DR   IntAct; P14599; 8.
DR   STRING; 7227.FBpp0298292; -.
DR   GlyGen; P14599; 5 sites.
DR   PaxDb; P14599; -.
DR   EnsemblMetazoa; FBtr0070109; FBpp0070104; FBgn0000108.
DR   GeneID; 31002; -.
DR   KEGG; dme:Dmel_CG7727; -.
DR   CTD; 31002; -.
DR   FlyBase; FBgn0000108; Appl.
DR   VEuPathDB; VectorBase:FBgn0000108; -.
DR   eggNOG; KOG3540; Eukaryota.
DR   GeneTree; ENSGT00530000063252; -.
DR   InParanoid; P14599; -.
DR   PhylomeDB; P14599; -.
DR   Reactome; R-DME-114608; Platelet degranulation.
DR   Reactome; R-DME-3000178; ECM proteoglycans.
DR   Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-DME-416476; G alpha (q) signalling events.
DR   Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-DME-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   SignaLink; P14599; -.
DR   BioGRID-ORCS; 31002; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Appl; fly.
DR   GenomeRNAi; 31002; -.
DR   PRO; PR:P14599; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0000108; Expressed in eye disc (Drosophila) and 13 other tissues.
DR   ExpressionAtlas; P14599; baseline and differential.
DR   Genevisible; P14599; DM.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0007611; P:learning or memory; IMP:FlyBase.
DR   GO; GO:0007616; P:long-term memory; IDA:FlyBase.
DR   GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR   GO; GO:1901215; P:negative regulation of neuron death; IMP:FlyBase.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR   GO; GO:0048678; P:response to axon injury; IMP:FlyBase.
DR   GO; GO:0051602; P:response to electrical stimulus; IMP:FlyBase.
DR   GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR   GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR   Gene3D; 1.20.120.770; -; 1.
DR   Gene3D; 3.30.1490.140; -; 1.
DR   Gene3D; 3.90.570.10; -; 1.
DR   InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR   InterPro; IPR008155; Amyloid_glyco.
DR   InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR   InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR   InterPro; IPR008154; Amyloid_glyco_extra.
DR   InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR   InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR   InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR   InterPro; IPR019543; APP_amyloid_C.
DR   InterPro; IPR019744; APP_CUBD_CS.
DR   InterPro; IPR036176; E2_sf.
DR   PANTHER; PTHR23103; PTHR23103; 1.
DR   Pfam; PF10515; APP_amyloid; 1.
DR   Pfam; PF12924; APP_Cu_bd; 1.
DR   Pfam; PF12925; APP_E2; 1.
DR   Pfam; PF02177; APP_N; 1.
DR   SMART; SM00006; A4_EXTRA; 1.
DR   SUPFAM; SSF109843; SSF109843; 1.
DR   SUPFAM; SSF56491; SSF56491; 1.
DR   SUPFAM; SSF89811; SSF89811; 1.
DR   PROSITE; PS00319; APP_CUBD; 1.
DR   PROSITE; PS51869; APP_E1; 1.
DR   PROSITE; PS51870; APP_E2; 1.
DR   PROSITE; PS00320; APP_INTRA; 1.
PE   1: Evidence at protein level;
KW   Amyloid; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Membrane; Neurogenesis; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..887
FT                   /note="Amyloid-beta-like protein"
FT                   /id="PRO_0000000202"
FT   TOPO_DOM        28..813
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        814..834
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        835..887
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..199
FT                   /note="E1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DOMAIN          395..597
FT                   /note="E2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
FT   REGION          30..133
FT                   /note="GFLD subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   REGION          141..199
FT                   /note="CuBD subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   REGION          225..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           875..880
FT                   /note="YENPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P05067"
FT   COMPBIAS        245..268
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..315
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        81..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        106..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        143..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        154..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        168..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   CONFLICT        177
FT                   /note="S -> T (in Ref. 1; AAA28874)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="Missing (in Ref. 1; AAA28874)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332
FT                   /note="V -> M (in Ref. 4; CAA21409/CAA18093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        743
FT                   /note="S -> T (in Ref. 1; AAA28874)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   887 AA;  98333 MW;  F0F0855AD65A5275 CRC64;
     MCAALRRNLL LRSLWVVLAI GTAQVQAASP RWEPQIAVLC EAGQIYQPQY LSEEGRWVTD
     LSKKTTGPTC LRDKMDLLDY CKKAYPNRDI TNIVESSHYQ KIGGWCRQGA LNAAKCKGSH
     RWIKPFRCLG PFQSDALLVP EGCLFDHIHN ASRCWPFVRW NQTGAAACQE RGMQMRSFAM
     LLPCGISVFS GVEFVCCPKH FKTDEIHVKK TDLPVMPAAQ INSANDELVM NDEDDSNDSN
     YSKDANEDDL DDEDDLMGDD EEDDMVADEA ATAGGSPNTG SSGDSNSGSL DDINAEYDSG
     EEGDNYEEDG AGSESEAEVE ASWDQSGGAK VVSLKSDSSS PSSAPVAPAP EKAPVKSESV
     TSTPQLSASA AAFVAANSGN SGTGAGAPPS TAQPTSDPYF THFDPHYEHQ SYKVSQKRLE
     ESHREKVTRV MKDWSDLEEK YQDMRLADPK AAQSFKQRMT ARFQTSVQAL EEEGNAEKHQ
     LAAMHQQRVL AHINQRKREA MTCYTQALTE QPPNAHHVEK CLQKLLRALH KDRAHALAHY
     RHLLNSGGPG GLEAAASERP RTLERLIDID RAVNQSMTML KRYPELSAKI AQLMNDYILA
     LRSKDDIPGS SLGMSEEAEA GILDKYRVEI ERKVAEKERL RLAEKQRKEQ RAAEREKLRE
     EKLRLEAKKV DDMLKSQVAE QQSQPTQSST QSQAQQQQQE KSLPGKELGP DAALVTAANP
     NLETTKSEKD LSDTEYGEAT VSSTKVQTVL PTVDDDAVQR AVEDVAAAVA HQEAEPQVQH
     FMTHDLGHRE SSFSLRREFA QHAHAAKEGR NVYFTLSFAG IALMAAVFVG VAVAKWRTSR
     SPHAQGFIEV DQNVTTHHPI VREEKIVPNM QINGYENPTY KYFEVKE
 
 
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