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SIF1_DROME
ID   SIF1_DROME              Reviewed;        2072 AA.
AC   P91621; Q9VRN7;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Protein still life, isoform SIF type 1;
GN   Name=sif; ORFNames=CG34418;
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Head;
RX   PubMed=8999801; DOI=10.1126/science.275.5299.543;
RA   Sone M.;
RT   "Still life, a protein in synaptic terminals of Drosophila homologous to
RT   GDP-GTP exchangers.";
RL   Science 275:543-547(1997).
RN   [2]
RP   ERRATUM OF PUBMED:8999801.
RX   PubMed=9072802;
RA   Sone M., Hoshino M., Suzuki E., Kuroda S., Kaibuchi K., Nakagoshi H.,
RA   Saigo K., Nabeshima Y., Hama C.;
RL   Science 275:1405-1405(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   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=30290152; DOI=10.1016/j.ajhg.2018.09.004;
RA   Ansar M., Chung H.L., Taylor R.L., Nazir A., Imtiaz S., Sarwar M.T.,
RA   Manousopoulou A., Makrythanasis P., Saeed S., Falconnet E., Guipponi M.,
RA   Pournaras C.J., Ansari M.A., Ranza E., Santoni F.A., Ahmed J., Shah I.,
RA   Gul K., Black G.C., Bellen H.J., Antonarakis S.E.;
RT   "Bi-allelic loss-of-function variants in DNMBP cause infantile cataracts.";
RL   Am. J. Hum. Genet. 103:568-578(2018).
CC   -!- FUNCTION: Regulates synaptic differentiation through the organization
CC       of actin cytoskeleton possibly by activating Rho-like GTPases. Is
CC       likely a factor in the cascade of Rac1 or Cdc42 in the neurons
CC       (PubMed:8999801). May play a role in maintaining proper septate
CC       junction functions. Required for eye development and most likely
CC       affects corneal lens-formation (PubMed:30290152).
CC       {ECO:0000269|PubMed:30290152, ECO:0000269|PubMed:8999801}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:8999801}.
CC       Note=Localizes to the submembranous region of synaptic terminals.
CC       {ECO:0000269|PubMed:8999801}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=SIF type 1; Synonyms=B;
CC         IsoId=P91621-1; Sequence=Displayed;
CC       Name=C;
CC         IsoId=P91620-2; Sequence=External;
CC       Name=SIF type 2; Synonyms=A;
CC         IsoId=P91620-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: In the adult eye is expressed in the two primary
CC       pigment cells in the subapical region of the eye. Also present in
CC       photoreceptors. {ECO:0000269|PubMed:30290152}.
CC   -!- DEVELOPMENTAL STAGE: At stage 14, expression occurs in each segment of
CC       the central nervous system. At stage 17, expression becomes restricted
CC       to the synaptic regions of the brain and ventral nerve cord, where
CC       synapses undergo maturation (PubMed:8999801). At 45 hours after
CC       puparium formation (apf) expression is enriched in the shaft of bristle
CC       cells in the sub-apical region. Present in all photoreceptors
CC       (PubMed:30290152). {ECO:0000269|PubMed:30290152,
CC       ECO:0000269|PubMed:8999801}.
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DR   EMBL; D86547; BAA13109.1; -; mRNA.
DR   EMBL; AE014296; AAF50755.3; -; Genomic_DNA.
DR   PIR; T13707; T13707.
DR   RefSeq; NP_001097519.2; NM_001104049.4. [P91621-1]
DR   RefSeq; NP_729084.1; NM_168126.4. [P91621-1]
DR   AlphaFoldDB; P91621; -.
DR   SMR; P91621; -.
DR   BioGRID; 68698; 6.
DR   IntAct; P91621; 3.
DR   STRING; 7227.FBpp0111624; -.
DR   PaxDb; P91621; -.
DR   DNASU; 43892; -.
DR   EnsemblMetazoa; FBtr0112708; FBpp0111620; FBgn0085447. [P91621-1]
DR   EnsemblMetazoa; FBtr0330122; FBpp0303155; FBgn0085447. [P91621-1]
DR   GeneID; 43892; -.
DR   KEGG; dme:Dmel_CG34418; -.
DR   CTD; 43892; -.
DR   FlyBase; FBgn0085447; sif.
DR   VEuPathDB; VectorBase:FBgn0085447; -.
DR   eggNOG; KOG3519; Eukaryota.
DR   GeneTree; ENSGT00940000174094; -.
DR   InParanoid; P91621; -.
DR   Reactome; R-DME-193648; NRAGE signals death through JNK.
DR   Reactome; R-DME-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-DME-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR   Reactome; R-DME-8980692; RHOA GTPase cycle.
DR   Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR   SignaLink; P91621; -.
DR   BioGRID-ORCS; 43892; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; sif; fly.
DR   GenomeRNAi; 43892; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0085447; Expressed in brain and 10 other tissues.
DR   ExpressionAtlas; P91621; baseline.
DR   Genevisible; P91621; DM.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IDA:FlyBase.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:FlyBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:FlyBase.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR   GO; GO:0050770; P:regulation of axonogenesis; IMP:FlyBase.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISS:FlyBase.
DR   GO; GO:0050803; P:regulation of synapse structure or activity; TAS:FlyBase.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 3.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR003116; RBD_dom.
DR   InterPro; IPR043537; Tiam1/Tiam2/Sif.
DR   InterPro; IPR040655; TIAM1_CC-Ex.
DR   InterPro; IPR000697; WH1/EVH1_dom.
DR   PANTHER; PTHR46001; PTHR46001; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF02196; RBD; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF18385; Tiam_CC_Ex; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00455; RBD; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00461; WH1; 1.
DR   SUPFAM; SSF48065; SSF48065; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein;
KW   Guanine-nucleotide releasing factor; Lipoprotein; Myristate;
KW   Reference proteome; Repeat; Synapse.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..2072
FT                   /note="Protein still life, isoform SIF type 1"
FT                   /id="PRO_0000080974"
FT   DOMAIN          29..147
FT                   /note="WH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT   DOMAIN          840..958
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          1121..1188
FT                   /note="RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT   DOMAIN          1204..1293
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          1436..1630
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   REGION          153..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1088..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1403..1424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1803..1832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1844..2039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2051..2072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1913..1942
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1951..1991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1992..2035
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        320
FT                   /note="D -> V (in Ref. 1; BAA13109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1374..1381
FT                   /note="Missing (in Ref. 1; BAA13109)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2072 AA;  231130 MW;  3CAFE543F72DD331 CRC64;
     MGNKLSCSCA PLMRKAYRYE DSPWQSSRRR DGHLLSSFRL WAEVFHVSAS GAGTVKWQQV
     SEDLVPVNIT CIQDSPECIF HITAYNSQVD KILDVRLVQP GTRIGQASEC FVYWKDPMTN
     DTWGLNFTSP IDAKQFRECC SPSFKFSRKA SSSYSLKLDP PGKGKVKAKR KPLSTPASPS
     RVRQEPQCTC MSAEQYARLR TDPRVRGSST LPRNVGSHRI TDVDGQQQVG SGKVVSAVSS
     TSLYDNVASG GPGTNQGADT LPRQMKGGQQ DRQDVANSGV NTNTPGVIVT GVGNVGSDMC
     GQNHVGSQVG NDDPAACQMD MDLSKSEGTQ AGGGLHQSVG TCTSSSKGTG TRNKDFGDDM
     TRDAHSHDMH QHNVINNNTR RKTKSTEDMN VDTSTLKRML KPMPSTESPV TSPEMGRRRY
     NYYNANAAQT LGHPPHMHQH GMAMGMGGGG GGGHHIMNNN TMGRASSQSS RFSGSRSSHE
     IGRGYPPRNL YLELERERSC IEGSPPSDNV MFDNQCYATT PSSSNGNSDQ DQSYGQQQSS
     GQHPQQQQGP PQRSSRHQHH HQQAPNVTPT PGSPTSRLLL EYEMHLRNTL AKGMDAESYS
     LHTFEALLSQ SMENLANAKS STLPLPPHRP LSTIRDKERD RDRDGYYSDR NELIRERERE
     RDRGYLSDHN SSFSNSRCAS CIGESARAQW FRHSDGWRSG SSTIGSGSGH GMMTQQIPGS
     GHKRSPWDSL PSLRQDSSLN DSGYKSARAD SLEQRAEFIR QDSLRSEYLS DRESRYGIVQ
     QASIESTDSR MCYLTSSEIS DDDRMSLTTA VSDEDDGESV MASPYKAKAT GTAASSFNCT
     GAVRKAGFLS VKKWLLRKKH QIELARKRGW KGYWVCLKGT TLLFYPCDSR EGRSVEAAPK
     HLIIVDGAIM QPIPEHPKRD YIFCLSTAFG DAYLFQAPCQ VELENWVNSI HSACAAAFAR
     HRGKTGTLHL LQEEIFRLEK AIESDHKLKH MAELQQSVVT DQETRHQIQT QILQWEENLE
     RLHCEQFRLR CYMASLQSGE LPNPKSLLTH VSRPTKNTLN KLGVFTVSSF HAFICARSPS
     LLNNLLAGRG ATKRRPPMLS RSNSGSSRRS MQMNSRDEPE KTFKVAMPDN AYSTVYLRDA
     MSVEEFLASA CARRNLNPME HFVRVKKRRD MEDHNYFVPH RNDLIENYLH NHEFVEVCMK
     ILYQVELQRT TLEQMWGFSV EAELIENAER QDELCCYVSR VEDKSVAMHN GIIKGDEIMV
     INGAIVSDLD MMYLESVLQE EQSLSMMMRS SRTEPPDLVG IMRVTDDMID SLVCPPPPTD
     PPVMSEEMIT GLIVPAPGWN GTSKDLYSPE AESSPATSFV DPAAMAAQLA VGGVGGVVVG
     GLGVAKPTSR TSSFEIENLL KTAEQETRKS SPTGSVTSSV STTALTPSRQ LTDAEKLRKV
     VMELVDTERT YVKHLNNLLE HYLEPMKRET FLSNAEINAL FGNIHEIVTF QRQFLQNLEE
     SLDLEPDFNK FEHCGQFRNV LFAIGSAFLY YVNHFKLYSS FCASHSKAQK VLHPNEGNHA
     LQEFLAARNP KQQHSSTLES YLIKPIQRIL KYPLLLQQMR NLTDTRADEH VHLCEALKGM
     EKVAEHINEM QRIHEEYGAI FDHLFRQHQK SCKQPIDLSP GDLLYYGGVE WLNISDFLGK
     IKKGLELHAM CFVFKSAVVF LCKERLRQKK KLMGVSSKNA TNEVEIIRYQ VLIPVTEVQV
     RASSAKDMDS HFLWELIHLR SQLQRRSEKV YVLSNSTADF RNAFLKTIRQ IIRESVRNMS
     IPMKNFGGSS GSVSGHSSQG MGSMGYPGNS QTLERPKQQI TIVHGSHTLG KPKKKSGSQR
     HSAGNIDYDN LSGSQEADDL PPSVGVVHYA SGHTHGQQMQ PAGFRGRSKT VGDVTEITCS
     SPEPHQQQQQ QQQQQQQLMQ QGHAHAHPHP HPHPREPPPP PIRQPHLHHH SSDIERIDPG
     TKSEGEEDSQ QGTIRPKATL GRTPNHLTLS TTSTLSVGST GSQARLIQSS HPPASYQPVL
     MKDLGSPVWK PRDMINLGTD PQSTTRKDDV KN
 
 
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