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ZSWM8_MOUSE
ID   ZSWM8_MOUSE             Reviewed;        1832 AA.
AC   Q3UHH1; B2RX90; Q5U4B9; Q6PCY6; Q80Y41; Q8CE12; Q8CHC3; Q9D789;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Zinc finger SWIM domain-containing protein 8 {ECO:0000305};
GN   Name=Zswim8 {ECO:0000303|PubMed:24012004};
GN   Synonyms=Kiaa0913 {ECO:0000303|PubMed:12465718};
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] (ISOFORMS 1 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 64-1832 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 622-1832 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 769-1559 (ISOFORMS 1/2).
RC   TISSUE=Brain;
RX   PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT   The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-53; SER-1155 AND
RP   SER-1158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, 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   [7]
RP   IDENTIFICATION IN A SCF-LIKE E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=24012004; DOI=10.1016/j.neuron.2013.06.035;
RA   Wang Z., Hou Y., Guo X., van der Voet M., Boxem M., Dixon J.E.,
RA   Chisholm A.D., Jin Y.;
RT   "The EBAX-type Cullin-RING E3 ligase and Hsp90 guard the protein quality of
RT   the SAX-3/Robo receptor in developing neurons.";
RL   Neuron 79:903-916(2013).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [9]
RP   FUNCTION.
RX   PubMed=33184237; DOI=10.1126/science.abc9359;
RA   Shi C.Y., Kingston E.R., Kleaveland B., Lin D.H., Stubna M.W., Bartel D.P.;
RT   "The ZSWIM8 ubiquitin ligase mediates target-directed microRNA
RT   degradation.";
RL   Science 0:0-0(2020).
CC   -!- FUNCTION: Substrate recognition component of a SCF-like E3 ubiquitin-
CC       protein ligase complex that promotes target-directed microRNA
CC       degradation (TDMD), a process that mediates degradation of microRNAs
CC       (miRNAs) (PubMed:33184237). The SCF-like E3 ubiquitin-protein ligase
CC       complex acts by catalyzing ubiquitination and subsequent degradation of
CC       AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs
CC       for degradation (By similarity). Specifically recognizes and binds AGO
CC       proteins when they are engaged with a TDMD target (By similarity). May
CC       also acts as a regulator of axon guidance: specifically recognizes
CC       misfolded ROBO3 and promotes its ubiquitination and subsequent
CC       degradation (By similarity). {ECO:0000250|UniProtKB:A7E2V4,
CC       ECO:0000269|PubMed:33184237}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:A7E2V4}.
CC   -!- SUBUNIT: Component of the SCF-like E3 ubiquitin-protein ligase complex
CC       which contains CUL3, RBX1, ELOB, ELOC and ZSWIM8.
CC       {ECO:0000305|PubMed:24012004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24012004}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q3UHH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHH1-2; Sequence=VSP_029595;
CC       Name=3;
CC         IsoId=Q3UHH1-3; Sequence=VSP_029598;
CC       Name=4;
CC         IsoId=Q3UHH1-4; Sequence=VSP_029592, VSP_029599, VSP_029600;
CC       Name=5;
CC         IsoId=Q3UHH1-5; Sequence=VSP_029593, VSP_029594, VSP_029596,
CC                                  VSP_029597;
CC   -!- SIMILARITY: Belongs to the ZSWIM8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26298.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK009454; BAB26298.1; ALT_INIT; mRNA.
DR   EMBL; AK029263; BAC26361.1; -; mRNA.
DR   EMBL; AK147398; BAE27886.1; -; mRNA.
DR   EMBL; BC059058; AAH59058.1; -; mRNA.
DR   EMBL; BC085161; AAH85161.1; -; mRNA.
DR   EMBL; BC049362; AAH49362.1; -; mRNA.
DR   EMBL; BC151046; AAI51047.1; -; mRNA.
DR   EMBL; BC151056; AAI51057.1; -; mRNA.
DR   EMBL; BC151173; AAI51174.1; -; mRNA.
DR   EMBL; AB093273; BAC41457.3; -; mRNA.
DR   CCDS; CCDS36820.1; -. [Q3UHH1-1]
DR   CCDS; CCDS88587.1; -. [Q3UHH1-2]
DR   CCDS; CCDS88588.1; -. [Q3UHH1-3]
DR   RefSeq; NP_001239010.1; NM_001252081.1. [Q3UHH1-3]
DR   RefSeq; NP_001239011.1; NM_001252082.1. [Q3UHH1-2]
DR   RefSeq; NP_082272.1; NM_027996.3. [Q3UHH1-1]
DR   AlphaFoldDB; Q3UHH1; -.
DR   SMR; Q3UHH1; -.
DR   BioGRID; 234542; 9.
DR   IntAct; Q3UHH1; 5.
DR   MINT; Q3UHH1; -.
DR   STRING; 10090.ENSMUSP00000022358; -.
DR   iPTMnet; Q3UHH1; -.
DR   PhosphoSitePlus; Q3UHH1; -.
DR   EPD; Q3UHH1; -.
DR   jPOST; Q3UHH1; -.
DR   MaxQB; Q3UHH1; -.
DR   PaxDb; Q3UHH1; -.
DR   PeptideAtlas; Q3UHH1; -.
DR   PRIDE; Q3UHH1; -.
DR   ProteomicsDB; 275111; -. [Q3UHH1-1]
DR   ProteomicsDB; 275112; -. [Q3UHH1-2]
DR   ProteomicsDB; 275113; -. [Q3UHH1-3]
DR   ProteomicsDB; 275114; -. [Q3UHH1-4]
DR   ProteomicsDB; 275115; -. [Q3UHH1-5]
DR   Antibodypedia; 48437; 5 antibodies from 5 providers.
DR   Ensembl; ENSMUST00000022358; ENSMUSP00000022358; ENSMUSG00000021819. [Q3UHH1-1]
DR   Ensembl; ENSMUST00000223840; ENSMUSP00000153027; ENSMUSG00000021819. [Q3UHH1-2]
DR   Ensembl; ENSMUST00000224751; ENSMUSP00000153285; ENSMUSG00000021819. [Q3UHH1-3]
DR   GeneID; 268721; -.
DR   KEGG; mmu:268721; -.
DR   UCSC; uc007sko.2; mouse. [Q3UHH1-1]
DR   UCSC; uc007skp.2; mouse. [Q3UHH1-2]
DR   UCSC; uc007skq.1; mouse. [Q3UHH1-5]
DR   UCSC; uc007skr.3; mouse. [Q3UHH1-3]
DR   CTD; 23053; -.
DR   MGI; MGI:1919156; Zswim8.
DR   VEuPathDB; HostDB:ENSMUSG00000021819; -.
DR   eggNOG; KOG3615; Eukaryota.
DR   GeneTree; ENSGT00940000156999; -.
DR   HOGENOM; CLU_001052_0_0_1; -.
DR   InParanoid; Q3UHH1; -.
DR   OMA; QMQMYIS; -.
DR   OrthoDB; 88229at2759; -.
DR   PhylomeDB; Q3UHH1; -.
DR   TreeFam; TF324881; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 268721; 7 hits in 71 CRISPR screens.
DR   ChiTaRS; Zswim8; mouse.
DR   PRO; PR:Q3UHH1; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q3UHH1; protein.
DR   Bgee; ENSMUSG00000021819; Expressed in undifferentiated genital tubercle and 221 other tissues.
DR   ExpressionAtlas; Q3UHH1; baseline and differential.
DR   Genevisible; Q3UHH1; MM.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:2000627; P:positive regulation of miRNA catabolic process; IDA:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Metal-binding; Phosphoprotein;
KW   Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..1832
FT                   /note="Zinc finger SWIM domain-containing protein 8"
FT                   /id="PRO_0000311803"
FT   ZN_FING         172..208
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT   REGION          45..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..720
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1046
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1146..1162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         564
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         1141
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         1155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         1270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         1831
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   VAR_SEQ         1..895
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029592"
FT   VAR_SEQ         1..121
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029593"
FT   VAR_SEQ         122..126
FT                   /note="LYSCL -> MKRTF (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029594"
FT   VAR_SEQ         669..702
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029595"
FT   VAR_SEQ         770..771
FT                   /note="LF -> RG (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029596"
FT   VAR_SEQ         772..1832
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029597"
FT   VAR_SEQ         806..812
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029598"
FT   VAR_SEQ         1707..1734
FT                   /note="VNYVHQFCVGAAKGVLSPFVLQEIVMET -> NTSPPQDHCPPVSLPFLSQT
FT                   SFLALTQS (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029599"
FT   VAR_SEQ         1735..1832
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029600"
FT   CONFLICT        599
FT                   /note="G -> E (in Ref. 1; BAC26361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1317..1318
FT                   /note="QA -> KS (in Ref. 3; BAC41457)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1664
FT                   /note="R -> L (in Ref. 2; AAH59058)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1832 AA;  197061 MW;  30BD7C1D3157F93B CRC64;
     MELMFAEWED GERFSFEDSD RFEEDSLCSF ISEAESLCQN WRGWRKQSAG PNSPTGGGGG
     GGSGGTRTRD GLVIPLVELS AKQVAFHIPF EVVEKVYPPV PEQLQLRIAF WSFPENEEDI
     RLYSCLANGS ADEFQRGDQL FRMRAVKDPL QIGFHLSATV VPPQMVPPKG AYNVAVMFDR
     CRVTSCSCTC GAGAKWCTHV VALCLFRIHN ASAVCLRAPV SESLSRLQRD QLQKFAQYLI
     SELPQQILPT AQRLLDELLS SQSTAINTVC GAPDPTAGPS ASDQSTWYLD ESTLTDNIKK
     TLHKFCGPSP VVFSDVNSMY LSSTEPPAAA EWACLLRPLR GREPEGVWNL LSIVREMFKR
     RDSNAAPLLE ILTDQCLTYE QITGWWYSVR TSASHSSASG HTGRSNGQSE VAAHACASMC
     DEMVTLWRLA VLDPALSPQR RRELCAQLRQ WQLKVIENVK RGQHKKTLER LFPGFRPAVE
     ACYFNWEEAY PLPGVTYSGT DRKLALCWAR ALPARPGASR SGGLEESRPR PLPTEPAVRP
     KEPGAKRKGL GEGISSQRGP RRLSAEGGDK ALHKMGPSGG KAKVLGGTGS GGKSSAGSGS
     KRRLSSEDSS LEPDLAEMSL DDSSLALGAE ASTFGGFPES PPPCPSSVGS RGPSTFLPEP
     PDTYEEDAGV YFSEGPEPPT ASADHPGLLP GEVCTRDDLP STDDSGSGLH KTKEAAPAVG
     EEDDDYQAYY LNAQDGAGGE EEKAEGGTGE EHDLFAGLKP LEQESRMEVL FACAEALHAH
     GYSNEASRLT VELAQDLLAN PPDLKVEPPP AKGKKNKVST SRQTWVATNT LTKAAFLLTV
     LSERPEHHSL AFRVGMFALE LQRPPASTKA LEVKLAYQES EVAALLKKIP RGPSEMSTIR
     CRAEELREGT LCDYRPVLPL MLASFIFDVL CAPVVSLTGS RPPSRNWTNE MPGDEELGFE
     AAVAALGMKT TVSEAEHPLL CEGTRREKGD LALALMITYK DDQAKLKKIL DKLLDRESQT
     HKPQTLSSFY SSSRPATANQ RSPSKHGAPS APGALQPLTS SSAGPAQPGN VAGAGPGPTE
     GFTEKNVPES SPHSPCEGLP PEAALTPRPE GKVPSRLALG SRGGYNGRGW GSPGRPKKKH
     TGMASIDSSA PETTSDSSPT LSRRPLRGGW APTSWGRGQD SDSISSSSSD SLGSSSSSGS
     RRASASGGAR AKTVDVGRCY KGRRPESHAP HVPNQPSEAA AHFYFELAKT VLIKAGGNSS
     TSIFTHPSSS GGHQGPHRNL HLCAFEIGLY ALGLHNFVSP NWLSRTYSSH VSWITGQAME
     IGSAALTILV ECWDGHLTPP EVASLADRAS RARDSNMVRA AAELALSCLP HAHALNPNEI
     QRALVQCKEQ DNLMLEKACM AVEEAAKGGG VYPEVLFEVA HQWFWLYEET AGGSSTAREG
     ATSCSGSGMR AAGEAGRGLP EGRGAPGTEP VTVAAAAVTA AATVVPVISV GSSLYPGPGL
     GHGHSPGLHP YTALQPHLPC SPQYLTHPAH PAHPMPHMPR PAVFPVPSSA YPQGVHPAFL
     GAQYPYSVTP PSLAATAVSF PVPSMAPITV HPYHTEPGLP LPTSVALSSV HPASTFPAIQ
     GASLPALTTQ PSPLVSGGFP PPEEETHSQP VNPHSLHHLH AAYRVGMLAL EMLGRRAHND
     HPNNFSRSPP YTDDVKWLLG LAAKLGVNYV HQFCVGAAKG VLSPFVLQEI VMETLQRLNP
     IHAHNHLRAP AFHQLVQRCQ QAYMQYIHHR LIHLTPADYD DFVNAIRSAR SAFCLTPMGM
     MQFNDILQNL KRSKQTKELW QRVSLEITTF SP
 
 
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