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DOCK6_MOUSE
ID   DOCK6_MOUSE             Reviewed;        2080 AA.
AC   Q8VDR9; E9QKQ0; Q3UM59; Q6PFY0; Q8BJS1; Q9D461;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Dedicator of cytokinesis protein 6;
GN   Name=Dock6; Synonyms=Kiaa1395;
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 2 AND 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1871-2080 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Mammary gland, and Testis;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-2080 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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   [4]
RP   INDUCTION.
RX   PubMed=17196961; DOI=10.1016/j.yexcr.2006.11.017;
RA   Miyamoto Y., Yamauchi J., Sanbe A., Tanoue A.;
RT   "Dock6, a Dock-C subfamily guanine nucleotide exchanger, has the dual
RT   specificity for Rac1 and Cdc42 and regulates neurite outgrowth.";
RL   Exp. Cell Res. 313:791-804(2007).
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-178; SER-870; SER-878;
RP   SER-882; THR-2064 AND SER-2065, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=21820096; DOI=10.1016/j.ajhg.2011.07.009;
RA   Shaheen R., Faqeih E., Sunker A., Morsy H., Al-Sheddi T., Shamseldin H.E.,
RA   Adly N., Hashem M., Alkuraya F.S.;
RT   "Recessive mutations in DOCK6, encoding the guanidine nucleotide exchange
RT   factor DOCK6, lead to abnormal actin cytoskeleton organization and Adams-
RT   Oliver syndrome.";
RL   Am. J. Hum. Genet. 89:328-333(2011).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-863, AND IDENTIFICATION BY MASS
RP   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).
CC   -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42
CC       and RAC1 small GTPases (By similarity). Through its activation of CDC42
CC       and RAC1, regulates neurite outgrowth in an vitro differentiation
CC       system. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC       region {ECO:0000250}. Note=Mainly located near the cell surface.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VDR9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VDR9-2; Sequence=VSP_022259, VSP_022260, VSP_022261;
CC       Name=3;
CC         IsoId=Q8VDR9-3; Sequence=VSP_022257, VSP_022258;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in lung and
CC       heart. {ECO:0000269|PubMed:21820096}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 9.5 dpc in the growing edge of the
CC       limb buds and in the developing heart. At 10.5 dpc, strongly expressed
CC       at the edge of the limb buds, while expression in the heart maintained.
CC       At 11.5 dpc, detected in the apical ectodermal ridge of all 4 limbs,
CC       with higher expression in hindlimbs than in forelimbs. By 12.5 and 13.5
CC       dpc, expression pattern more diffused in the limbs. At 13.5 dpc,
CC       clearly observed in the developing digits.
CC       {ECO:0000269|PubMed:21820096}.
CC   -!- INDUCTION: Up-regulated during differentiation of the N1E-115
CC       neuroblastoma cell line. {ECO:0000269|PubMed:17196961}.
CC   -!- DOMAIN: The DOCKER domain may mediate some GEF activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00983}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21414.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH21414.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC37843.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK016777; BAB30423.2; -; mRNA.
DR   EMBL; AK080190; BAC37843.1; ALT_FRAME; mRNA.
DR   EMBL; AK145109; BAE26239.1; -; mRNA.
DR   EMBL; AC161371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC166992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021414; AAH21414.1; ALT_INIT; mRNA.
DR   EMBL; BC043042; AAH43042.1; -; mRNA.
DR   EMBL; BC057368; AAH57368.2; -; mRNA.
DR   RefSeq; NP_796004.2; NM_177030.3.
DR   RefSeq; XP_011240856.1; XM_011242554.2. [Q8VDR9-1]
DR   AlphaFoldDB; Q8VDR9; -.
DR   SMR; Q8VDR9; -.
DR   BioGRID; 235607; 3.
DR   STRING; 10090.ENSMUSP00000034728; -.
DR   iPTMnet; Q8VDR9; -.
DR   PhosphoSitePlus; Q8VDR9; -.
DR   jPOST; Q8VDR9; -.
DR   MaxQB; Q8VDR9; -.
DR   PaxDb; Q8VDR9; -.
DR   PeptideAtlas; Q8VDR9; -.
DR   PRIDE; Q8VDR9; -.
DR   ProteomicsDB; 279755; -. [Q8VDR9-1]
DR   ProteomicsDB; 279756; -. [Q8VDR9-2]
DR   ProteomicsDB; 279757; -. [Q8VDR9-3]
DR   Antibodypedia; 69705; 43 antibodies from 13 providers.
DR   Ensembl; ENSMUST00000034728; ENSMUSP00000034728; ENSMUSG00000032198. [Q8VDR9-1]
DR   GeneID; 319899; -.
DR   KEGG; mmu:319899; -.
DR   UCSC; uc009omn.1; mouse. [Q8VDR9-1]
DR   UCSC; uc009omq.1; mouse. [Q8VDR9-2]
DR   UCSC; uc009omt.1; mouse. [Q8VDR9-3]
DR   CTD; 57572; -.
DR   MGI; MGI:1914789; Dock6.
DR   VEuPathDB; HostDB:ENSMUSG00000032198; -.
DR   eggNOG; KOG1997; Eukaryota.
DR   GeneTree; ENSGT00940000159313; -.
DR   InParanoid; Q8VDR9; -.
DR   OrthoDB; 20156at2759; -.
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 319899; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; Dock6; mouse.
DR   PRO; PR:Q8VDR9; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8VDR9; protein.
DR   Bgee; ENSMUSG00000032198; Expressed in dorsal pancreas and 205 other tissues.
DR   ExpressionAtlas; Q8VDR9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08696; C2_Dock-C; 1.
DR   Gene3D; 1.20.58.740; -; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR037808; C2_Dock-C.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR021816; DOCK_C/D_N.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR043162; DOCK_C_lobe_C.
DR   InterPro; IPR027357; DOCKER_dom.
DR   PANTHER; PTHR23317; PTHR23317; 1.
DR   Pfam; PF06920; DHR-2; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   Pfam; PF11878; DUF3398; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Guanine-nucleotide releasing factor;
KW   Methylation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..2080
FT                   /note="Dedicator of cytokinesis protein 6"
FT                   /id="PRO_0000189994"
FT   DOMAIN          546..712
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT   DOMAIN          1620..2056
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT   REGION          20..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1101..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         863
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         870
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         878
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         882
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HP0"
FT   MOD_RES         2064
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2065
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2069
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HP0"
FT   VAR_SEQ         241..244
FT                   /note="DEAV -> VGAY (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022257"
FT   VAR_SEQ         245..2080
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022258"
FT   VAR_SEQ         905..939
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022259"
FT   VAR_SEQ         1019..1062
FT                   /note="DMKLAERLNASLAFFLSDLLSIADRGYIFSLVRAHYKQVATRLQ -> VRKD
FT                   SAQGCSVVRDPVCHVGLFIHGLFLEHLWFTWPWLDVETQL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022260"
FT   VAR_SEQ         1063..2080
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022261"
FT   CONFLICT        145
FT                   /note="W -> R (in Ref. 1; BAE26239)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2080 AA;  233267 MW;  AC9541FB05DB78D0 CRC64;
     MAASERRAFA HKINRTVAAE VRKQVSRERS GSPHSSRRSS SSLGVPLTEV IEPLDFEDVL
     LSRPPEVEPG PLRDLIEFPV DDLELLKQPR ECRTTESGVP EDGQLDAQVR AAVEMYSEDW
     VIVRRRYQHL STAYSPITTE TQREWQKGLT CQVFEQDTPG DERTGPEDVD DPQHCSGSPE
     DTPRSSGASG IFSLRNLAAD SLLPTLLEQA APEDVDRRNE ALRRQHRAPT LLTLYPAPDE
     DEAVERCSRP EPPREHFGQR ILVKCLSLKF EIEIEPIFGT LALYDVREKK KISENFYFDL
     NSDSVKGLLR AHGTHPAIST LARSAIFSVT YPSPDIFLVV KLEKVLQQGD ISECCEPYMV
     MKEADTAKNK EKLEKLRLAA EQFCTRLGRY RMPFAWTAVH LANIVSRPQD RDSDSEGERR
     PTWAERRRRG PQDRGYSGDD ACSFSSFRPA TLTVTNFFKQ EAERLSDEDL FKFLADMRRP
     SSLLRRLRPV TAQLKLDISP APENLHFCLS PDLLHVKPYP DPRGRPTKEI LEFPAREVYA
     PHSCYRNLLF VYPHSLNFSS RQGSVRNLAV RIQYMAGEDQ SQALPVIFGK SSCSEFTREA
     FTPVVYHNKS PEFYEEFKLR LPACVTENHH LFFTFYHVSC QPRPGTALET PVGFTWIPLL
     QHGRLRTGPF CLPVSVDQPP PSYSVLTPDV ALPGMRWVDG HKGVFSVELT AVSSVHPQDP
     HLDKFFTLVH VLEEGIFPFR LKETVLSEGT MEQELRASLA ALRLASPEPL VAFSHLVLDK
     LVRLVVRPPI ICGQMVNLGR GAFEAMAHVA SLVHRNLEAV QDSRGHCPLL ASYVHYAFRL
     PGGDLSLPGE APPATVQAAT LARGSGRPAS LYLARSKSIS SSNPDLAVVP GSVDDEVSRI
     LASKGVDRSH SWVNSAYAPG GSKAVLRRVP PYCGADPRQL LHEELALQWV VSGSAVRELV
     LQHAWFFFQL MVKSMELHLL LGQRLDTPRK LRFPGRFLDD IAALVASVGL EVITRVHKDM
     KLAERLNASL AFFLSDLLSI ADRGYIFSLV RAHYKQVATR LQSAPNPTAL LTLRMDFTRI
     LCSHEHYVTL NLPCCPLSPP ASPSPSVSST TSQSSTFSSQ APDPKVTSMF ELSGPFRQQH
     FLSGLLLTEL ALALDPEAEG ASLLHKKAIS AVHSLLCSHD VDSRYAEATV KAKVAELYLP
     LLSLARDTLP QLHGFAEGSG QRSRLASMLD SDTEGEGDIG STINPSVAMA IAGGPLAPGS
     RTSISQGPST AARSGCPLSA ESSRTLLVCV LWVLKNAEPT LLQRWAADLA LPQLGRLLDL
     LYLCLAAFEY KGKKAFERIN SLTFKKSLDM KARLEEAILG TIGARQEMVR RSRERSPFGN
     QENVRWRKSA THWRQTSDRV DKTKDEMEHE ALVDGNLATE ASLVVLDTLE TIVQTVMLSE
     ARESILSAVL KVVLYSLGSA QSALFLQHGL ATQRALVSKF PELLFEEDTE LCADLCLRLL
     RHCGSRISTI RMHASASLYL LMRQNFEIGH NFARVKMLVT MSLSSLVGTT QNFSEEHLRK
     SLKTILTYAE EDIGLRDSTF AEQVQDLMFN LHMILTDTVK MKEHQEDPEM LMDLMYRIAR
     GYQGSPDLRL TWLQNMAGKH AELGNHAEAA QCMVHAAALV AEYLALLEDS RHLPVGCVSF
     QNVSSNVLEE SAISDDILSP DEEGFCSGKN FTELGLVGLL EQAAGYFTMG GLYEAVNEVY
     KNLIPILEAH RDYKKLAAVH GKLQEAFTKI MHQSSGWERV FGTYFRVGFY GTRFGDLDEQ
     EFVYKEPSIT KLAEISHRLE EFYTERFGDD VVEIIKDSNP VDKSKLDPQK AYIQITYVEP
     HFDTYELKDR VTYFDRNYGL RAFLFCTPFT PDGRAHGELA EQHKRKTLLS TEHAFPYIKT
     RIRVCHREET VLTPVEVAIE DMQKKTRELA FATEQDPPDA KMLQMVLQGS VGPTVNQGPL
     EVAQVFLSEI PEDPKLFRHH NKLRLCFKDF CKKCEDALRK NKALIGPDQK EYHRELERHY
     SRLREALQPL LTQRLPQLLA PSSTSLRSSM NRSSFRKADL
 
 
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