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DYHC2_RAT
ID   DYHC2_RAT               Reviewed;        4306 AA.
AC   Q9JJ79; P70576; Q63167;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cytoplasmic dynein 2 heavy chain 1;
DE   AltName: Full=Cytoplasmic dynein 2 heavy chain;
DE   AltName: Full=Dynein cytoplasmic heavy chain 2;
DE   AltName: Full=Dynein heavy chain isotype 1B;
DE   AltName: Full=Dynein-like protein 4;
GN   Name=Dync2h1; Synonyms=Dhc1b, Dlp4, Dnch2, Dnchc2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DYNC2LI1, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=12432068; DOI=10.1242/jcs.00168;
RA   Mikami A., Tynan S.H., Hama T., Luby-Phelps K., Saito T., Crandall J.E.,
RA   Besharse J.C., Vallee R.B.;
RT   "Molecular structure of cytoplasmic dynein 2 and its distribution in
RT   neuronal and ciliated cells.";
RL   J. Cell Sci. 115:4801-4808(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1665-1744.
RC   TISSUE=Kidney;
RX   PubMed=8812413; DOI=10.1006/geno.1996.0422;
RA   Vaughan K.T., Mikami A., Paschal B.M., Holzbaur E.L.F., Hughes S.M.,
RA   Echeverri C.J., Moore K.J., Gilbert D.J., Copeland N.G., Jenkins N.A.,
RA   Vallee R.B.;
RT   "Multiple mouse chromosomal loci for dynein-based motility.";
RL   Genomics 36:29-38(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1670-1860, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=7657712; DOI=10.1242/jcs.108.5.1883;
RA   Tanaka Y., Zhang Z., Hirokawa N.;
RT   "Identification and molecular evolution of new dynein-like protein
RT   sequences in rat brain.";
RL   J. Cell Sci. 108:1883-1893(1995).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=8832411; DOI=10.1242/jcs.109.7.1891;
RA   Criswell P.S., Ostrowski L.E., Asai D.J.;
RT   "A novel cytoplasmic dynein heavy chain: expression of DHC1b in mammalian
RT   ciliated epithelial cells.";
RL   J. Cell Sci. 109:1891-1898(1996).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=9450951; DOI=10.1091/mbc.9.2.237;
RA   Criswell P.S., Asai D.J.;
RT   "Evidence for four cytoplasmic dynein heavy chain isoforms in rat testis.";
RL   Mol. Biol. Cell 9:237-247(1998).
RN   [6]
RP   INTERACTION WITH DYNC2LI1.
RX   PubMed=11907264; DOI=10.1091/mbc.01-08-0402;
RA   Grissom P.M., Vaisberg E.A., McIntosh J.R.;
RT   "Identification of a novel light intermediate chain (D2LIC) for mammalian
RT   cytoplasmic dynein 2.";
RL   Mol. Biol. Cell 13:817-829(2002).
CC   -!- FUNCTION: May function as a motor for intraflagellar retrograde
CC       transport. Functions in cilia biogenesis. May play a role in transport
CC       between endoplasmic reticulum and Golgi or organization of the Golgi in
CC       cells (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The cytoplasmic dynein complex 2 is probably composed by a
CC       heavy chain DYNC2H1 homodimer and a number of DYNC2LI1 light
CC       intermediate chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:12432068}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q45VK7}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q45VK7}. Cytoplasm {ECO:0000269|PubMed:12432068,
CC       ECO:0000269|PubMed:8832411}. Note=Localizes to the apical cytoplasm
CC       (PubMed:8832411). May localize to Golgi apparatus, cytoplasmic vesicle
CC       and endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed both in ciliated and unciliated
CC       tissues. Detected in brain and testis (at protein level).
CC       {ECO:0000269|PubMed:7657712, ECO:0000269|PubMed:8832411,
CC       ECO:0000269|PubMed:9450951}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in adult and juvenile brain.
CC       {ECO:0000269|PubMed:7657712}.
CC   -!- INDUCTION: Up-regulated during ciliogenesis.
CC       {ECO:0000269|PubMed:8832411}.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR   EMBL; AB041881; BAA97048.1; -; mRNA.
DR   EMBL; U61748; AAC52802.1; -; mRNA.
DR   EMBL; D26495; BAA05503.1; -; mRNA.
DR   PIR; I70174; I70174.
DR   RefSeq; NP_075413.1; NM_023024.1.
DR   SMR; Q9JJ79; -.
DR   BioGRID; 249321; 1.
DR   CORUM; Q9JJ79; -.
DR   STRING; 10116.ENSRNOP00000043252; -.
DR   CarbonylDB; Q9JJ79; -.
DR   iPTMnet; Q9JJ79; -.
DR   PhosphoSitePlus; Q9JJ79; -.
DR   jPOST; Q9JJ79; -.
DR   PaxDb; Q9JJ79; -.
DR   PRIDE; Q9JJ79; -.
DR   GeneID; 65209; -.
DR   KEGG; rno:65209; -.
DR   UCSC; RGD:71042; rat.
DR   CTD; 79659; -.
DR   RGD; 71042; Dync2h1.
DR   eggNOG; KOG3595; Eukaryota.
DR   InParanoid; Q9JJ79; -.
DR   OrthoDB; 26380at2759; -.
DR   PhylomeDB; Q9JJ79; -.
DR   Reactome; R-RNO-5610787; Hedgehog 'off' state.
DR   Reactome; R-RNO-5620924; Intraflagellar transport.
DR   PRO; PR:Q9JJ79; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR   GO; GO:0005930; C:axoneme; ISO:RGD.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISO:RGD.
DR   GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0005874; C:microtubule; ISO:RGD.
DR   GO; GO:0031514; C:motile cilium; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IPI:WormBase.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR   GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR   GO; GO:0030900; P:forebrain development; ISO:RGD.
DR   GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0035721; P:intraciliary retrograde transport; ISO:RGD.
DR   GO; GO:0001822; P:kidney development; ISO:RGD.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR   GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR   GO; GO:0016485; P:protein processing; ISO:RGD.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; ISO:RGD.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.10.8.720; -; 1.
DR   Gene3D; 1.20.140.100; -; 1.
DR   Gene3D; 3.10.490.20; -; 1.
DR   Gene3D; 3.20.180.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 5.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035699; AAA_6.
DR   InterPro; IPR035706; AAA_9.
DR   InterPro; IPR041658; AAA_lid_11.
DR   InterPro; IPR042219; AAA_lid_11_sf.
DR   InterPro; IPR026983; DHC_fam.
DR   InterPro; IPR026815; DYNC2H1.
DR   InterPro; IPR042222; Dynein_2_N.
DR   InterPro; IPR043157; Dynein_AAA1S.
DR   InterPro; IPR041228; Dynein_C.
DR   InterPro; IPR043160; Dynein_C_barrel.
DR   InterPro; IPR024743; Dynein_HC_stalk.
DR   InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR   InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR   InterPro; IPR013602; Dynein_heavy_linker.
DR   InterPro; IPR013594; Dynein_heavy_tail.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10676; PTHR10676; 1.
DR   PANTHER; PTHR10676:SF352; PTHR10676:SF352; 1.
DR   Pfam; PF12774; AAA_6; 1.
DR   Pfam; PF12780; AAA_8; 1.
DR   Pfam; PF12781; AAA_9; 1.
DR   Pfam; PF18198; AAA_lid_11; 1.
DR   Pfam; PF08385; DHC_N1; 1.
DR   Pfam; PF08393; DHC_N2; 1.
DR   Pfam; PF18199; Dynein_C; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   Pfam; PF12777; MT; 1.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; SSF52540; 4.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Dynein; Membrane; Microtubule; Motor protein;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..4306
FT                   /note="Cytoplasmic dynein 2 heavy chain 1"
FT                   /id="PRO_0000318745"
FT   REGION          1..1650
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1651..1875
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          1941..2161
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2249..2505
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2617..2862
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          2880..3168
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3243..3472
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3689..3904
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          669..696
FT                   /evidence="ECO:0000255"
FT   COILED          2896..2981
FT                   /evidence="ECO:0000255"
FT   COILED          3108..3199
FT                   /evidence="ECO:0000255"
FT   COILED          3407..3441
FT                   /evidence="ECO:0000255"
FT   BINDING         145..152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1689..1696
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1979..1986
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2291..2298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2655..2662
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1670
FT                   /note="K -> R (in Ref. 2; AAC52802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1715
FT                   /note="C -> R (in Ref. 2; AAC52802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1781
FT                   /note="V -> I (in Ref. 3; BAA05503)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   4306 AA;  492218 MW;  A4AC9B7B9E7FA330 CRC64;
     MAGSLSDVRK LFLFTTTQNY FGLRPELWDQ TPLSNCPEVN NFLDDGNQML LRVQRSDAGL
     AFSNTIDFDD TKDKVLVFFK LRPEVITDGN LHTNILVSSM LESPINSLYQ AVRQVFAPML
     LKDQEWSRNF DPKLQNLLSE LEAGLGVVLR KSDTNLPKLK LKEDDTRGIL TPSDEFQFWI
     EQAHRGSKQI SKERASYFKE LFETIAREFY NLDSLSLLEV VDLVETTRDV VDDVWRQAEH
     DHYPESRMLH LLDVIGGSFG RFVQKKLGSL KLWEDPYYLV KENLKAGISI CEQWVIVCSH
     LTGQVWQRYV PHPWKSEKYF PETLDRLGKR LEEVLAIRTI HEKLLYFLPA SEERIVCLSR
     VFEPFTGVNP VQYNPYTEPL WKAAVSQYEK IIAPAEQKIA GKLKNYISEI QDSPQQLLQA
     FLKYKELVKR PTISKELMLE RETLLARLGD SAKDFRLDFE NRCRGIPGDA SGPLSGKNLS
     EVVNNIVWVR QLELKVDDTI KIAEALLSDL SGFRSFHRSA EDLLDQFKLY EQEQFDDWSR
     EVQSGLSDSR SGLCIEANSR IMELDPNDGA LKVHYSDRLV ILLREVRQLS ALGFVIPAKI
     QQVANVAQKF CKQAIILKQV AHFYNSIDQQ MIQSQRPMML QSALAFEQII KNSKAGSGGK
     SQITWDNPKE LEGYIQKLQN AAERLATENR RLRKWHITFC EKVVILMNID LLRQQQRWKD
     GLQELRTGLA SVAAQGFQPS DMRAWRQHWN HQLYKALEHQ YQMGLEALNE NLPEINVDLT
     YKQGRLQFRP PFEEIRAKYY REMKRFIGIP NQFKGVGGAG DESIFSVMID RNASGFLTIY
     SKAEDLFRRL SAVLHQHKEW VVIGQVDMEA LVEKNLSTVH DWEKNFKALK IKGKEVERLP
     SAVKVDCLNI NCSPVKTVID DLIQKLFDLL VLSLKKSIQT HIHEIDTFVT EAMKVLTVIP
     QSVEEIGDTN LQYSNLQDRR PEILPLFQEA EDKNRLLRTV AGGGVETVSN LRAKWDKFEL
     MMESHQLMIK DQIEVMKGNV KSRLQIYYQE LDKFKARWDQ LKPGDDIIET GQQNTMDQSA
     KSIKEKKIEF DDLEVIRKKL VDDCHHFGLE ESNFSLAYSI SKDIESCAQI WALYEEFQQG
     LQEMAKEDWI TYRTKIYIFE EFLINWHERL RKVEEHSVMT VKLQSEVDRY KIIIPILKYV
     RGEHLSPDHW LDLFRLLGLP RGTSLEKLLF GDLLRVADTI VEKASDLKDL NSRAQGEVTI
     REALRELDLW GVGAVFSLID YEDSQNRTIK LIKDWKDIVN QVGDNRCLLQ SLKDSPYYKG
     FEDKVSIWER KLAQLDEYLQ NLNHIQRKWV YLEPIFGRGA LPKEQTRFNK VDEDFRSIMM
     DIRKDSRVTT LTTHAGIRNT LLTILDQLQR CQKSLNEFLE EKRSAFPRFY FIGDDDLLEI
     LGQSTNPSVI QSHLKKLFAG INSVCFDEES KHITAMRSLE GEVVPFKSKV LLSNNVEAWL
     NDLALEMKQT LKQLLKECVT AGRSSQGAID PSLFPSQILC LAEQIKFTED VEDAIRDHSL
     HQIEAQLAAK LERYTSVDTS SEDPGNSESG ILELKLKTLI LDIIHNIDIV KQLNQAQVHT
     TDDWAWKKQV RFYMKSDHTC YVQMVDSELQ YTYEYQGNAP KLVYTPLTDK CYLTLTQAMK
     MGLGGNPYGP AGTGKTESVK ALGGLLGRQV LVFNCDEGID VKSMGRIFVG LVKCGAWGCF
     DEFNRLEEAV LSAVSMQIQT IQDALKNHRS VCELLGKEVE VNANSGIFIT MNPAGKGYGG
     RQKLPDNLKQ LFRPVAMSRP DNDLIAEVIL YSEGFKDAKE LGRKLVAIFN LSRELLTPQQ
     HYDWGLRALK TVLRGSGNLL RQLKKSGTKQ DVNENHIVVQ ALRLNTMSKF TFADCTRFDA
     LIKDVFPGID FKEVEYNELS SALKQVFEEA NYEVIPNQMK KALELYEQLR QRTGVVIVGP
     SGAGKSTLWR MLRAALCKIG KVVKQYTMNP KAMPRHQLLG HIDMDTREWS DGVLTNSARQ
     VVREPQDVSS WIICDGDIDP EWIESLNSVL DDNRLLTMPS GERIQFGPNV NFVFETHDLS
     CASPATISRM GMIFLSDEET DLNSLIKSWL RNQPVEYRSN LENWIGDYFS KALQWVLKQN
     DYVVETSLVG TVMNGLSHLH GCKYHDQFII NLIRGLGGNL NMKSRLEFTK EVFNWARETP
     PDSHRPMDTY FDCDRGQLAS YVLKKPESLT ADDFSSGHSL PVIQTPDMQR GLDYFKPWLS
     SETKQPFILV GPEGCGKGML LRYAFSQLRS TEIATIHCSA QTTSRHLLQK LSQTCMVIST
     NTGRVYRPKD CERLVLYLKD INLPKLDKWG TSTLVAFLQQ VLTYQGFYDE NLEWVGLENI
     QIVASMSAGG RLGRHKLTTR FTSIVRLCAV DYPEREQLQT IYGAYLEAVL HKNLKNHSIW
     GSSSKIYLLA GSMVQVYEQV RAKFTVDDYS HYFFTPCILT QWVLGLFRYD LEGGSSNHPL
     DYVLEVVAYE ARRLFRDKIV GVKELHLFDN ILTSVLQGDW GSDILDNMAD SFYVTWGAQH
     ISGAKIAPGQ PLPPHGKPLG KLSSADLKDV IKKGLIHYGR DNQNLDILLF QEVLEYMSRI
     DRVLSFPGGS LLLAGRSGVG RRTVTSLVSH MHGAVLFSPK ISRGYEPKQF RTDLKHVLHL
     AGIEAQQVVL LLEDYQFVHP TFLEMINSLL SSGEVPGLYT LEELEPLLLP LKDQASQDGF
     FGPVFNYFTY RIQQNLHIVL IMDSANLNFI INCESNPALH KKCRVLWMEG WSDSSMKKIP
     EMLFSEADIE EKYEKKRKDE KKKSSVDPDF IKSFLLIHES CKAYGATPSR YMTFLRVYSA
     ISSSKRKELL KRQSHLQAGV SKLNEAKALV DELNRKAGEQ SILLRIKQDE ADSALQEITV
     SMQDASEQKT ELERLKHRIA EEVVKIEERK SKIDDELKEV QPLVNEAKLA VGNIRPESLS
     EIRSLRMPPD VIRDILEGVL RLMGIFDTSW VSMKSFLAKR GVREDIATFD ARNIPKEIRE
     SVEELLFKNK ASFDPKNAKR ASTAAAPLAA WVKANVQYSH VLERIQPLET EQSGLELNLK
     KTEDRKRKLE DLLNSVGQKV SELKEKFQSR TSEAAKLEAE VSKAQETIKA AEVLISQLDR
     EHRRWNAQVA EIAEELATLP KRAQLAAAFI TYLSAAPEGL RKNCLEEWTK AAGLEKFDLR
     RFLCTESEQL IWKSEGLPSD DLSIENALVI LQSRVCPFLI DPSSQATEWL KTHLKDSHLE
     VINQQDSNFI TALELAVRFG KTLIIQEMDG VEPVLYPLLR RDLVAQGPRY VVQIGDKIID
     YNEDFRLFLS TRNPNPFIPP DAASIVTEVN FTTTRSGLRG QLLALTIQHE KPDLEEQKTK
     LLQQEEDKKI QLARLEESLL ETLATSQGNI LENKDLIESL NQTKASSALI QDSLKESYKL
     QISLDRERDA YLPLAESASK MYFIISDLSK INNMYRFSLA SFLRLFQRAL QNKQDSESTE
     QRIQCLVNSL KHMVYEYICR CLFKADQLMF ALHFVRGMHP EFFQENEWDT FTGVVVGDML
     RKADSQQRIR DQLPSWIDQE RSWAVATLKI SLPGLYQTLC FEDGTLWRTY YHHSMCEQEF
     PSILAKKVSL FQQVLVVQAL RPDRLQSAMA LFACKALGLK ELSPLPLNLK RLYKETLEIE
     PILIIISPGA DPSQELQELA NAERSSERYH QVAMGQGQAD LAIQMLKECA RNGDWLCLKN
     LHLVVSWLPV LEKELNTLQP KESFRLWLTA EVHPNFTPIL LQSSLKITYE SPPGLKKNLM
     RTYESWTPEQ ISKKDNIHRA HALFSLAWFH AACQERRNFI PQGWTKFYEF SLSDLRAGYH
     VIDRLFDGSK DVQWEFVHGL LENSIYGGRI DNYFDLRVLQ SYLKQFFNSS IIDVLNQRNK
     KSIFPYSISL PDSCSILDYR AVIEKLPEDD KPSFFGLPAN IARSSQRMTS SQVISQLRIL
     GRSVTAGCKF DREIWSNELS PVLNLWKKLN QNSNLIHQKV SPPNDRQGSP ILSFIILEQF
     NAIRLVQSVH QSLAALSKVI RGTTLLSSEV QKLASALLNQ KCPLTWQSKW EGPEDPLQYL
     RGLVARTLAI QNWVEKAEKQ ALLADTLDLS ELFHPDTFLN ALRQETARAT GCSVDSLKFV
     ASWKGRLQEA KLQIKISGLL LEGCSFDGSR LSENQHDSPS VSSVLPCYMG WTPQGSYGPY
     SPDECISLPV YTSAERDCVV TNIDVPCGGN QDQWIQCGAA LFLKNQ
 
 
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