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CFTR_TRIVU
ID   CFTR_TRIVU              Reviewed;        1478 AA.
AC   Q5D1Z7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cystic fibrosis transmembrane conductance regulator;
DE            Short=CFTR;
DE   AltName: Full=ATP-binding cassette sub-family C member 7;
DE   AltName: Full=Channel conductance-controlling ATPase;
DE            EC=5.6.1.6 {ECO:0000250|UniProtKB:P13569};
DE   AltName: Full=cAMP-dependent chloride channel;
GN   Name=CFTR; Synonyms=ABCC7;
OS   Trichosurus vulpecula (Brush-tailed possum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Phalangeridae; Trichosurus.
OX   NCBI_TaxID=9337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Demmers K.J., Juengel J.L., McLeod B.J., Butt A.G.;
RT   "Sequencing of the cystic fibrosis transmembrane conductance regulator
RT   (CFTR) in the brushtail possum (Trichosurus vulpecula).";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Epithelial ion channel that plays an important role in the
CC       regulation of epithelial ion and water transport and fluid homeostasis.
CC       Mediates the transport of chloride ions across the cell membrane (By
CC       similarity). Channel activity is coupled to ATP hydrolysis. The ion
CC       channel is also permeable to HCO(3)(-); selectivity depends on the
CC       extracellular chloride concentration. Exerts its function also by
CC       modulating the activity of other ion channels and transporters.
CC       Contributes to the regulation of the pH and the ion content of the
CC       epithelial fluid layer. Modulates the activity of the epithelial sodium
CC       channel (ENaC) complex, in part by regulating the cell surface
CC       expression of the ENaC complex. May regulate bicarbonate secretion and
CC       salvage in epithelial cells by regulating the transporter SLC4A7. Can
CC       inhibit the chloride channel activity of ANO1 (By similarity). Plays a
CC       role in the chloride and bicarbonate homeostasis during sperm
CC       epididymal maturation and capacitation (By similarity).
CC       {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + closed Cl(-) channel = ADP + phosphate + open
CC         Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000250|UniProtKB:P13569};
CC   -!- SUBUNIT: Monomer; does not require oligomerization for channel
CC       activity. May form oligomers in the membrane (By similarity). Interacts
CC       with SLC26A3, SLC26A6 and SLC9A3R1 (By similarity). Interacts with
CC       SHANK2 (By similarity). Interacts with MYO6 (By similarity). Interacts
CC       (via C-terminus) with GOPC (via PDZ domain); this promotes CFTR
CC       internalization and thereby decreases channel activity. Interacts with
CC       SLC4A7 through SLC9A3R1. Found in a complex with MYO5B and RAB11A.
CC       Interacts with ANO1. Interacts with SLC26A8 (By similarity). Interacts
CC       with AHCYL1; the interaction increases CFTR activity (By similarity).
CC       Interacts with CSE1L (By similarity). The core-glycosylated form
CC       interacts with GORASP2 (via PDZ GRASP-type 1 domain) in respone to ER
CC       stress (By similarity). Interacts with MARCHF2; the interaction leads
CC       to CFTR ubiqtuitination and degradation (By similarity).
CC       {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361,
CC       ECO:0000250|UniProtKB:P34158}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P13569}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P13569}. Cell membrane
CC       {ECO:0000250|UniProtKB:P26361}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P13569}. Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P13569}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P13569}. Nucleus {ECO:0000250|UniProtKB:P34158}.
CC       Note=The channel is internalized from the cell surface into an
CC       endosomal recycling compartment, from where it is recycled to the cell
CC       membrane. In the oviduct and bronchus, detected on the apical side of
CC       epithelial cells, but not associated with cilia. In Sertoli cells, a
CC       processed product is detected in the nucleus. ER stress induces
CC       GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of
CC       core-glycosylated CFTR to cell membrane. {ECO:0000250|UniProtKB:P13569,
CC       ECO:0000250|UniProtKB:P34158}.
CC   -!- DOMAIN: Binds and hydrolyzes ATP via the two cytoplasmic ABC
CC       transporter nucleotide-binding domains. The two ATP-binding domains
CC       interact with each other, forming a head-to-tail dimer. Normal ATPase
CC       activity requires interaction between the two domains. The first ABC
CC       transporter nucleotide-binding domain has no ATPase activity by itself.
CC       {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
CC   -!- DOMAIN: The PDZ-binding motif mediates interactions with GOPC and with
CC       the SLC4A7, SLC9A3R1/EBP50 complex. {ECO:0000250|UniProtKB:P13569}.
CC   -!- DOMAIN: The disordered R region mediates channel activation when it is
CC       phosphorylated, but not in the absence of phosphorylation.
CC       {ECO:0000250|UniProtKB:P13569}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13569}.
CC   -!- PTM: Phosphorylated; cAMP treatment promotes phosphorylation and
CC       activates the channel. Dephosphorylation decreases the ATPase activity
CC       (in vitro). Phosphorylation at PKA sites activates the channel.
CC       Phosphorylation at PKC sites enhances the response to phosphorylation
CC       by PKA. Phosphorylated by AMPK; this inhibits channel activity.
CC       {ECO:0000250|UniProtKB:P13569}.
CC   -!- PTM: Ubiquitinated, leading to its degradation in the lysosome.
CC       Deubiquitination by USP10 in early endosomes enhances its endocytic
CC       recycling to the cell membrane. Ubiquitinated by RNF185 during ER
CC       stress. Ubiquitinated by MARCHF2 (By similarity).
CC       {ECO:0000250|UniProtKB:P13569}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       CFTR transporter (TC 3.A.1.202) subfamily. {ECO:0000305}.
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DR   EMBL; AY916796; AAX13970.1; -; mRNA.
DR   AlphaFoldDB; Q5D1Z7; -.
DR   SMR; Q5D1Z7; -.
DR   BRENDA; 5.6.1.6; 6475.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR   GO; GO:0019869; F:chloride channel inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005260; F:intracellularly ATP-gated chloride channel activity; ISS:UniProtKB.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR   GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR   GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB.
DR   GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR   GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
DR   GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR009147; CFTR/ABCC7.
DR   InterPro; IPR025837; CFTR_reg_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223:SF19; PTHR24223:SF19; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF14396; CFTR_R; 1.
DR   PRINTS; PR01851; CYSFIBREGLTR.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   TIGRFAMs; TIGR01271; CFTR_protein; 1.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Chloride; Chloride channel;
KW   Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; Ion transport;
KW   Isomerase; Isopeptide bond; Lipoprotein; Membrane; Nucleotide-binding;
KW   Nucleus; Palmitate; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..1478
FT                   /note="Cystic fibrosis transmembrane conductance regulator"
FT                   /id="PRO_0000093430"
FT   TOPO_DOM        1..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        78..98
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        99..122
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        123..146
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        147..195
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        196..216
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        217..222
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        223..243
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        244..298
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        299..319
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        320..339
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        340..358
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        359..860
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        861..881
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        882..917
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        918..938
FT                   /note="Discontinuously helical; Name=8"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        939..989
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        990..1010
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        1011..1012
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        1013..1033
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        1034..1094
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        1095..1115
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        1116..1129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TRANSMEM        1130..1150
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   TOPO_DOM        1151..1478
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   DOMAIN          81..365
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          423..646
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          861..1154
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1208..1441
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          654..833
FT                   /note="Disordered R region"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   REGION          1384..1478
FT                   /note="Interaction with GORASP2"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   REGION          1446..1478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1476..1478
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   COMPBIAS        1460..1478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         401
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   BINDING         434
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   BINDING         458..465
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P26361"
FT   BINDING         1217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   BINDING         1242..1249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         660
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         670
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         686
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         700
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         712
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         737
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         769
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         797
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         815
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         1442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   MOD_RES         1454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   LIPID           524
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   LIPID           1393
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
FT   CARBOHYD        896
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        899
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        908
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        688
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P13569"
SQ   SEQUENCE   1478 AA;  168170 MW;  86DCDEF74F6F6504 CRC64;
     MQRSPLEKAN VFSKLFFSWT RPILKKGFRR RLELSDIYQI PSCNSADHLS EKLEREWDRE
     LASKKKPKLI NALRRCFFWR FVFHGIILYL GEVTKAVQPL LLGRIIASYD PDNKAERSIA
     IYLGIGLCLL FIVRTLLLHP AIFGLHHMGM QMRIALFSLI YKKTLKLSSR VLDKISTGQL
     ISLLSNNLNK FDEGLALAHF VWIAPLQVVL LMGLLWDLLQ ASAFCGLAFL VVLALFQAWL
     GQMMMKYRER RAGKINERLV ITSEMIDNIQ SVKAYCWEEA METMIENLRQ TELKLTRKTA
     YVRYFNSSAF FFSGFFVVFL AVLPYALIKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT
     WYDSLGAINK IQDFLQKEEY KTLEYNLTTT DVMMENITAF WDEGFGDLFI KVKQSNSDGK
     IPNGDHGLFF SNFSLLGTPV LKNISFKIEK GQLLAVAGST GAGKTSLLML IMGELEPSEG
     KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEEI SKFAEKDNTI
     LGEGGITLSG GQRARISLAR AIYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
     ILITSKMEHL KKADKILILH EGSCYFYGAF SELQSLRPDF SSKLMGFDSF DQFSADRRSS
     ILTETLRRFS IEGDAAVSWN EGKMQSFKQT GDFGERRKNS VLSPLNSNRK FSVVQKGQQQ
     MNGIEENDDE PLERRLSLVP DSEQGEAILP RSNMINTGPT FQGRNRRQSV LNLMTRPSVH
     QGQGMYRTGN AAVRKMSMVP QSQLSEIDIY SRRLSRDSGM DISDEINEED LKEWFFDDVE
     NIPAVTTWNT YLRYITVHKS LIFVLIWCLV IFLVEVGASL VGLWVLKETS LKDKANTTNN
     TYAVIITNTS KYYLFYIYVG VADTFFALGL LRGLPLVHTL ISVSKILHHK MLCSVLKAPM
     STFSTLKAGG ILNRFSKDIA ILDDLLPLTI FDFVQLILIV VGALIVVSVL QPYIFLATVP
     VIIAFIMLRA YFLQTSQQLK QLESEARTPI FTHLVTSLKG LWTLRAFGRQ PYFETLFHKA
     LNLHTANWFL YMSTLRWFQM RIEIIFVTFF CIVTFISILT TGDGEGRVGI LLTLAMNIMS
     TLQWAVNSSI DVDSLMRSVS RVFKFIDMPS EEPLPPKPTK SKKNQLSQVL IIENEHVKKE
     NWPSGGQMTV KDLTAKYIDG GNAVLENISF SISSGQRVGL LGRTGSGKST LLAAFLRLLN
     TQGDIQIDGV SWDSVPLQQW RKAFGVIPQK VFIFSGTFRK NLDPYGQWSD HELWKVADEV
     GLKSVIEQFP GKLDFVLVDA GCVLSHGHKQ LICLARSVLS KAKILLLDEP SAHLDPITYQ
     IIRRALKNAF ADCTVILSEH RIEAMLECQR FLVIEESKVR QYESIQKLVT EKRLYGQAIS
     HSDRMKLFPH RNSSRHKSRA KITALKEETE EEVQETRL
 
 
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