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NFKB1_CANLF
ID   NFKB1_CANLF             Reviewed;         972 AA.
AC   Q6F3J0; F1PM82;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Nuclear factor NF-kappa-B p105 subunit;
DE   AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1;
DE   Contains:
DE     RecName: Full=Nuclear factor NF-kappa-B p50 subunit;
GN   Name=NFKB1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Oguma K., Kano R., Hasegawa A.;
RT   "Canis familiaris nuclear factor of kappa light polypeptide gene enhancer
RT   in B-cells 1 (p105) (NFKB1), mRNA.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
CC   -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in
CC       almost all cell types and is the endpoint of a series of signal
CC       transduction events that are initiated by a vast array of stimuli
CC       related to many biological processes such as inflammation, immunity,
CC       differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B
CC       is a homo- or heterodimeric complex formed by the Rel-like domain-
CC       containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and
CC       NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most
CC       abundant one. The dimers bind at kappa-B sites in the DNA of their
CC       target genes and the individual dimers have distinct preferences for
CC       different kappa-B sites that they can bind with distinguishable
CC       affinity and specificity. Different dimer combinations act as
CC       transcriptional activators or repressors, respectively. NF-kappa-B is
CC       controlled by various mechanisms of post-translational modification and
CC       subcellular compartmentalization as well as by interactions with other
CC       cofactors or corepressors. NF-kappa-B complexes are held in the
CC       cytoplasm in an inactive state complexed with members of the NF-kappa-B
CC       inhibitor (I-kappa-B) family. In a conventional activation pathway, I-
CC       kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to
CC       different activators, subsequently degraded thus liberating the active
CC       NF-kappa-B complex which translocates to the nucleus. NF-kappa-B
CC       heterodimeric p65-p50 and RelB-p50 complexes are transcriptional
CC       activators. The NF-kappa-B p50-p50 homodimer is a transcriptional
CC       repressor, but can act as a transcriptional activator when associated
CC       with BCL3. NFKB1 appears to have dual functions such as cytoplasmic
CC       retention of attached NF-kappa-B proteins by p105 and generation of p50
CC       by a cotranslational processing. The proteasome-mediated process
CC       ensures the production of both p50 and p105 and preserves their
CC       independent function, although processing of NFKB1/p105 also appears to
CC       occur post-translationally. p50 binds to the kappa-B consensus sequence
CC       5'-GGRNNYYCC-3', located in the enhancer region of genes involved in
CC       immune response and acute phase reactions. In a complex with MAP3K8,
CC       NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is
CC       released by proteasome-dependent degradation of NFKB1/p105 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex (By similarity).
CC       Homodimer; component of the NF-kappa-B p50-p50 complex (By similarity).
CC       Component of the NF-kappa-B p105-p50 complex (By similarity). Component
CC       of the NF-kappa-B p50-c-Rel complex (By similarity). Component of a
CC       complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By
CC       similarity). Also interacts with MAP3K8 (By similarity). NF-kappa-B p50
CC       subunit interacts with NCOA3 coactivator, which may coactivate NF-
CC       kappa-B dependent expression via its histone acetyltransferase activity
CC       (By similarity). Interacts with DSIPI; this interaction prevents
CC       nuclear translocation and DNA-binding (By similarity). Interacts with
CC       SPAG9 and UNC5CL (By similarity). NFKB1/p105 interacts with CFLAR; the
CC       interaction inhibits p105 processing into p50 (By similarity).
CC       NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (By
CC       similarity). Interacts with GSK3B; the interaction prevents processing
CC       of p105 to p50 (By similarity). NFKB1/p50 interacts with NFKBIE (By
CC       similarity). NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B
CC       p50 subunit interacts with NFKBID (By similarity). Directly interacts
CC       with MEN1 (By similarity). Interacts with HIF1AN (By similarity).
CC       Interacts with FEM1A; interaction is direct (By similarity).
CC       {ECO:0000250|UniProtKB:P19838, ECO:0000250|UniProtKB:P25799}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Nuclear, but also found in the cytoplasm in an inactive form
CC       complexed to an inhibitor (I-kappa-B). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic
CC       retention, inhibition of DNA-binding by p50 homodimers, and/or
CC       transcription activation.
CC   -!- PTM: While translation occurs, the particular unfolded structure after
CC       the GRR repeat promotes the generation of p50 making it an acceptable
CC       substrate for the proteasome. This process is known as cotranslational
CC       processing. The processed form is active and the unprocessed form acts
CC       as an inhibitor (I kappa B-like), being able to form cytosolic
CC       complexes with NF-kappa B, trapping it in the cytoplasm. Complete
CC       folding of the region downstream of the GRR repeat precludes processing
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation at 'Ser-931' and 'Ser-936' are required for
CC       BTRC/BTRCP-mediated proteolysis. {ECO:0000250}.
CC   -!- PTM: S-nitrosylation of Cys-61 affects DNA binding. {ECO:0000250}.
CC   -!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
CC       prostaglandin-J2 is autocatalytic and reversible. It may occur as an
CC       alternative to other cysteine modifications, such as S-nitrosylation
CC       and S-palmitoylation (By similarity). {ECO:0000250}.
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DR   EMBL; AB183419; BAD27479.1; -; mRNA.
DR   RefSeq; NP_001003344.1; NM_001003344.1.
DR   AlphaFoldDB; Q6F3J0; -.
DR   SMR; Q6F3J0; -.
DR   STRING; 9615.ENSCAFP00000056706; -.
DR   PaxDb; Q6F3J0; -.
DR   Ensembl; ENSCAFT00000017092; ENSCAFP00000015815; ENSCAFG00000010730.
DR   Ensembl; ENSCAFT00030037443; ENSCAFP00030032664; ENSCAFG00030020386.
DR   Ensembl; ENSCAFT00040043145; ENSCAFP00040037640; ENSCAFG00040022966.
DR   Ensembl; ENSCAFT00845045189; ENSCAFP00845035432; ENSCAFG00845025570.
DR   GeneID; 442859; -.
DR   KEGG; cfa:442859; -.
DR   CTD; 4790; -.
DR   VEuPathDB; HostDB:ENSCAFG00845025570; -.
DR   VGNC; VGNC:43780; NFKB1.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000158625; -.
DR   InParanoid; Q6F3J0; -.
DR   OrthoDB; 916931at2759; -.
DR   Reactome; R-CFA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-CFA-1810476; RIP-mediated NFkB activation via ZBP1.
DR   Reactome; R-CFA-193692; Regulated proteolysis of p75NTR.
DR   Reactome; R-CFA-202424; Downstream TCR signaling.
DR   Reactome; R-CFA-209560; NF-kB is activated and signals survival.
DR   Reactome; R-CFA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-CFA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR   Reactome; R-CFA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-CFA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR   Reactome; R-CFA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-CFA-5621575; CD209 (DC-SIGN) signaling.
DR   Reactome; R-CFA-6798695; Neutrophil degranulation.
DR   Reactome; R-CFA-9020702; Interleukin-1 signaling.
DR   Reactome; R-CFA-933542; TRAF6 mediated NF-kB activation.
DR   Proteomes; UP000002254; Chromosome 32.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd01177; IPT_NFkappaB; 1.
DR   Gene3D; 1.10.533.10; -; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.340; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR033926; IPT_NFkappaB.
DR   InterPro; IPR030503; NF-kB_p105.
DR   InterPro; IPR000451; NFkB/Dor.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR030492; RHD_CS.
DR   InterPro; IPR032397; RHD_dimer.
DR   InterPro; IPR011539; RHD_DNA_bind_dom.
DR   InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR   PANTHER; PTHR24169; PTHR24169; 1.
DR   PANTHER; PTHR24169:SF9; PTHR24169:SF9; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF16179; RHD_dimer; 1.
DR   Pfam; PF00554; RHD_DNA_bind; 1.
DR   PRINTS; PR00057; NFKBTNSCPFCT.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS01204; REL_1; 1.
DR   PROSITE; PS50254; REL_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Activator; ANK repeat; Cytoplasm; DNA-binding; Hydroxylation;
KW   Isopeptide bond; Lipoprotein; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; S-nitrosylation; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..972
FT                   /note="Nuclear factor NF-kappa-B p105 subunit"
FT                   /id="PRO_0000223240"
FT   CHAIN           1..433
FT                   /note="Nuclear factor NF-kappa-B p50 subunit"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000223241"
FT   DOMAIN          39..246
FT                   /note="RHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT   REPEAT          539..568
FT                   /note="ANK 1"
FT   REPEAT          578..607
FT                   /note="ANK 2"
FT   REPEAT          611..640
FT                   /note="ANK 3"
FT   REPEAT          647..676
FT                   /note="ANK 4"
FT   REPEAT          681..711
FT                   /note="ANK 5"
FT   REPEAT          715..744
FT                   /note="ANK 6"
FT   REPEAT          768..798
FT                   /note="ANK 7"
FT   DOMAIN          814..889
FT                   /note="Death"
FT   REGION          372..394
FT                   /note="GRR"
FT                   /evidence="ECO:0000250"
FT   REGION          425..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..972
FT                   /note="Interaction with CFLAR"
FT                   /evidence="ECO:0000250"
FT   REGION          647..681
FT                   /note="Essential for interaction with HIF1AN"
FT                   /evidence="ECO:0000250"
FT   REGION          894..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           360..365
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        425..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            433..434
FT                   /note="Cleavage (when cotranslationally processed)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="S-nitrosocysteine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         337
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         431
FT                   /note="N6-acetyllysine; by EP300"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         440
FT                   /note="N6-acetyllysine; by EP300"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         675
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         756
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63369"
FT   MOD_RES         908
FT                   /note="Phosphoserine; by GSK3-beta; in vitro"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         912
FT                   /note="Phosphoserine; by GSK3-beta; in vitro"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         931
FT                   /note="Phosphoserine; by IKKB"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         936
FT                   /note="Phosphoserine; by IKKB"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         941
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   MOD_RES         947
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P25799"
FT   LIPID           61
FT                   /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9-
FT                   yl)cysteine; alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        325
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P19838"
FT   CONFLICT        289
FT                   /note="E -> G (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="E -> G (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="A -> T (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="H -> N (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="E -> G (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        822
FT                   /note="I -> T (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        838
FT                   /note="L -> Q (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        939
FT                   /note="K -> R (in Ref. 1; BAD27479)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   972 AA;  105631 MW;  189557C55699014F CRC64;
     MAEDDTYLGA HEQMFHLDPL THTIFNPELF QPEMPLPTAD GPYLQILEQP KQRGFRFRYV
     CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV TNGKNIHLHA HSLVGKHCED
     GICTVTAGPK DMVVGFANLG ILHVTKKKVF ETLEARMTEA CTKGYNPGLL VHPDLAYLQA
     EGGGDRQLTD REKEIIRQAA LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY
     DSKAPNASNL KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEEN GGIWEGFGDF
     SPTDVHRQFA IVFKTPKYKD VNITKPASVF VQLRRKSDLE TSEPKPFLYY PEIKDKEEVQ
     RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGAGST GPGYGFPHYG FPTYGGITFH
     PGTTKSNAGM KHGTIDTPSK NDSEGCGKNV DREAVNLSGK VTEPTEQDKE SSMGVDEVTL
     TYTVGIKEEN SRFQDNLFLE KAMQLAKRHA NALFDYAVTG DVKMLLAVQR HLTAVQDENG
     DSVLHLAIIH LHAQLVRDLL EVTSGLISDD IINMRNDLYQ TPLHLAVITK QEAVVDDLLR
     AGADLSLLDR LGNSVLHLAA KEGQDKILSI LLKHKKAALL MDHPNGEGLN AIHIAVMSNS
     MPCLLLLVAA GADVNAQERK SGRTALHLAV EHDNISLAGC LLLEGDAHVD STTYDGTTPL
     HIAAGRGSTR LAALLKAAGA DPLVENFEPL YDLDDSWEKD GEDEGVVPGT TPLDMATNWQ
     VFDILNGKPY EPEFTSDDLL AQGDMKQLTE DAKLQLYKLL EIPDPDKNWA TLAQKLGLGI
     LNNAFRLSPA PSKTLMDNYE VSGGTIKELV EALRQMGYTE AIEVIQAAFC APETAAPSPG
     KGAPQTLSLP LSSASTRSPV DEVRDDSICD SGVETSFRKL SFTESLTSGS SLLTLNKAPH
     EYGQEGPIEG KI
 
 
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