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RPGF2_CANLF
ID   RPGF2_CANLF             Reviewed;        1498 AA.
AC   F1PBJ0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Rap guanine nucleotide exchange factor 2;
DE   AltName: Full=Cyclic nucleotide ras GEF;
DE            Short=CNrasGEF;
DE   AltName: Full=Neural RAP guanine nucleotide exchange protein;
DE            Short=nRap GEP;
DE   AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 1;
DE            Short=PDZ-GEF1;
DE   AltName: Full=RA-GEF-1;
DE   AltName: Full=Ras/Rap1-associating GEF-1;
GN   Name=RAPGEF2; Synonyms=NRAPGEP, PDZGEF1;
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 [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).
RN   [2]
RP   INTERACTION WITH CDH1; CTNNB1 AND TJP1, AND SUBCELLULAR LOCATION.
RX   PubMed=10873669; DOI=10.1006/bbrc.2000.3002;
RA   Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A.,
RA   Kaibuchi K.;
RT   "Identification of a novel beta-catenin-interacting protein.";
RL   Biochem. Biophys. Res. Commun. 273:712-717(2000).
CC   -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF),
CC       which activates Rap and Ras family of small GTPases by exchanging bound
CC       GDP for free GTP in a cAMP-dependent manner. Serves as a link between
CC       cell surface receptors and Rap/Ras GTPases in intracellular signaling
CC       cascades. Acts also as an effector for Rap1 by direct association with
CC       Rap1-GTP thereby leading to the amplification of Rap1-mediated
CC       signaling. Shows weak activity on HRAS. It is controversial whether
CC       RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated
CC       beta-1 adrenergic receptor ADRB1 leads to the Ras activation through
CC       the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and
CC       Erk1/2 signaling pathway that leads to sustained inhibition of long
CC       term melanogenesis by reducing dendrite extension and melanin
CC       synthesis. Provides also inhibitory signals for cell proliferation of
CC       melanoma cells and promotes their apoptosis in a cAMP-independent
CC       nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-
CC       Raf/ERK signaling through a pathway that is independent on both PKA and
CC       RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of
CC       the major forebrain fiber connections forming the corpus callosum, the
CC       anterior commissure and the hippocampal commissure during brain
CC       development. Involved in neuronal growth factor (NGF)-induced sustained
CC       activation of Rap1 at late endosomes and in brain-derived neurotrophic
CC       factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a
CC       role in the regulation of embryonic blood vessel formation and in the
CC       establishment of basal junction integrity and endothelial barrier
CC       function. May be involved in the regulation of the vascular endothelial
CC       growth factor receptor KDR and cadherin CDH5 expression at allantois
CC       endothelial cell-cell junctions.
CC   -!- SUBUNIT: Found in a complex, at least composed of KIDINS220, MAGI2,
CC       NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a
CC       neuronal growth factor (NGF)-dependent manner. Interacts (via C-
CC       terminal domain) with NEDD4 (via WW domains); this interaction leads to
CC       ubiquitination and degradation via the proteasome pathway in a cAMP-
CC       independent manner. Interacts with MAGI1 (via PDZ domain). Interacts
CC       with ADRB1 (via C-terminal PDZ motif); the interaction is direct.
CC       Interacts (via Ras-associating domain) with RAP1A (via GTP-bound active
CC       form). Interacts weakly with HRAS (via GDP- and GTP-bound forms).
CC       Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW domains)
CC       (By similarity). Interacts with CDH1, CTNNB1 and TJP1. {ECO:0000250,
CC       ECO:0000269|PubMed:10873669}.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:10873669}.
CC       Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}.
CC       Cell membrane {ECO:0000250}. Late endosome {ECO:0000250}.
CC       Note=Associated with the synaptic plasma membrane. Localized diffusely
CC       in the cytoplasm before neuronal growth factor (NGF) stimulation.
CC       Recruited to late endosomes after NGF stimulation. Colocalized with the
CC       high affinity nerve growth factor receptor NTRK1 at late endosomes.
CC       Translocated to the perinuclear region in a RAP1A-dependent manner.
CC       Translocated to the cell membrane (By similarity). Colocalized with
CC       CTNNB1 and TJP1 at cell-cell contacts. {ECO:0000250}.
CC   -!- DOMAIN: The Ras-associating domain is necessary for the Rap guanine
CC       nucleotide exchange activity. The N-terminal regionis necessary for
CC       cAMP-binding. The PDZ domain is necessary for its targeting to the cell
CC       membrane (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RAPGEF2 family. {ECO:0000305}.
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DR   EMBL; AAEX03010088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003639545.1; XM_003639497.3.
DR   AlphaFoldDB; F1PBJ0; -.
DR   IntAct; F1PBJ0; 1.
DR   STRING; 9615.ENSCAFP00000066461; -.
DR   PaxDb; F1PBJ0; -.
DR   Ensembl; ENSCAFT00040009936; ENSCAFP00040008617; ENSCAFG00040004820.
DR   Ensembl; ENSCAFT00845010658; ENSCAFP00845008308; ENSCAFG00845005844.
DR   GeneID; 100856359; -.
DR   KEGG; cfa:100856359; -.
DR   CTD; 9693; -.
DR   VEuPathDB; HostDB:ENSCAFG00845005844; -.
DR   eggNOG; KOG3542; Eukaryota.
DR   GeneTree; ENSGT00940000156418; -.
DR   HOGENOM; CLU_002782_0_1_1; -.
DR   InParanoid; F1PBJ0; -.
DR   OMA; XLDSWSV; -.
DR   OrthoDB; 31139at2759; -.
DR   TreeFam; TF313184; -.
DR   Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
DR   Proteomes; UP000002254; Chromosome 15.
DR   Bgee; ENSCAFG00000008719; Expressed in cardiac muscle of left ventricle and 47 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
DR   GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR   GO; GO:0050699; F:WW domain binding; ISS:UniProtKB.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
DR   GO; GO:0031547; P:brain-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR   GO; GO:0071321; P:cellular response to cGMP; ISS:UniProtKB.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
DR   GO; GO:0021884; P:forebrain neuron development; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048022; P:negative regulation of melanin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR   GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
DR   GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:1901888; P:regulation of cell junction assembly; ISS:UniProtKB.
DR   GO; GO:0021591; P:ventricular system development; ISS:UniProtKB.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 1.10.840.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR030739; RapGEF2.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23113; PTHR23113; 1.
DR   PANTHER; PTHR23113:SF217; PTHR23113:SF217; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Cytoplasm; Developmental protein;
KW   Differentiation; Endosome; GTPase activation;
KW   Guanine-nucleotide releasing factor; Membrane; Neurogenesis;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..1498
FT                   /note="Rap guanine nucleotide exchange factor 2"
FT                   /id="PRO_0000423854"
FT   DOMAIN          267..380
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          385..468
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          606..692
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   DOMAIN          717..944
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1094..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1224..1257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1304..1371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1392..1498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..96
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1105..1159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1243..1257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1304..1335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1338..1352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1354..1368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         135..252
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F1M386"
FT   MOD_RES         644
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:F1M386"
FT   MOD_RES         806
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F1M386"
FT   MOD_RES         930
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F1M386"
FT   MOD_RES         933
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F1M386"
FT   MOD_RES         1022
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CHG7"
FT   MOD_RES         1079
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT   MOD_RES         1088
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT   MOD_RES         1094
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT   MOD_RES         1115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CHG7"
FT   MOD_RES         1119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CHG7"
FT   MOD_RES         1158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4G8"
FT   MOD_RES         1175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F1M386"
SQ   SEQUENCE   1498 AA;  167320 MW;  CCA24CD5403DB165 CRC64;
     MKPLAIPANH GVMGQQEKHS LPADFTKLHL TDSLHPQVTH VSSSHSGCSI TSDSGSSSLS
     DIYQATESEA GDMDLSGLPE TAVDSEDDDD EEDIERASDP LMSRDIVRDC LEKDPIDRTD
     DDIEQLLEFM HQLPAFANMT MSVRRELCAV MVFAVVERAG TIVLNDGEEL DSWSVILNGS
     VEVTYPDGKA EILCMGNSFG VSPTMDKEYM KGVMRTKVDD CQFVCIAQQD YCRILNQVEK
     NMQKVEEEGE IVMVKEHREL DRTGTRKGHI VIKGTSERLT MHLVEEHSVV DPTFIEDFLL
     TYRTFLSSPM EVGKKLLEWF NDPSLRDKVT RVVLLWVNNH FNDFEGDPAM TRFLEEFENN
     LEREKMGGHL RLLNIACAAK AKRRLMTLTK PSREAPLPFI LLGGSEKGFG IFVDSVDSGS
     KATEAGLKRG DQILEVNGQN FENIQLSKAM EILRNNTHLS ITVKTNLFVF KELLTRLSEE
     KRNGAPHLPK IGDIKKASRY SIPDLAVDVE QVIGLEKVNK KSKANTVGGR NKLKKILDKT
     RISILPQKPY NDIGIGQSQD DSIVGLRQTK HIPTALPVSG TLSSSNPDLL QSHHRILDFS
     TTPDLPDQVL RVFKADQQSR YIMISKDTTA KEVVIQAIRE FAVTATPDQY SLCEVSVTPE
     GVIKQRRLPD QLSKLADRIQ LSGRYYLKNN METETLCSDE DAQELLRESQ ISLLQLSTVE
     VATQLSMRNF ELFRNIEPTE YIDDLFKLKS KTSCANLKKF EEVINQETFW VASEILRETN
     QLKRMKIIKH FIKIALHCRE CKNFNSMFAI ISGLNLAPVA RLRTTWEKLP NKYEKLFQDL
     QDLFDPSRNM AKYRNVLNSQ NLQPPIIPLF PVIKKDLTFL HEGNDSKVDG LVNFEKLRMI
     AKEIRHVGRM ASVNMDPALM FRTRKKKWRS LGSLSQGSTN ATVLDVAQTG GHKKRVRRSS
     FLNAKKLYED AQMARKVKQY LSNLELEMDE ESLQTLSLQC EPATNTLPKN PGDKKPVKSE
     TSPVAPRAGS QQKAQAQPPP PQPQPQHKIN QGLQVPAVSL YPSRKKVPVK DLPPFGINSP
     QALKKILSLS EEGSLERHKK QAEDTISNAS SQLSSPPTSP QSSPRKGYTL APSGTVDNFS
     DSGHSEISSR SSIVSNSSFD SVPVSLHEER RQRHSVSIVE TNLGVGRMER RTMMEPDQYS
     LGSYAPMAES RGLYATATVI SSPSTEELSQ DQGDRASLDA ADSGRGSWTS CSSGSHDNIQ
     TIQHQRSWET LPFGHTHFDY SGDPAGLWAS SSHMDQIMFS DHSTKYNRQN QSRESLEQAQ
     SRASWASSTG YWGEDSEGDT GTIKRRGGKD VSIEAESSSV TSVTTEETKP VPMPAHVAVT
     SSTAKGLIVR KEGRYREPPP TPPGYIGIPI TDFPEGHSHP ARKPPDYNVA LQRSRMVARP
     TDTAAPSPIQ QPHGHPASGR PVNKPQWHKP NECDPRLAPY QSQGFSTEED EDEQVSAV
 
 
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