位置:首页 > 蛋白库 > E2AK4_RAT
E2AK4_RAT
ID   E2AK4_RAT               Reviewed;        1649 AA.
AC   D4A7V9;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=eIF-2-alpha kinase GCN2 {ECO:0000250|UniProtKB:Q9QZ05};
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9QZ05};
DE   AltName: Full=Eukaryotic translation initiation factor 2-alpha kinase 4 {ECO:0000312|RGD:1311439};
DE   AltName: Full=GCN2-like protein;
GN   Name=Eif2ak4 {ECO:0000312|RGD:1311439}; Synonyms=Gcn2;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   POSSIBLE FUNCTION.
RX   PubMed=15051816; DOI=10.1093/jn/134.4.717;
RA   Gietzen D.W., Ross C.M., Hao S., Sharp J.W.;
RT   "Phosphorylation of eIF2alpha is involved in the signaling of indispensable
RT   amino acid deficiency in the anterior piriform cortex of the brain in
RT   rats.";
RL   J. Nutr. 134:717-723(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=15774759; DOI=10.1126/science.1104882;
RA   Hao S., Sharp J.W., Ross-Inta C.M., McDaniel B.J., Anthony T.G., Wek R.C.,
RA   Cavener D.R., McGrath B.C., Rudell J.B., Koehnle T.J., Gietzen D.W.;
RT   "Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform
RT   cortex.";
RL   Science 307:1776-1778(2005).
CC   -!- FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates
CC       the alpha subunit of eukaryotic translation initiation factor 2
CC       (EIF2S1/eIF-2-alpha) in response to low amino acid availability (By
CC       similarity). Plays a role as an activator of the integrated stress
CC       response (ISR) required for adaptation to amino acid starvation (By
CC       similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress
CC       converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor,
CC       leading to a global attenuation of cap-dependent translation, and thus
CC       to a reduced overall utilization of amino acids, while concomitantly
CC       initiating the preferential translation of ISR-specific mRNAs, such as
CC       the transcriptional activator ATF4, and hence allowing ATF4-mediated
CC       reprogramming of amino acid biosynthetic gene expression to alleviate
CC       nutrient depletion (By similarity). Required for the translational
CC       induction of protein kinase PRKCH following amino acid starvation (By
CC       similarity). Binds uncharged tRNAs (By similarity). Involved in cell
CC       cycle arrest by promoting cyclin D1 mRNA translation repression after
CC       the unfolded protein response pathway (UPR) activation or cell cycle
CC       inhibitor CDKN1A/p21 mRNA translation activation in response to amino
CC       acid deprivation (By similarity). Plays a role in the consolidation of
CC       synaptic plasticity, learning as well as formation of long-term memory
CC       (By similarity). Plays a role in neurite outgrowth inhibition (By
CC       similarity). Plays a role in feeding behavior to maintain amino acid
CC       homeostasis; contributes to the innate aversion toward diets of
CC       imbalanced amino acid composition (PubMed:15051816, PubMed:15774759).
CC       Plays a proapoptotic role in response to glucose deprivation (By
CC       similarity). Promotes global cellular protein synthesis repression in
CC       response to UV irradiation independently of the stress-activated
CC       protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK
CC       signaling pathways (By similarity). Plays a role in the antiviral
CC       response against alphavirus infection; impairs early viral mRNA
CC       translation of the incoming genomic virus RNA, thus preventing
CC       alphavirus replication (By similarity). {ECO:0000250|UniProtKB:P15442,
CC       ECO:0000250|UniProtKB:Q9P2K8, ECO:0000250|UniProtKB:Q9QZ05,
CC       ECO:0000269|PubMed:15051816, ECO:0000269|PubMed:15774759}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:Q9QZ05};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9QZ05};
CC   -!- SUBUNIT: Homodimer; homodimerization is important for kinase activation
CC       by uncharged tRNAs. Interacts with GCN1; this interaction stimulates
CC       EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety
CC       of stress conditions, such as amino acid depletion, UV-C irradiation,
CC       proteasome inhibitor treatment and glucose deprivation. Interacts with
CC       DNAJC3; this interaction inhibits EIF2AK4/GCN2 kinase activity during
CC       endoplasmic reticulum (ER), hypothermic and amino acid-starving stress
CC       conditions. {ECO:0000250|UniProtKB:P15442,
CC       ECO:0000250|UniProtKB:Q9QZ05}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZ05}.
CC   -!- DOMAIN: The histidyl-tRNA synthetase-like region and protein kinase
CC       domains are necessary for eIF-2-alpha kinase activity and eIF-2-alpha-
CC       mediated translational control. The histidyl-tRNA synthetase-like
CC       domain is necessary for binding to uncharged tRNAs. Kinase domain 1 is
CC       a degenerate kinase domain. {ECO:0000250|UniProtKB:Q9QZ05}.
CC   -!- PTM: Autophosphorylated; autophosphorylation on Thr-899 is increased
CC       upon amino acid starvation and in UV irradiation cells and inhibited in
CC       presence of IMPACT. {ECO:0000250|UniProtKB:Q9QZ05}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR07053494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07053495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; D4A7V9; -.
DR   SMR; D4A7V9; -.
DR   STRING; 10116.ENSRNOP00000009222; -.
DR   jPOST; D4A7V9; -.
DR   PaxDb; D4A7V9; -.
DR   PeptideAtlas; D4A7V9; -.
DR   PRIDE; D4A7V9; -.
DR   RGD; 1311439; Eif2ak4.
DR   VEuPathDB; HostDB:ENSRNOG00000006027; -.
DR   eggNOG; KOG1035; Eukaryota.
DR   HOGENOM; CLU_001222_1_0_1; -.
DR   InParanoid; D4A7V9; -.
DR   OMA; GSEMIYE; -.
DR   TreeFam; TF101512; -.
DR   PRO; PR:D4A7V9; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000006027; Expressed in stomach and 20 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005844; C:polysome; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; ISS:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR   GO; GO:0070417; P:cellular response to cold; ISO:RGD.
DR   GO; GO:1990253; P:cellular response to leucine starvation; ISO:RGD.
DR   GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR   GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR   GO; GO:0036492; P:eiF2alpha phosphorylation in response to endoplasmic reticulum stress; ISO:RGD.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR   GO; GO:0140469; P:GCN2-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0007612; P:learning; ISS:UniProtKB.
DR   GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR   GO; GO:0044828; P:negative regulation by host of viral genome replication; ISS:UniProtKB.
DR   GO; GO:0032792; P:negative regulation of CREB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR   GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR   GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR   GO; GO:0032057; P:negative regulation of translational initiation in response to stress; ISO:RGD.
DR   GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR   GO; GO:0002821; P:positive regulation of adaptive immune response; ISO:RGD.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR   GO; GO:0071264; P:positive regulation of translational initiation in response to starvation; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR   GO; GO:0060259; P:regulation of feeding behavior; ISO:RGD.
DR   GO; GO:0010998; P:regulation of translational initiation by eIF2 alpha phosphorylation; ISS:UniProtKB.
DR   GO; GO:0043558; P:regulation of translational initiation in response to stress; ISO:RGD.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR   GO; GO:0002286; P:T cell activation involved in immune response; ISO:RGD.
DR   GO; GO:0019081; P:viral translation; ISS:UniProtKB.
DR   Gene3D; 3.10.110.10; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR016255; Gcn2.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR024435; HisRS-related_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF12745; HGTP_anticodon2; 1.
DR   Pfam; PF00069; Pkinase; 3.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR   SMART; SM00591; RWD; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50908; RWD; 1.
PE   3: Inferred from homology;
KW   Acetylation; Activator; ATP-binding; Cell cycle; Coiled coil; Cytoplasm;
KW   Differentiation; Growth arrest; Kinase; Neurogenesis; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; RNA-binding;
KW   Serine/threonine-protein kinase; Stress response; Transferase;
KW   Translation regulation; tRNA-binding.
FT   CHAIN           1..1649
FT                   /note="eIF-2-alpha kinase GCN2"
FT                   /id="PRO_0000435425"
FT   DOMAIN          25..137
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   DOMAIN          296..539
FT                   /note="Protein kinase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          590..1001
FT                   /note="Protein kinase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1493
FT                   /note="Histidyl-tRNA synthetase-like"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZ05"
FT   COILED          146..205
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        706..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        847
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         596..604
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         619
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K8"
FT   MOD_RES         667
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K8"
FT   MOD_RES         870
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K8"
FT   MOD_RES         899
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZ05"
FT   MOD_RES         904
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1259
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K8"
SQ   SEQUENCE   1649 AA;  186724 MW;  75D093684454115F CRC64;
     MAGGRGAAGR GPAEPQESYS QRQDHELQAL EAIYGSDFQD LRPDARGRVR EPPEINLVLY
     PQGLAGEEVY VQVELRVKCP PTYPDVVPEI ELKNTKGLSN ESVNLLKSHL EELAKKQCGE
     VMIFELAHHV QSFLSEHNKP PPKSFHEEML ERQAQEKQQR LLEARQKEEQ EQREILHEIQ
     KRKEEIKEEK KRKEMAKQER LEITSLTNQD HASKRDPAGH RAAAFLHGGS PDFVGNGKAR
     AHSSGRSRRE RQYSVCSGEA SPGSCDILYF CVGSADQLMV HKGKCVGSDE QLGKVVYNAL
     ETATGSFVLL YEWVLQWQKK MGPCLTSQEK EKIDKCKKQI QGAETEFSSL VKLSHPNIVR
     YFAMNSREEK DSIVVDILAE HISGISLAAH LSHSGPVPMH QLRKYTAQLL AGLDYLHRNS
     VVHKVLSTAS VLVDAEGTVK ITDYSISKRL ADICKEDVFE QTRVRFSDSA LPYKTGKKGD
     VWRLGLLLLS LSQGQECEEY PVTIPSDLPA DFQDFLKKCV CLDDKERWSP QQLLKHSFIN
     PQPKMPLVEQ SPEDSGGQDY IETIIPSNQL PSAAFFTETQ RQFSRYFIEF EELQLLGKGA
     FGAVIKVQNK LDGCCYAVKR IPINPASRQF RRIKGEVTLL SRLHHENIVR YYNAWIERHE
     RPAVPGTPPP DYIPQAQNSS ATGGKASGDT EELGSVEAAA PPPILSSSVE WSTSAERSNS
     ARFPVTGQDS SSDEEDEDER DGVFSQSFLP ASDSDSDIIF DNEDENSKSQ NQDEDCNEKD
     SRHEIEPSVT TEAVHYLYIQ MEYCEKSTLR DTIDQGLFRD TSRLWRLFRE ILDGLAYIHE
     KGMIHRDLKP VNIFLDSDDH VKIGDFGLAT DHLAFNAEGK QDDQAGDHVI KSDPSGHLTG
     MVGTALYVSP EVQGSTKSAY NQKVDLFSLG IILFEMSYHP MVTASERIFV LNQLRDPTSP
     KFPDDFEDGE HTKQKSVISW LLNHDPAKRP TAMELLKSEL LPPPQMEESE LHEVLHHTLA
     NTDGKAYRTM MSQLFCQHSS PAIDYTYDSD ILKGNFLIRT AKIQQLVCET IVRVFKRHGA
     VQLCTPLLLP RNRQIYEHNE AALFMDHSGM LVMLPFDLRV PFARYVARNN ILNLKRYCIE
     RVFRPRKLDR FHPKELLECA FDIVTSTANS SLPTAETIYT IYEVIQEFPA LQERNYSIYL
     NHTMLLKAIL LHCGIPEDKL SQVYVILYDA VTEKLTRREV EAKFCNLSLS SNSLCRLYKF
     IEQKGDLQDL TPTINSLIKQ KTGIAQLVKY SLKDLEEVVG LLKKLGVKLQ VSINLGLVYK
     VQQHNGIIFQ FLAFSKRRQR VVPEILAAGG RYDLLIPKFR GPQALGPVPT AVGVSIAIDK
     IFAAVLNMGE PVTVSSCDLL VVSAGQMSMS RAINLTQKLW TAGITAEIMY DWSQSQEELQ
     EYCRHHEITY VALVSDKEGS HVKVKSFEKE RQTEKRVLES DLVDHVMQKL RTKVGDERNF
     RDASDNLAVQ TLKGSFSNAS GLFEIHGTTV VPTVSVISPE KLSASTRRRH EIQVQTRLQT
     TLANLHQKSS EIEILAVDLP KETILQFLSL EWDADEQAFN TTVKQLLSRL PKQRYLKLVC
     DEIYNIKVEK KVSVLFLYSY RDDYYRILF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024