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ERL2_ARATH
ID   ERL2_ARATH              Reviewed;         967 AA.
AC   Q6XAT2; Q9LYP7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=LRR receptor-like serine/threonine-protein kinase ERL2;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein ERECTA-like kinase 2;
DE   Flags: Precursor;
GN   Name=ERL2; OrderedLocusNames=At5g07180; ORFNames=T28J14.120;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=14985254; DOI=10.1242/dev.01028;
RA   Shpak E.D., Berthiaume C.T., Hill E.J., Torii K.U.;
RT   "Synergistic interaction of three ERECTA-family receptor-like kinases
RT   controls Arabidopsis organ growth and flower development by promoting cell
RT   proliferation.";
RL   Development 131:1491-1501(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA   Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT   "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT   like protein kinase genes in Arabidopsis thaliana.";
RL   BMC Genomics 11:19-19(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=16002616; DOI=10.1126/science.1109710;
RA   Shpak E.D., McAbee J.M., Pillitteri L.J., Torii K.U.;
RT   "Stomatal patterning and differentiation by synergistic interactions of
RT   receptor kinases.";
RL   Science 309:290-293(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=17652352; DOI=10.1242/dev.004788;
RA   Pillitteri L.J., Bemis S.M., Shpak E.D., Torii K.U.;
RT   "Haploinsufficiency after successive loss of signaling reveals a role for
RT   ERECTA-family genes in Arabidopsis ovule development.";
RL   Development 134:3099-3109(2007).
CC   -!- FUNCTION: Receptor kinase that regulates inflorescence architecture and
CC       organ shape as well as stomatal patterning, including density and
CC       clustering, together with ERL1 and ER. {ECO:0000269|PubMed:14985254,
CC       ECO:0000269|PubMed:16002616, ECO:0000269|PubMed:17652352}.
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   -!- 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;
CC   -!- INTERACTION:
CC       Q6XAT2; O04567: At1g27190; NbExp=2; IntAct=EBI-16895926, EBI-1238687;
CC       Q6XAT2; C0LGI5: At1g69990; NbExp=3; IntAct=EBI-16895926, EBI-20651225;
CC       Q6XAT2; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-16895926, EBI-20651957;
CC       Q6XAT2; Q8VYT3: At4g30520; NbExp=3; IntAct=EBI-16895926, EBI-16902452;
CC       Q6XAT2; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-16895926, EBI-6298290;
CC       Q6XAT2; Q94F62: BAK1; NbExp=4; IntAct=EBI-16895926, EBI-617138;
CC       Q6XAT2; O22476: BRI1; NbExp=2; IntAct=EBI-16895926, EBI-1797828;
CC       Q6XAT2; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-16895926, EBI-590903;
CC       Q6XAT2; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16895926, EBI-20651413;
CC       Q6XAT2; Q42371: ERECTA; NbExp=4; IntAct=EBI-16895926, EBI-16940407;
CC       Q6XAT2; C0LGW6: ERL1; NbExp=2; IntAct=EBI-16895926, EBI-16914248;
CC       Q6XAT2; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-16895926, EBI-16895926;
CC       Q6XAT2; Q9FL28: FLS2; NbExp=4; IntAct=EBI-16895926, EBI-1799448;
CC       Q6XAT2; Q9C8I6: IOS1; NbExp=3; IntAct=EBI-16895926, EBI-16924837;
CC       Q6XAT2; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16895926, EBI-20651739;
CC       Q6XAT2; Q9LFS4: NIK1; NbExp=4; IntAct=EBI-16895926, EBI-16146189;
CC       Q6XAT2; Q8RY65: NIK2; NbExp=4; IntAct=EBI-16895926, EBI-20664696;
CC       Q6XAT2; Q9C7S5: PSY1R; NbExp=3; IntAct=EBI-16895926, EBI-16904988;
CC       Q6XAT2; Q9ZRF9: RPK1; NbExp=3; IntAct=EBI-16895926, EBI-1238953;
CC       Q6XAT2; Q94AG2: SERK1; NbExp=4; IntAct=EBI-16895926, EBI-1555537;
CC       Q6XAT2; Q9SKG5: SERK4; NbExp=3; IntAct=EBI-16895926, EBI-6290483;
CC       Q6XAT2; Q8LPS5: SERK5; NbExp=4; IntAct=EBI-16895926, EBI-16887868;
CC       Q6XAT2; Q06BH3: SRF1; NbExp=2; IntAct=EBI-16895926, EBI-16955764;
CC       Q6XAT2; Q9FG24: SRF2; NbExp=2; IntAct=EBI-16895926, EBI-16955365;
CC       Q6XAT2; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-16895926, EBI-20651925;
CC       Q6XAT2; Q6R2K1: SRF5; NbExp=3; IntAct=EBI-16895926, EBI-20651875;
CC       Q6XAT2; Q9C8M9: SRF6; NbExp=3; IntAct=EBI-16895926, EBI-16954301;
CC       Q6XAT2; Q9LUL4: SRF7; NbExp=3; IntAct=EBI-16895926, EBI-16964596;
CC       Q6XAT2; Q8RWZ1: SUB; NbExp=4; IntAct=EBI-16895926, EBI-17072125;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in developing organs, including
CC       bud clusters, flowers, siliques and young rosettes. Also detected in
CC       mature aboveground organs, such as leaves, stems and pedicels, but
CC       barely in roots. {ECO:0000269|PubMed:14985254}.
CC   -!- DEVELOPMENTAL STAGE: At the vegetative stage, strongly expressed in the
CC       shoot meristem, leaf primordia and juvenile leaves. At the reproductive
CC       stage, localized in the young developing flowers.
CC       {ECO:0000269|PubMed:14985254}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB87274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY244746; AAP69764.1; -; mRNA.
DR   EMBL; AL163652; CAB87274.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED91118.1; -; Genomic_DNA.
DR   EMBL; FJ708772; ACN59363.1; -; mRNA.
DR   PIR; T48489; T48489.
DR   RefSeq; NP_196335.2; NM_120800.4.
DR   PDB; 5XKN; X-ray; 3.65 A; A/B=30-575.
DR   PDBsum; 5XKN; -.
DR   AlphaFoldDB; Q6XAT2; -.
DR   SMR; Q6XAT2; -.
DR   BioGRID; 15888; 28.
DR   IntAct; Q6XAT2; 56.
DR   STRING; 3702.AT5G07180.1; -.
DR   PaxDb; Q6XAT2; -.
DR   PRIDE; Q6XAT2; -.
DR   ProteomicsDB; 220694; -.
DR   EnsemblPlants; AT5G07180.1; AT5G07180.1; AT5G07180.
DR   GeneID; 830609; -.
DR   Gramene; AT5G07180.1; AT5G07180.1; AT5G07180.
DR   KEGG; ath:AT5G07180; -.
DR   Araport; AT5G07180; -.
DR   TAIR; locus:2182855; AT5G07180.
DR   eggNOG; ENOG502QTEP; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; Q6XAT2; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; Q6XAT2; -.
DR   PRO; PR:Q6XAT2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q6XAT2; baseline and differential.
DR   Genevisible; Q6XAT2; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central.
DR   GO; GO:0009553; P:embryo sac development; IGI:TAIR.
DR   GO; GO:0048481; P:plant ovule development; IGI:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0010103; P:stomatal complex morphogenesis; IGI:TAIR.
DR   Gene3D; 3.80.10.10; -; 3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 14.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Glycoprotein; Kinase; Leucine-rich repeat;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..967
FT                   /note="LRR receptor-like serine/threonine-protein kinase
FT                   ERL2"
FT                   /id="PRO_0000387510"
FT   TOPO_DOM        28..585
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        586..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        607..967
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          74..97
FT                   /note="LRR 1"
FT   REPEAT          98..120
FT                   /note="LRR 2"
FT   REPEAT          122..145
FT                   /note="LRR 3"
FT   REPEAT          146..166
FT                   /note="LRR 4"
FT   REPEAT          170..192
FT                   /note="LRR 5"
FT   REPEAT          194..216
FT                   /note="LRR 6"
FT   REPEAT          218..240
FT                   /note="LRR 7"
FT   REPEAT          242..261
FT                   /note="LRR 8"
FT   REPEAT          265..287
FT                   /note="LRR 9"
FT   REPEAT          289..311
FT                   /note="LRR 10"
FT   REPEAT          313..335
FT                   /note="LRR 11"
FT   REPEAT          337..359
FT                   /note="LRR 12"
FT   REPEAT          361..382
FT                   /note="LRR 13"
FT   REPEAT          385..406
FT                   /note="LRR 14"
FT   REPEAT          409..431
FT                   /note="LRR 15"
FT   REPEAT          433..456
FT                   /note="LRR 16"
FT   REPEAT          457..479
FT                   /note="LRR 17"
FT   REPEAT          481..503
FT                   /note="LRR 18"
FT   REPEAT          505..527
FT                   /note="LRR 19"
FT   REPEAT          529..550
FT                   /note="LRR 20"
FT   DOMAIN          651..921
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          921..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..947
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        776
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         657..665
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         679
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         640
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         648
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         724
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         763
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   MOD_RES         818
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   MOD_RES         826
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        549
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   967 AA;  106680 MW;  90096C7B67CE852C CRC64;
     MRRIETMKGL FFCLGMVVFM LLGSVSPMNN EGKALMAIKA SFSNVANMLL DWDDVHNHDF
     CSWRGVFCDN VSLNVVSLNL SNLNLGGEIS SALGDLMNLQ SIDLQGNKLG GQIPDEIGNC
     VSLAYVDFST NLLFGDIPFS ISKLKQLEFL NLKNNQLTGP IPATLTQIPN LKTLDLARNQ
     LTGEIPRLLY WNEVLQYLGL RGNMLTGTLS PDMCQLTGLW YFDVRGNNLT GTIPESIGNC
     TSFEILDVSY NQITGVIPYN IGFLQVATLS LQGNKLTGRI PEVIGLMQAL AVLDLSDNEL
     TGPIPPILGN LSFTGKLYLH GNKLTGQIPP ELGNMSRLSY LQLNDNELVG KIPPELGKLE
     QLFELNLANN NLVGLIPSNI SSCAALNQFN VHGNFLSGAV PLEFRNLGSL TYLNLSSNSF
     KGKIPAELGH IINLDTLDLS GNNFSGSIPL TLGDLEHLLI LNLSRNHLNG TLPAEFGNLR
     SIQIIDVSFN FLAGVIPTEL GQLQNINSLI LNNNKIHGKI PDQLTNCFSL ANLNISFNNL
     SGIIPPMKNF TRFSPASFFG NPFLCGNWVG SICGPSLPKS QVFTRVAVIC MVLGFITLIC
     MIFIAVYKSK QQKPVLKGSS KQPEGSTKLV ILHMDMAIHT FDDIMRVTEN LDEKYIIGYG
     ASSTVYKCTS KTSRPIAIKR IYNQYPSNFR EFETELETIG SIRHRNIVSL HGYALSPFGN
     LLFYDYMENG SLWDLLHGPG KKVKLDWETR LKIAVGAAQG LAYLHHDCTP RIIHRDIKSS
     NILLDGNFEA RLSDFGIAKS IPATKTYAST YVLGTIGYID PEYARTSRLN EKSDIYSFGI
     VLLELLTGKK AVDNEANLHQ MILSKADDNT VMEAVDAEVS VTCMDSGHIK KTFQLALLCT
     KRNPLERPTM QEVSRVLLSL VPSPPPKKLP SPAKVQEGEE RRESHSSDTT TPQWFVQFRE
     DISKSSL
 
 
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