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MYB88_ARATH
ID   MYB88_ARATH             Reviewed;         484 AA.
AC   F4IRB4; F4IRB5; O64502; Q94GA5;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Transcription factor MYB88 {ECO:0000303|PubMed:9839469};
DE   AltName: Full=Myb-related protein 88 {ECO:0000303|PubMed:9839469};
DE            Short=AtMYB88 {ECO:0000303|PubMed:9839469};
GN   Name=MYB88 {ECO:0000303|PubMed:9839469};
GN   OrderedLocusNames=At2g02820 {ECO:0000312|Araport:AT2G02820};
GN   ORFNames=T20F6.4 {ECO:0000312|EMBL:AAC05340.2};
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] (ISOFORM 3), GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=9839469; DOI=10.1046/j.1365-313x.1998.00278.x;
RA   Kranz H.D., Denekamp M., Greco R., Jin H.-L., Leyva A., Meissner R.C.,
RA   Petroni K., Urzainqui A., Bevan M., Martin C., Smeekens S., Tonelli C.,
RA   Paz-Ares J., Weisshaar B.;
RT   "Towards functional characterisation of the members of the R2R3-MYB gene
RT   family from Arabidopsis thaliana.";
RL   Plant J. 16:263-276(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Qu L.-J., Gu H.;
RT   "The MYB transcription factor family in Arabidopsis: A genome-wide cloning
RT   and expression pattern analysis.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=11597504; DOI=10.1016/s1369-5266(00)00199-0;
RA   Stracke R., Werber M., Weisshaar B.;
RT   "The R2R3-MYB gene family in Arabidopsis thaliana.";
RL   Curr. Opin. Plant Biol. 4:447-456(2001).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=16155180; DOI=10.1105/tpc.105.034116;
RA   Lai L.B., Nadeau J.A., Lucas J., Lee E.-K., Nakagawa T., Zhao L.,
RA   Geisler M., Sack F.D.;
RT   "The Arabidopsis R2R3 MYB proteins FOUR LIPS and MYB88 restrict divisions
RT   late in the stomatal cell lineage.";
RL   Plant Cell 17:2754-2767(2005).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=20675570; DOI=10.1105/tpc.110.074609;
RA   Xie Z., Lee E., Lucas J.R., Morohashi K., Li D., Murray J.A., Sack F.D.,
RA   Grotewold E.;
RT   "Regulation of cell proliferation in the stomatal lineage by the
RT   Arabidopsis MYB FOUR LIPS via direct targeting of core cell cycle genes.";
RL   Plant Cell 22:2306-2321(2010).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21105921; DOI=10.1111/j.1365-313x.2010.04364.x;
RA   Xie Z., Li D., Wang L., Sack F.D., Grotewold E.;
RT   "Role of the stomatal development regulators FLP/MYB88 in abiotic stress
RT   responses.";
RL   Plant J. 64:731-739(2010).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21772250; DOI=10.1038/emboj.2011.240;
RA   Vanneste S., Coppens F., Lee E., Donner T.J., Xie Z., Van Isterdael G.,
RA   Dhondt S., De Winter F., De Rybel B., Vuylsteke M., De Veylder L.,
RA   Friml J., Inze D., Grotewold E., Scarpella E., Sack F., Beemster G.T.,
RA   Beeckman T.;
RT   "Developmental regulation of CYCA2s contributes to tissue-specific
RT   proliferation in Arabidopsis.";
RL   EMBO J. 30:3430-3441(2011).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=22915737; DOI=10.1093/jxb/ers209;
RA   Makkena S., Lee E., Sack F.D., Lamb R.S.;
RT   "The R2R3 MYB transcription factors FOUR LIPS and MYB88 regulate female
RT   reproductive development.";
RL   J. Exp. Bot. 63:5545-5558(2012).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=24123248; DOI=10.1093/jxb/ert313;
RA   Lee E., Liu X., Eglit Y., Sack F.;
RT   "FOUR LIPS and MYB88 conditionally restrict the G1/S transition during
RT   stomatal formation.";
RL   J. Exp. Bot. 64:5207-5219(2013).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=24687979; DOI=10.1093/jxb/eru139;
RA   Yang K., Wang H., Xue S., Qu X., Zou J., Le J.;
RT   "Requirement for A-type cyclin-dependent kinase and cyclins for the
RT   terminal division in the stomatal lineage of Arabidopsis.";
RL   J. Exp. Bot. 65:2449-2461(2014).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH RBR1.
RC   STRAIN=cv. Columbia;
RX   PubMed=24571519; DOI=10.1111/tpj.12489;
RA   Lee E., Lucas J.R., Sack F.D.;
RT   "Deep functional redundancy between FAMA and FOUR LIPS in stomatal
RT   development.";
RL   Plant J. 78:555-565(2014).
RN   [15]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia GL1;
RX   PubMed=26391711; DOI=10.3732/ajb.1500056;
RA   Lei Q., Lee E., Keerthisinghe S., Lai L., Li M., Lucas J.R., Wen X.,
RA   Ren X., Sack F.D.;
RT   "The FOUR LIPS and MYB88 transcription factor genes are widely expressed in
RT   Arabidopsis thaliana during development.";
RL   Am. J. Bot. 102:1521-1528(2015).
RN   [16]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26578065; DOI=10.1038/ncomms9821;
RA   Chen Q., Liu Y., Maere S., Lee E., Van Isterdael G., Xie Z., Xuan W.,
RA   Lucas J., Vassileva V., Kitakura S., Marhavy P., Wabnik K., Geldner N.,
RA   Benkova E., Le J., Fukaki H., Grotewold E., Li C., Friml J., Sack F.,
RA   Beeckman T., Vanneste S.;
RT   "A coherent transcriptional feed-forward motif model for mediating auxin-
RT   sensitive PIN3 expression during lateral root development.";
RL   Nat. Commun. 6:8821-8821(2015).
RN   [17]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=26578169; DOI=10.1038/ncomms9822;
RA   Wang H.-Z., Yang K.-Z., Zou J.-J., Zhu L.-L., Xie Z.D., Morita M.T.,
RA   Tasaka M., Friml J., Grotewold E., Beeckman T., Vanneste S., Sack F.,
RA   Le J.;
RT   "Transcriptional regulation of PIN genes by FOUR LIPS and MYB88 during
RT   Arabidopsis root gravitropism.";
RL   Nat. Commun. 6:8822-8822(2015).
CC   -!- FUNCTION: Transcription factor that binds to DNA in promoters cis-
CC       regulatory element 5'-GGCGCGC-3' of cell cycle genes, including
CC       cyclins, cyclin-dependent kinases (CDKs), and components of the pre-
CC       replication complex (PubMed:20675570, PubMed:24687979). Binds to DNA in
CC       promoters cis-regulatory element 5'-AGCCG-3' of auxin regulated genes
CC       (e.g. PIN3 and PIN7) (PubMed:26578169). Together with FAMA and MYB124,
CC       ensures that stomata contain just two guard cells (GCs) by enforcing a
CC       single symmetric precursor cell division before stomatal maturity
CC       (PubMed:24571519). Represses the expression of the mitosis-inducing
CC       factors CDKB1-1 and CDKA-1, specifically required for the last guard
CC       mother cells (GMC) symmetric divisions in the stomatal pathway
CC       (PubMed:20675570, PubMed:24687979). Represses CYCA2-3 in newly formed
CC       guard cells (PubMed:21772250). Together with MYB88, regulates stomata
CC       spacing by restricting divisions late in the stomatal cell lineage thus
CC       limiting the number of GMC divisions (PubMed:16155180). In
CC       collaboration with CDKB1-1 and CDKB1-2, restrict the G1/S transition
CC       and chloroplast and nuclear number during stomatal formation, and
CC       normally maintain fate and developmental progression throughout the
CC       stomatal cell lineage (PubMed:24123248). Involved in sensing and/or
CC       transducing abiotic stress (e.g. drought and salt), probably via the
CC       positive regulation of NAC019 (PubMed:21105921). Regulates female
CC       reproduction being required for entry into megasporogenesis, probably
CC       via the regulation of cell cycle genes (PubMed:22915737). Plays a minor
CC       role in lateral roots (LRs) initiation (PubMed:26578065). Involved
CC       complementarily in establishing the gravitropic set-point angles of
CC       lateral roots by regulating the transcription of PIN3 and PIN7 in
CC       gravity-sensing cells of primary and lateral roots (PubMed:26578169).
CC       {ECO:0000269|PubMed:16155180, ECO:0000269|PubMed:20675570,
CC       ECO:0000269|PubMed:21105921, ECO:0000269|PubMed:21772250,
CC       ECO:0000269|PubMed:22915737, ECO:0000269|PubMed:24123248,
CC       ECO:0000269|PubMed:24571519, ECO:0000269|PubMed:24687979,
CC       ECO:0000269|PubMed:26578065, ECO:0000269|PubMed:26578169}.
CC   -!- SUBUNIT: Interacts with RBR1. {ECO:0000269|PubMed:24571519}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC       ECO:0000269|PubMed:20675570}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=F4IRB4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4IRB4-2; Sequence=VSP_058732, VSP_058733;
CC       Name=3;
CC         IsoId=F4IRB4-3; Sequence=VSP_058731;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in all organs including
CC       roots, leaves, hypocotyls stems, flowers, siliques and buds.
CC       {ECO:0000269|PubMed:16155180, ECO:0000269|PubMed:26391711}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates during ovule development. Detected at
CC       low levels in ovules and in the embryo sac of stage 13 flowers
CC       (PubMed:22915737). Not detected during embryo development. In seedlings
CC       and young plants, present in some spots (presumably stomata) in
CC       cotyledons and later in veins of hypocotyls as well as of petioles,
CC       hydathodes, stipules, in roots and lateral root primordia, and in the
CC       lower halves of first leaves. Detected in the phloem, as well as in the
CC       cortex of inflorescence stems. In roots, confined in developing xylem
CC       cells in the part of the differentiation zone with well-developed root
CC       hairs (PubMed:26391711). Present in lateral root tips and subsequently
CC       in a larger area. Accumulates in columella cells of lateral roots
CC       (PubMed:26578169). Expressed at the base of developing flowers,
CC       including ovaries. In flowers, detected in parts of the major stem
CC       axis, and in the anther at some stages of development, present in veins
CC       of sepals and accumulates progressively in ovaries, filaments,
CC       receptacles, and ovules. Also detected in the valve margins and
CC       receptacles of siliques and at the joint between the stigma and the
CC       style, as well as in the tapetum around pollen grains in maturing
CC       anthers (PubMed:26391711). {ECO:0000269|PubMed:22915737,
CC       ECO:0000269|PubMed:26391711, ECO:0000269|PubMed:26578169}.
CC   -!- DISRUPTION PHENOTYPE: Double mutants flp-7 myb88 and flp-1 myb88 have
CC       strong defects in stomata repartition with large stomatal clusters
CC       formation (PubMed:16155180). Increased accumulation of CDKB1-1 in the
CC       double mutant flp-1 myb88 (PubMed:20675570). Double mutants flp-1 myb88
CC       have increased susceptibility to drought and high salt (NaCl), as well
CC       as increased rates of water loss; these phenotypes are associated with
CC       reduced accumulation of many typical abiotic stress gene transcripts.
CC       Lower stomatal closure in response to abscisic acid (ABA) treatment
CC       (PubMed:21105921). Accumulation of CYCA2-3 in newly formed guard cells
CC       in flp-1 myb88 double mutant (PubMed:21772250). The double mutants flp-
CC       1 myb88 and flp-7 myb88 treated with oryzalin, a microtubule
CC       depolymerizing drug, exhibit round-to-oval-shaped single guard cells
CC       (sGCs) associated with increased DNA content due to endoreplication
CC       leading to 10C DNA levels. The quadruple mutant flp-1 myb88 cdkb1;1
CC       cdkb1;2 has a reduced number of large single guard cells blocked at
CC       mitosis, with strongly altered shape and size and characterized by
CC       enlarged nucleus due to endomitosis and endocycling, as well as
CC       extensive chloroplast replication (PubMed:24123248). Triple mutants
CC       cdka;1 flp-1 myb88 don't have guard cells stacks but accumulates sGCs.
CC       Accumulation of CDKA-1 in the double mutant flp-1 myb88
CC       (PubMed:24687979). Increased number of ovules produced by the placenta
CC       but reduced female fertility due to defective meiotic entry and
CC       progression, and subsequent altered embryo sac development, thus
CC       leading to reduced seed set (PubMed:22915737). The double mutants flp-1
CC       myb88 and flp-7 myb88 lack lateral roots with reduced PIN3 levels
CC       (PubMed:26578065). Abnormal gravitropic set-point angles (lower than 30
CC       degree) of lateral roots (PubMed:26578169).
CC       {ECO:0000269|PubMed:16155180, ECO:0000269|PubMed:20675570,
CC       ECO:0000269|PubMed:21105921, ECO:0000269|PubMed:21772250,
CC       ECO:0000269|PubMed:22915737, ECO:0000269|PubMed:24123248,
CC       ECO:0000269|PubMed:24687979, ECO:0000269|PubMed:26578065,
CC       ECO:0000269|PubMed:26578169}.
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DR   EMBL; AF175994; AAD53099.2; -; mRNA.
DR   EMBL; AY550305; AAS58516.1; -; mRNA.
DR   EMBL; AC002521; AAC05340.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05629.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05630.1; -; Genomic_DNA.
DR   EMBL; BT026343; ABH04450.1; -; mRNA.
DR   PIR; T00846; T00846.
DR   RefSeq; NP_001030957.1; NM_001035880.3. [F4IRB4-1]
DR   RefSeq; NP_565291.2; NM_126337.4. [F4IRB4-2]
DR   AlphaFoldDB; F4IRB4; -.
DR   SMR; F4IRB4; -.
DR   STRING; 3702.AT2G02820.2; -.
DR   PaxDb; F4IRB4; -.
DR   ProteomicsDB; 251410; -. [F4IRB4-1]
DR   EnsemblPlants; AT2G02820.1; AT2G02820.1; AT2G02820. [F4IRB4-2]
DR   EnsemblPlants; AT2G02820.2; AT2G02820.2; AT2G02820. [F4IRB4-1]
DR   GeneID; 814812; -.
DR   Gramene; AT2G02820.1; AT2G02820.1; AT2G02820. [F4IRB4-2]
DR   Gramene; AT2G02820.2; AT2G02820.2; AT2G02820. [F4IRB4-1]
DR   KEGG; ath:AT2G02820; -.
DR   Araport; AT2G02820; -.
DR   TAIR; locus:2058827; AT2G02820.
DR   eggNOG; KOG0048; Eukaryota.
DR   HOGENOM; CLU_018700_1_0_1; -.
DR   InParanoid; F4IRB4; -.
DR   OrthoDB; 1499244at2759; -.
DR   PhylomeDB; F4IRB4; -.
DR   PRO; PR:F4IRB4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IRB4; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR   GO; GO:0010052; P:guard cell differentiation; IGI:UniProtKB.
DR   GO; GO:0010235; P:guard mother cell cytokinesis; IMP:UniProtKB.
DR   GO; GO:0010444; P:guard mother cell differentiation; IMP:UniProtKB.
DR   GO; GO:0048527; P:lateral root development; IMP:UniProtKB.
DR   GO; GO:0009554; P:megasporogenesis; IMP:UniProtKB.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:UniProtKB.
DR   GO; GO:1901333; P:positive regulation of lateral root development; IMP:UniProtKB.
DR   GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR   GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR   GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR   GO; GO:0032875; P:regulation of DNA endoreduplication; IMP:UniProtKB.
DR   GO; GO:2000037; P:regulation of stomatal complex patterning; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR   GO; GO:0009629; P:response to gravity; IMP:UniProtKB.
DR   GO; GO:0010376; P:stomatal complex formation; IMP:UniProtKB.
DR   CDD; cd00167; SANT; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Developmental protein; DNA-binding;
KW   Nucleus; Reference proteome; Repeat; Repressor; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..484
FT                   /note="Transcription factor MYB88"
FT                   /id="PRO_0000438721"
FT   DOMAIN          25..76
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          77..131
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        53..76
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        104..127
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           13..20
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        226..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         177..484
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_058731"
FT   VAR_SEQ         449..455
FT                   /note="ERNFLLK -> VSIHLTN (in isoform 2)"
FT                   /id="VSP_058732"
FT   VAR_SEQ         456..484
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058733"
FT   CONFLICT        165
FT                   /note="A -> V (in Ref. 1; AAD53099)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   484 AA;  54508 MW;  59947404B3C6E4D5 CRC64;
     MEETTKQNNM KKKKKILLHS DDSKKKERHI VTWSPEEDDI LRKQISLQGT ENWAIIASKF
     NDKSTRQCRR RWYTYLNSDF KRGGWSPEED TLLCEAQRLF GNRWTEIAKV VSGRTDNAVK
     NRFTTLCKKR AKHEAMAKEN RIACCVNSDN KRLLFPDGIS TPLKAESESP LTKKMRRSHI
     PNLTEIKSYG DRSHIKVEST MNQQRRHPFS VVAHNATSSD GTEEQKQIGN VKESDGEDKS
     NQEVFLKKDD SKVTALMQQA ELLSSLAQKV NADNTDQSME NAWKVLQDFL NKSKENDLFR
     YGIPDIDFQL DEFKDLVEDL RSSNEDSQSS WRQPDLHDSP ASSEYSSGSG SGSTIMTHPS
     GDKTQQLMSD TQTTSHQQNG GELLQDNGIV SDATVEQVGL LSTGHDVLKN SNETVPIPGE
     EEFNSPVQVT PLFRSLAAGI PSPQFSESER NFLLKTLGVE SPSPYPSANP SQPPPCKRVL
     LDSL
 
 
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