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MWL2_ARATH
ID   MWL2_ARATH              Reviewed;         217 AA.
AC   O65708;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Protein MODIFYING WALL LIGNIN-2 {ECO:0000303|PubMed:26930070};
DE            Short=MWL-2 {ECO:0000303|PubMed:26930070};
DE   Flags: Precursor;
GN   Name=MWL2 {ECO:0000303|PubMed:26930070};
GN   OrderedLocusNames=At4g19370 {ECO:0000312|Araport:AT4G19370};
GN   ORFNames=T5K18.150 {ECO:0000312|EMBL:AEE84173.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=16244158; DOI=10.1104/pp.105.063479;
RA   Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA   Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT   "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT   reveals numerous transcript variants.";
RL   Plant Physiol. 139:1323-1337(2005).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=26930070; DOI=10.1371/journal.pone.0150254;
RA   Mewalal R., Mizrachi E., Coetzee B., Mansfield S.D., Myburg A.A.;
RT   "The Arabidopsis domain of unknown function 1218 (DUF1218) containing
RT   proteins, MODIFYING WALL LIGNIN-1 and 2 (At1g31720/MWL-1 and At4g19370/MWL-
RT   2) function redundantly to alter secondary cell wall lignin content.";
RL   PLoS ONE 11:E0150254-E0150254(2016).
CC   -!- FUNCTION: Together with MWL1, contributes to secondary cell wall
CC       biology, specifically lignin biosynthesis.
CC       {ECO:0000269|PubMed:26930070}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26930070};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Double mutants lacking both
CC       MWL1 and MWL2 exhibit smaller rosettes with a decrease in rosette fresh
CC       weight and stem height associated with a reduction in total lignin
CC       content and an increase in syringyl/guaiacyl (S/G) monomer ratio.
CC       {ECO:0000269|PubMed:26930070}.
CC   -!- SIMILARITY: Belongs to the DESIGUAL family. {ECO:0000305}.
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DR   EMBL; AL022580; CAA18624.1; -; Genomic_DNA.
DR   EMBL; AL161550; CAB78939.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84173.1; -; Genomic_DNA.
DR   EMBL; AY954860; AAX55186.1; -; mRNA.
DR   EMBL; DQ132708; AAZ52738.1; -; mRNA.
DR   PIR; T05820; T05820.
DR   RefSeq; NP_193672.1; NM_118057.3.
DR   AlphaFoldDB; O65708; -.
DR   SMR; O65708; -.
DR   STRING; 3702.AT4G19370.1; -.
DR   PaxDb; O65708; -.
DR   PRIDE; O65708; -.
DR   EnsemblPlants; AT4G19370.1; AT4G19370.1; AT4G19370.
DR   GeneID; 827678; -.
DR   Gramene; AT4G19370.1; AT4G19370.1; AT4G19370.
DR   KEGG; ath:AT4G19370; -.
DR   Araport; AT4G19370; -.
DR   TAIR; locus:2140391; AT4G19370.
DR   eggNOG; ENOG502S1EJ; Eukaryota.
DR   HOGENOM; CLU_110866_0_0_1; -.
DR   InParanoid; O65708; -.
DR   OMA; RYEEGGC; -.
DR   OrthoDB; 1145302at2759; -.
DR   PhylomeDB; O65708; -.
DR   PRO; PR:O65708; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O65708; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009808; P:lignin metabolic process; IGI:TAIR.
DR   InterPro; IPR009606; DEAL/Modifying_wall_lignin1/2.
DR   Pfam; PF06749; DUF1218; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Lignin biosynthesis; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..217
FT                   /note="Protein MODIFYING WALL LIGNIN-2"
FT                   /id="PRO_0000446980"
FT   TOPO_DOM        24..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..94
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   217 AA;  24387 MW;  D5DB695407191211 CRC64;
     MHNLFLYSVV FSLGLVSFIT CFAAEFKRTQ KEDIRWDTER NCYVPGSHAF GLGSAAVLCF
     CLAQIVGNIV VFRNHRTRTK REDGYKITDL TLPTVLLLLS WSNFVVVVLI LSTAISMSRA
     QAYGEGWLDE DCYLVKDGVF AASGCLAILG LGALTISATR IKVKKQQQLV QVVIKDQNQD
     QRRSMEEEQK HDEHQTNKSE SVIHLVEEVS STNISRI
 
 
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