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GLYT7_ARATH
ID   GLYT7_ARATH             Reviewed;         514 AA.
AC   Q5XV99; Q9M2M7;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Glycosyltransferase-like At3g57200 {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g57200 {ECO:0000312|Araport:AT3G57200};
GN   ORFNames=F28O9.50 {ECO:0000312|EMBL:CAB68126.1};
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 {ECO:0000312|EMBL:AAU44493.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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;
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   [4]
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   [5]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=15010620; DOI=10.1023/b:plan.0000019067.05185.d6;
RA   Lertpiriyapong K., Sung Z.R.;
RT   "The elongation defective1 mutant of Arabidopsis is impaired in the gene
RT   encoding a serine-rich secreted protein.";
RL   Plant Mol. Biol. 53:581-595(2003).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=14742875; DOI=10.1105/tpc.018077;
RA   Brocard-Gifford I., Lynch T.J., Garcia M.E., Malhotra B., Finkelstein R.R.;
RT   "The Arabidopsis thaliana ABSCISIC ACID-INSENSITIVE8 encodes a novel
RT   protein mediating abscisic acid and sugar responses essential for growth.";
RL   Plant Cell 16:406-421(2004).
CC   -!- FUNCTION: Involved in the coordination between cell elongation and
CC       cellulose synthesis by promoting the expression of genes involved in
CC       cell elongation and cellulose synthesis. Acts as a regulator of
CC       plasmodesmatal permeability. Maybe a glycosyltransferase.
CC       {ECO:0000250|UniProtKB:Q9C9Z9}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:Q9C9Z9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9C9Z9}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9C9Z9}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB68126.1; Type=Erroneous gene model prediction;
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DR   EMBL; AL137080; CAB68126.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79626.1; -; Genomic_DNA.
DR   EMBL; AY735623; AAU44493.1; -; mRNA.
DR   EMBL; AY954853; AAX55179.1; -; mRNA.
DR   PIR; T45798; T45798.
DR   RefSeq; NP_191279.3; NM_115580.5.
DR   AlphaFoldDB; Q5XV99; -.
DR   iPTMnet; Q5XV99; -.
DR   PaxDb; Q5XV99; -.
DR   PRIDE; Q5XV99; -.
DR   ProteomicsDB; 247374; -.
DR   EnsemblPlants; AT3G57200.1; AT3G57200.1; AT3G57200.
DR   GeneID; 824887; -.
DR   Gramene; AT3G57200.1; AT3G57200.1; AT3G57200.
DR   KEGG; ath:AT3G57200; -.
DR   Araport; AT3G57200; -.
DR   TAIR; locus:2082573; AT3G57200.
DR   eggNOG; ENOG502QPZC; Eukaryota.
DR   HOGENOM; CLU_032860_0_0_1; -.
DR   InParanoid; Q5XV99; -.
DR   OrthoDB; 431242at2759; -.
DR   PhylomeDB; Q5XV99; -.
DR   PRO; PR:Q5XV99; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q5XV99; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009505; C:plant-type cell wall; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid; IEA:InterPro.
DR   InterPro; IPR008166; Glyco_transf_92.
DR   InterPro; IPR044224; KOBITO1-like.
DR   PANTHER; PTHR46701; PTHR46701; 1.
DR   Pfam; PF01697; Glyco_transf_92; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cell membrane; Cell wall;
KW   Cell wall biogenesis/degradation; Cytoplasm; Developmental protein;
KW   Differentiation; Glycoprotein; Glycosyltransferase; Growth regulation;
KW   Membrane; Reference proteome; Secreted; Signal; Transferase.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..514
FT                   /note="Glycosyltransferase-like At3g57200"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000430756"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   514 AA;  58424 MW;  59067B5D5F6576A4 CRC64;
     MAGLYSSSSS SKPTLSSSPS SSSSSRLFLL VTLLPLSLAC FAFVLQWRGG LDDPVTHWSI
     DHHEFPGMVT TQEKRSLRRS VSDSGCVDLL GQSRSPSFPY FRNWKFDYHS DLKPRICITT
     STSAGLEQTL PWIYFHKVIG VSTFYLFVEG KAASPNVSRV LETIPGVKVI YRTKELEEKQ
     AKSRIWNETW LSSFFYKPCN YELFVKQSLN MEMAITMAQD AGMEWIIHLD TDELIHPSGT
     HEYSLRKLLG NISADVDVVI FPNYESSVER DDIREPFSEV SMFKKNFDHL LRDVYFGNYK
     DATRGNPNYF LTYGNGKAAA RVQDHLRPNG AHRWHNYRKS PNEVKLEEAA VLHYTYPRFS
     DLTSRRDRCG CKPTKVDVKR CFMLEFDRAA FIIASTASSE EMLQWYREHV VWTDEKLKLK
     LLRKGILTRI YAPMVIIQEL REAGVFSSVV IAAHKSPSKN SSTADSTSGI TRESSQETGK
     RRVLEFHLDV DGESQASAVP PQSPPGLEAT QMEL
 
 
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