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GATL4_ARATH
ID   GATL4_ARATH             Reviewed;         351 AA.
AC   Q9M8J2; Q8GX53;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable galacturonosyltransferase-like 4;
DE            EC=2.4.1.-;
DE   AltName: Full=Galactinol synthase 9;
DE            Short=AtGolS9;
DE            Short=GolS-9;
GN   Name=GATL4; Synonyms=GOLS9; OrderedLocusNames=At3g06260; ORFNames=F28L1.20;
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=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] OF 149-351.
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-351.
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16540543; DOI=10.1073/pnas.0600120103;
RA   Sterling J.D., Atmodjo M.A., Inwood S.E., Kumar Kolli V.S., Quigley H.F.,
RA   Hahn M.G., Mohnen D.;
RT   "Functional identification of an Arabidopsis pectin biosynthetic
RT   homogalacturonan galacturonosyltransferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5236-5241(2006).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18502973; DOI=10.1104/pp.108.122465;
RA   Nishizawa A., Yabuta Y., Shigeoka S.;
RT   "Galactinol and raffinose constitute a novel function to protect plants
RT   from oxidative damage.";
RL   Plant Physiol. 147:1251-1263(2008).
CC   -!- FUNCTION: May be involved in pectin and/or xylans biosynthesis in cell
CC       walls. {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC43039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC018907; AAF30319.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74366.1; -; Genomic_DNA.
DR   EMBL; BT003687; AAO39915.1; -; mRNA.
DR   EMBL; AK118430; BAC43039.1; ALT_INIT; mRNA.
DR   RefSeq; NP_187277.1; NM_111501.3.
DR   AlphaFoldDB; Q9M8J2; -.
DR   SMR; Q9M8J2; -.
DR   BioGRID; 5135; 1.
DR   IntAct; Q9M8J2; 1.
DR   STRING; 3702.AT3G06260.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; Q9M8J2; -.
DR   PRIDE; Q9M8J2; -.
DR   ProteomicsDB; 230452; -.
DR   EnsemblPlants; AT3G06260.1; AT3G06260.1; AT3G06260.
DR   GeneID; 819800; -.
DR   Gramene; AT3G06260.1; AT3G06260.1; AT3G06260.
DR   KEGG; ath:AT3G06260; -.
DR   Araport; AT3G06260; -.
DR   TAIR; locus:2082450; AT3G06260.
DR   eggNOG; ENOG502QTN8; Eukaryota.
DR   HOGENOM; CLU_034713_0_0_1; -.
DR   InParanoid; Q9M8J2; -.
DR   OMA; HVPVFRE; -.
DR   OrthoDB; 1520602at2759; -.
DR   PhylomeDB; Q9M8J2; -.
DR   UniPathway; UPA00845; -.
DR   PRO; PR:Q9M8J2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M8J2; baseline and differential.
DR   Genevisible; Q9M8J2; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR   GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..351
FT                   /note="Probable galacturonosyltransferase-like 4"
FT                   /id="PRO_0000392606"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..351
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   351 AA;  40337 MW;  20EBAB1D8F080A94 CRC64;
     MASRSLSYTQ LLGLLSFILL LVTTTTMAVR VGVILHKPSA PTLPVFREAP AFRNGDQCGT
     READQIHIAM TLDTNYLRGT MAAVLSLLQH STCPENLSFH FLSLPHFEND LFTSIKSTFP
     YLNFKIYQFD PNLVRSKISK SIRQALDQPL NYARIYLADI IPSSVDRIIY LDSDLVVVDD
     IEKLWHVEME GKVVAAPEYC HANFTHYFTR TFWSDPVLVK VLEGKRPCYF NTGVMVVDVN
     KWRKGMYTQK VEEWMTIQKQ KRIYHLGSLP PFLLIFAGDI KAVNHRWNQH GLGGDNFEGR
     CRTLHPGPIS LLHWSGKGKP WLRLDSRKPC IVDHLWAPYD LYRSSRHSLE E
 
 
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