TUN_ARATH
ID TUN_ARATH Reviewed; 465 AA.
AC Q8L7M0; B3H5N4; Q9FX74;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=UDP-glycosyltransferase TURAN {ECO:0000303|PubMed:25919390};
DE EC=2.4.1.-;
GN Name=TUN {ECO:0000303|PubMed:25919390};
GN OrderedLocusNames=At1g16570 {ECO:0000312|EMBL:AEE29472.1};
GN ORFNames=F19K19.11 {ECO:0000312|EMBL:AAG10823.1};
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:AAM91582.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25919390; DOI=10.1371/journal.pbio.1002139;
RA Lindner H., Kessler S.A., Mueller L.M., Shimosato-Asano H.,
RA Boisson-Dernier A., Grossniklaus U.;
RT "TURAN and EVAN mediate pollen tube reception in Arabidopsis Synergids
RT through protein glycosylation.";
RL PLoS Biol. 13:E1002139-E1002139(2015).
CC -!- FUNCTION: Required for pollen tube (PT) growth and integrity by
CC affecting the stability of the pollen-specific ANX1 and ANX2 proteins.
CC Involved in protein N-glycosylation in the endoplasmic reticulum (ER),
CC especially in the female gametophyte. Mediates PT reception in
CC synergids through protein glycosylation. {ECO:0000269|PubMed:25919390}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25919390}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L7M0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L7M0-2; Sequence=VSP_057832;
CC -!- DEVELOPMENTAL STAGE: In ovules, mostly observed in the female
CC gametophyte (FG) including the synergids, which showed a ring shaped
CC localization around their nuclei, and throughout the pollen tube (PT).
CC {ECO:0000269|PubMed:25919390}.
CC -!- DISRUPTION PHENOTYPE: Pollen tube (PT) overgrowth inside the female
CC gametophyte (FG) without PT rupture. Premature burst immediately after
CC PT germination. Dwarf plants accumulating anthocyanins and dying
CC prematurely in RNAi conditions. Impaired accumulation of ANX1 and ANX2
CC proteins. {ECO:0000269|PubMed:25919390}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 33 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ139004; AHL38944.1; -; mRNA.
DR EMBL; AC011808; AAG10823.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29472.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29473.1; -; Genomic_DNA.
DR EMBL; AY128379; AAM91582.1; -; mRNA.
DR EMBL; BT008762; AAP49524.1; -; mRNA.
DR PIR; A86301; A86301.
DR RefSeq; NP_001117297.1; NM_001123825.1. [Q8L7M0-2]
DR RefSeq; NP_173105.1; NM_101521.3. [Q8L7M0-1]
DR AlphaFoldDB; Q8L7M0; -.
DR STRING; 3702.AT1G16570.2; -.
DR CAZy; GT33; Glycosyltransferase Family 33.
DR PRIDE; Q8L7M0; -.
DR ProteomicsDB; 234633; -. [Q8L7M0-1]
DR EnsemblPlants; AT1G16570.1; AT1G16570.1; AT1G16570. [Q8L7M0-1]
DR EnsemblPlants; AT1G16570.2; AT1G16570.2; AT1G16570. [Q8L7M0-2]
DR GeneID; 838227; -.
DR Gramene; AT1G16570.1; AT1G16570.1; AT1G16570. [Q8L7M0-1]
DR Gramene; AT1G16570.2; AT1G16570.2; AT1G16570. [Q8L7M0-2]
DR KEGG; ath:AT1G16570; -.
DR Araport; AT1G16570; -.
DR TAIR; locus:2017963; AT1G16570.
DR eggNOG; KOG2941; Eukaryota.
DR OMA; PLKVLWQ; -.
DR OrthoDB; 816895at2759; -.
DR PhylomeDB; Q8L7M0; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8L7M0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7M0; baseline and differential.
DR Genevisible; Q8L7M0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0048868; P:pollen tube development; IMP:UniProtKB.
DR GO; GO:0010483; P:pollen tube reception; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IMP:TAIR.
DR InterPro; IPR026051; ALG1-like.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR13036; PTHR13036; 1.
DR Pfam; PF13579; Glyco_trans_4_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..465
FT /note="UDP-glycosyltransferase TURAN"
FT /id="PRO_0000433636"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..465
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 414
FT /note="L -> LVSNSSFFLKDYFTKSTAEDSSNVLVFCLCEQ (in isoform
FT 2)"
FT /id="VSP_057832"
SQ SEQUENCE 465 AA; 52321 MW; A507B7E5B6DD971A CRC64;
MGKRGRACVV VLGDLGRSPR MQYHALSLAR QASFQVDIVA YGGSIPHEAV LNHPSIHIHT
MAQPRFIQYF PKILYPVTLL LKAFIQFTML LWFLFVKVPA PDIFLVQNPP SVPTLIAVKW
ASSWRRAAFV VDWHNFGYTL LALSLGRNNL LVSLYRWSEN HYGKMATGSL CVTKAMQHEL
DQNWGVRAKV LYDQPPEFFR PALLEERHEL FCRVRKDLCH PIGVYDFISR ELENQELNET
LFTTKFNADI SLKQNRPALV VSSTSWTPDE NFGILLEAAV MYDRRVAARS KGSETAEISE
EQHHYPNLLF IITGKGPEKE MYEEKIKRLN LRHVAFRTMW LAAEDYPLLL GSADLGVCLH
TSSSGLDLPM KVVDMFGCGL PVCSVSYSCI QELVKDGKNG LLFSSSSELA DQLLILFKGF
PGNCDALMSL KAGAMETGSS GRWATEWEDC AKPLITQVVS QIADS
