SIA2_ARATH
ID SIA2_ARATH Reviewed; 440 AA.
AC Q8RY00; Q9M301;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Sialyltransferase-like protein 2 {ECO:0000303|PubMed:24825296};
DE EC=2.4.-.- {ECO:0000305};
GN Name=SIA2 {ECO:0000303|PubMed:24825296};
GN OrderedLocusNames=At3g48820 {ECO:0000312|Araport:AT3G48820};
GN ORFNames=T21J18.90 {ECO:0000312|EMBL:CAB87910.1};
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 [MRNA].
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=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 [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].
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, AND SUBCELLULAR LOCATION.
RX PubMed=19470101; DOI=10.1111/j.1438-8677.2008.00138.x;
RA Daskalova S.M., Pah A.R., Baluch D.P., Lopez L.C.;
RT "The Arabidopsis thaliana putative sialyltransferase resides in the Golgi
RT apparatus but lacks the ability to transfer sialic acid.";
RL Plant Biol. 11:284-299(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24825296; DOI=10.1093/aob/mcu093;
RA Dumont M., Lehner A., Bouton S., Kiefer-Meyer M.C., Voxeur A., Pelloux J.,
RA Lerouge P., Mollet J.C.;
RT "The cell wall pectic polymer rhamnogalacturonan-II is required for proper
RT pollen tube elongation: implications of a putative sialyltransferase-like
RT protein.";
RL Ann. Bot. 114:1177-1188(2014).
CC -!- FUNCTION: May be involved in the transfer of 2-keto-3-deoxy-D-lyxo-
CC heptulosaric acid (Dha) and/or 2-keto-3-deoxy-D-manno-octulosonic acid
CC (Kdo) on the homogalacturonan backbone of rhamnogalacturonan-II.
CC Required for efficient pollen grain germination and pollen tube
CC elongation (PubMed:24825296). Does not possess sialyltransferase
CC activity in vitro (PubMed:19470101). {ECO:0000269|PubMed:19470101,
CC ECO:0000269|PubMed:24825296}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19470101}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8RY00-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Male gametophytic lethality when homozygous. May
CC be due to defect in pollen grain germination and pollen tube growth.
CC {ECO:0000269|PubMed:24825296}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87910.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ138796; AHL38736.1; -; mRNA.
DR EMBL; AL132963; CAB87910.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78459.1; -; Genomic_DNA.
DR EMBL; AY080589; AAL85966.1; -; mRNA.
DR EMBL; AY133816; AAM91750.1; -; mRNA.
DR PIR; T49278; T49278.
DR RefSeq; NP_190451.2; NM_114741.5. [Q8RY00-1]
DR AlphaFoldDB; Q8RY00; -.
DR STRING; 3702.AT3G48820.1; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q8RY00; -.
DR PRIDE; Q8RY00; -.
DR ProteomicsDB; 234511; -. [Q8RY00-1]
DR EnsemblPlants; AT3G48820.1; AT3G48820.1; AT3G48820. [Q8RY00-1]
DR GeneID; 824043; -.
DR Gramene; AT3G48820.1; AT3G48820.1; AT3G48820. [Q8RY00-1]
DR KEGG; ath:AT3G48820; -.
DR Araport; AT3G48820; -.
DR TAIR; locus:2099468; AT3G48820.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q8RY00; -.
DR OrthoDB; 532831at2759; -.
DR PhylomeDB; Q8RY00; -.
DR PRO; PR:Q8RY00; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RY00; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009846; P:pollen germination; IMP:UniProtKB.
DR GO; GO:0009860; P:pollen tube growth; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..440
FT /note="Sialyltransferase-like protein 2"
FT /id="PRO_0000434310"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..440
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 440 AA; 49480 MW; 25B999BC4A5701BC CRC64;
MKLLHLIFLL ALTTGISAVL IYIIGVSNLY ESNRFTNEDL EALQSLQNGF QKCVSANGLG
LQAAMGRDYC KVSINFPKDT VPKWKDPKSG ELEGLSYEFD LCEAVATWEQ VRNSSTILTK
EYIDALPNGW EDYAWRRINK GIQLNRCQNK SLCIEKLSLV LPETPPYFPR QFGRCAVIGN
SGDLLKTKFG KEIDTYDTVL RENGAPIQNY KEYVGEKSTF RLLNRGSAKA LDKVVELDEK
KQEVLLVKTT IHDIMNKMIR EVPIKNPVYL MLGASFGSAA KGTGLKALEF ALSTCDSVDM
YGFTVDPGYK EWTRYFSESR QGHTPLHGRA YYQMMECLGL IKIHSPMRAD PNRVVKWVPS
RSTIRSARIA AEKLLRRVGA GSADPLASCS IVKKRNKNKR PMVSHLRKPV SDHQKFVRST
SMYPVEHSPG HGQLCITPAD
