SIA1_ARATH
ID SIA1_ARATH Reviewed; 474 AA.
AC Q8VZJ0; Q9FRR9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Sialyltransferase-like protein 1 {ECO:0000305};
DE EC=2.4.-.- {ECO:0000305};
DE AltName: Full=Protein MALE GAMETOPHYTE DEFECTIVE 2 {ECO:0000303|PubMed:20738727};
GN Name=SIA1 {ECO:0000305}; Synonyms=MGP2 {ECO:0000303|PubMed:20738727};
GN OrderedLocusNames=At1g08660 {ECO:0000312|Araport:AT1G08660};
GN ORFNames=F22O13.14 {ECO:0000312|EMBL:AAF99778.1};
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=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].
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20738727; DOI=10.1111/j.1744-7909.2010.00963.x;
RA Deng Y., Wang W., Li W.Q., Xia C., Liao H.Z., Zhang X.Q., Ye D.;
RT "MALE GAMETOPHYTE DEFECTIVE 2, encoding a sialyltransferase-like protein,
RT is required for normal pollen germination and pollen tube growth in
RT Arabidopsis.";
RL J. Integr. Plant Biol. 52:829-843(2010).
CC -!- FUNCTION: Required for normal pollen grain germination and pollen tube
CC growth. May not be required for pollen development and female
CC gametophytic function. {ECO:0000269|PubMed:20738727}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:20738727}; 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=Q8VZJ0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in inflorescences and siliques and
CC at lower levels in roots, leaves and stems.
CC {ECO:0000269|PubMed:20738727}.
CC -!- DISRUPTION PHENOTYPE: Inhibition of pollen germination and retarded
CC pollen tube growth. {ECO:0000269|PubMed:20738727}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99778.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ139019; AHL38959.1; -; mRNA.
DR EMBL; AC003981; AAF99778.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28328.1; -; Genomic_DNA.
DR EMBL; AY064135; AAL36042.1; -; mRNA.
DR EMBL; AY124807; AAM70516.1; -; mRNA.
DR PIR; T00720; T00720.
DR RefSeq; NP_850940.1; NM_180609.4. [Q8VZJ0-1]
DR AlphaFoldDB; Q8VZJ0; -.
DR STRING; 3702.AT1G08660.1; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q8VZJ0; -.
DR PRIDE; Q8VZJ0; -.
DR ProteomicsDB; 234577; -. [Q8VZJ0-1]
DR DNASU; 837388; -.
DR EnsemblPlants; AT1G08660.1; AT1G08660.1; AT1G08660. [Q8VZJ0-1]
DR GeneID; 837388; -.
DR Gramene; AT1G08660.1; AT1G08660.1; AT1G08660. [Q8VZJ0-1]
DR KEGG; ath:AT1G08660; -.
DR Araport; AT1G08660; -.
DR TAIR; locus:2025540; AT1G08660.
DR eggNOG; KOG2692; Eukaryota.
DR HOGENOM; CLU_039790_0_0_1; -.
DR InParanoid; Q8VZJ0; -.
DR OrthoDB; 532831at2759; -.
DR PhylomeDB; Q8VZJ0; -.
DR PRO; PR:Q8VZJ0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VZJ0; baseline and differential.
DR Genevisible; Q8VZJ0; AT.
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; IDA: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:0008373; F:sialyltransferase activity; IEA:InterPro.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
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 InterPro; IPR044782; SIA1/STLP5.
DR PANTHER; PTHR47486; PTHR47486; 1.
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..474
FT /note="Sialyltransferase-like protein 1"
FT /id="PRO_0000434309"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..474
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 376..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 474 AA; 54216 MW; 13094B7D300B938E CRC64;
MRSHQAGRKL PLLQLLGCVA VFSVFVFTIQ SSFFADNNRK LDLQPEDIQI LSDFQSSVQQ
CVANRGLGLS AHIIDHCNLI LKFPEGTNST WYNAQFKVFE ALEFKYNVCE AVLLWEQYRN
MTTVLTREYL DVRPDGWLDY AAMRIAQLGA DKCYNRTLCE EHLNVILPAK PPFHPRQFHK
CAVVGNSGDL LKTEFGEEID SHDAVFRDNE APVNEKYAKY VGVKRDFRLV VRGAARNMIK
ILNGSDNEVL IIKSVTHRDF NEMIKRIPNP VYLFQGIVLR RGAKGTGMKS IELALSMCDI
VDIYGFTVDP GYTEWTRYFS TPRKGHNPLQ GRAYYQLLEC LGVIRIHSPM RSERKEDWSS
VPSREMISRA HTAALRLQRS QQPTSSKRDG SGQFGNCKVW GDADPTKGPV SGSPDMSETR
KKSNYKKWEV MPFRSLRKEA RDHYIQMKGV SQYKMDGNKL DDLVCVRHPL KLDT
