MUC70_ARATH
ID MUC70_ARATH Reviewed; 581 AA.
AC Q9FZ97; Q8W4K7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Probable hexosyltransferase MUCI70 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:30228108};
DE AltName: Full=Protein MUCILAGE-RELATED 70 {ECO:0000303|PubMed:30228108};
GN Name=MUCI70 {ECO:0000303|PubMed:30228108};
GN OrderedLocusNames=At1g28240 {ECO:0000312|Araport:AT1G28240};
GN ORFNames=F3H9.11 {ECO:0000312|EMBL:AAF98431.1};
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;
RA Zeng W., Gluza P., Heazlewood J.;
RT "Arabidopsis glycosyltransfereases: an update.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP PATHWAY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=30228108; DOI=10.1104/pp.18.00584;
RA Voiniciuc C., Engle K.A., Guenl M., Dieluweit S., Schmidt M.H., Yang J.Y.,
RA Moremen K.W., Mohnen D., Usadel B.;
RT "Identification of key enzymes for pectin synthesis in seed mucilage.";
RL Plant Physiol. 178:1045-1064(2018).
CC -!- FUNCTION: Probable glycosyltransferase involved in pectin and/or xylans
CC biosynthesis in cell walls (By similarity). Together with IRX14,
CC required for xylan and pectin synthesis in seed coat epidermal (SCE)
CC cells (PubMed:30228108). Collaboratively with GAUT11, essential for the
CC accumulation of seed mucilage, a gelatinous wall rich in unbranched
CC rhamnogalacturonan I (RG I), and for shaping the surface morphology of
CC seeds (PubMed:30228108). {ECO:0000250|UniProtKB:Q9LE59,
CC ECO:0000269|PubMed:30228108}.
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC {ECO:0000269|PubMed:30228108}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:30228108}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques and seeds.
CC {ECO:0000269|PubMed:30228108}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in developing seeds in siliques,
CC mainly in the seed coat and, to a lesser extent, in the embryo.
CC {ECO:0000269|PubMed:30228108}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction of seed mucilage accumulation
CC and major decrease in rhamnogalacturonan I (RG I), associated with
CC reduced absolute levels of rhamnose (Rha), arabinose (Ara) and
CC galacturonic acid (GalA) but increased absolute abundance of minor
CC sugars (e.g. galactose (Gal), xylose (Xyl), glucose (Glc) and mannose
CC (Man)) (PubMed:30228108). The double mutant muci70-1 gaut11-3 is
CC completely defective in seed mucilage production and exhibits a strong
CC release of minor sugars in total mucilage extracts (PubMed:30228108).
CC Plants missing both MUCI70 and IRX14 exhibit a severe reduction in both
CC xylan- and pectin-related sugars in total seed mucilage extracts
CC (PubMed:30228108). {ECO:0000269|PubMed:30228108}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; KY906044; ARJ31408.1; -; mRNA.
DR EMBL; AC021044; AAF98431.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30935.1; -; Genomic_DNA.
DR EMBL; AY062504; AAL32582.1; -; mRNA.
DR EMBL; BT002091; AAN72102.1; -; mRNA.
DR PIR; E86408; E86408.
DR RefSeq; NP_174145.1; NM_102589.4.
DR AlphaFoldDB; Q9FZ97; -.
DR PaxDb; Q9FZ97; -.
DR PRIDE; Q9FZ97; -.
DR ProteomicsDB; 191694; -.
DR EnsemblPlants; AT1G28240.1; AT1G28240.1; AT1G28240.
DR GeneID; 839718; -.
DR Gramene; AT1G28240.1; AT1G28240.1; AT1G28240.
DR KEGG; ath:AT1G28240; -.
DR Araport; AT1G28240; -.
DR TAIR; locus:2032137; AT1G28240.
DR eggNOG; ENOG502QV59; Eukaryota.
DR HOGENOM; CLU_027685_2_0_1; -.
DR InParanoid; Q9FZ97; -.
DR OMA; IREKTNW; -.
DR OrthoDB; 558859at2759; -.
DR PhylomeDB; Q9FZ97; -.
DR UniPathway; UPA00845; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ97; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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:0016757; F:glycosyltransferase activity; IMP:TAIR.
DR GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:TAIR.
DR GO; GO:0048358; P:mucilage pectin biosynthetic process; IMP:TAIR.
DR GO; GO:0010246; P:rhamnogalacturonan I biosynthetic process; IMP:TAIR.
DR GO; GO:0045491; P:xylan metabolic process; IMP:UniProtKB.
DR InterPro; IPR006852; DUF616.
DR PANTHER; PTHR12956; PTHR12956; 1.
DR Pfam; PF04765; DUF616; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..581
FT /note="Probable hexosyltransferase MUCI70"
FT /id="PRO_0000450758"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..581
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 514..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..569
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 177
FT /note="E -> G (in Ref. 1; ARJ31408 and 4; AAL32582/
FT AAN72102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 65578 MW; 78E72252332F91AC CRC64;
MTGLGVRSSS YGSLEKTGLN GVVLPIQITT TTRTKPSKMQ KDREGIVHWI CKFAGRKKVG
MLLLFLISAV VFLRVLYVGK GEDSQEGQGP PSLHFNGSSG VNYSNMLQTN EELNMNIGNI
SFKAKEVIVF PPPPIHFLGY SLPQGHPCNS FTLPPPPADR KRTGPRPCPV CYLPVEEAVA
LMPNAPSFSP VLKNLTYIYE EPLNRETEFG GSDFGGYPTL KHRNDSFDIK ETMSVHCGFV
KGPQPGRNTG FDIDEADLLE MKQCRGIVVA SAVFDAFDDV KAPQNISKYA EETVCFYMFV
DEETESILKR ERGLDGNKKV GIWRVVVVHN LPYSDGRRNG KVPKLLVHRM FPNARYSLWI
DGKLELVVDP YQILERFLWR KNATFAISRH YKRFDVLVEA EANKAAGKYD NASIDFQVDF
YKNEGLTPYS VAKLPITSDV PEGCVILREH VPISNLFTCL WFNEVDRFTS RDQISFSTVR
DKIAAKTNWT VSMFLDCERR NFVVQRYHRA EQERFARQRP PVPNFPPPPP SPPPPVLISS
DLPRKMSSGR ATPPRRRGRD RRSGQRGHRK ANLPVRLPDS A
