ALG12_ARATH
ID ALG12_ARATH Reviewed; 497 AA.
AC A8MR93; F4HVW9; F4HVX0; Q0WT37; Q1G329; Q1G330;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
DE EC=2.4.1.260;
DE AltName: Full=Alpha-1,6-mannosyltransferase ALG12;
DE AltName: Full=Asparagine-linked glycosylation protein 12;
DE AltName: Full=EMS-mutagenized BRI1 suppressor 4;
GN Name=ALG12; Synonyms=EBS4; OrderedLocusNames=At1g02145; ORFNames=T6A9;
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=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 [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] (ISOFORMS 2 AND 4).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF GLU-38 AND SER-307.
RX PubMed=20023196; DOI=10.1105/tpc.109.070284;
RA Hong Z., Jin H., Fitchette A.C., Xia Y., Monk A.M., Faye L., Li J.;
RT "Mutations of an alpha1,6 mannosyltransferase inhibit endoplasmic
RT reticulum-associated degradation of defective brassinosteroid receptors in
RT Arabidopsis.";
RL Plant Cell 21:3792-3802(2009).
CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Adds the
CC eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-
CC oligosaccharide precursor dolichol-PP-Man(7)GlcNAc(2).
CC {ECO:0000269|PubMed:20023196}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate +
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260;
CC Evidence={ECO:0000269|PubMed:20023196};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=A8MR93-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MR93-2; Sequence=VSP_041716, VSP_041718;
CC Name=3;
CC IsoId=A8MR93-3; Sequence=VSP_041715;
CC Name=4;
CC IsoId=A8MR93-4; Sequence=VSP_041716, VSP_041717;
CC Name=5;
CC IsoId=A8MR93-5; Sequence=VSP_041717;
CC Name=6;
CC IsoId=A8MR93-6; Sequence=VSP_041716;
CC -!- MISCELLANEOUS: In the absence of ALG12 activity, the N-glycans
CC transferred to proteins are aberrant, indicating that the
CC oligosaccharyltransferase (OST) complex is substrate-tolerant.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000305}.
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DR EMBL; AC064879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE27389.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27390.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27391.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27392.1; -; Genomic_DNA.
DR EMBL; DQ492198; ABF59127.1; -; mRNA.
DR EMBL; DQ492199; ABF59128.1; -; mRNA.
DR EMBL; AK227725; BAE99711.1; -; mRNA.
DR RefSeq; NP_001077446.1; NM_001083977.4. [A8MR93-5]
DR RefSeq; NP_001077447.2; NM_001083978.2. [A8MR93-2]
DR RefSeq; NP_001077448.1; NM_001083979.2. [A8MR93-1]
DR RefSeq; NP_001117214.1; NM_001123742.1. [A8MR93-6]
DR AlphaFoldDB; A8MR93; -.
DR STRING; 3702.AT1G02145.3; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR PaxDb; A8MR93; -.
DR PRIDE; A8MR93; -.
DR ProteomicsDB; 244895; -. [A8MR93-1]
DR EnsemblPlants; AT1G02145.1; AT1G02145.1; AT1G02145. [A8MR93-5]
DR EnsemblPlants; AT1G02145.2; AT1G02145.2; AT1G02145. [A8MR93-2]
DR EnsemblPlants; AT1G02145.3; AT1G02145.3; AT1G02145. [A8MR93-1]
DR EnsemblPlants; AT1G02145.4; AT1G02145.4; AT1G02145. [A8MR93-6]
DR GeneID; 5007658; -.
DR Gramene; AT1G02145.1; AT1G02145.1; AT1G02145. [A8MR93-5]
DR Gramene; AT1G02145.2; AT1G02145.2; AT1G02145. [A8MR93-2]
DR Gramene; AT1G02145.3; AT1G02145.3; AT1G02145. [A8MR93-1]
DR Gramene; AT1G02145.4; AT1G02145.4; AT1G02145. [A8MR93-6]
DR KEGG; ath:AT1G02145; -.
DR Araport; AT1G02145; -.
DR TAIR; locus:4010713407; AT1G02145.
DR eggNOG; KOG2516; Eukaryota.
DR HOGENOM; CLU_008917_0_0_1; -.
DR InParanoid; A8MR93; -.
DR OMA; FTQYDHH; -.
DR PhylomeDB; A8MR93; -.
DR BRENDA; 2.4.1.260; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:A8MR93; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A8MR93; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:TAIR.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:TAIR.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..497
FT /note="Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-
FT mannosyltransferase"
FT /id="PRO_0000412586"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..322
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_041715"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:17147637"
FT /id="VSP_041716"
FT VAR_SEQ 71..74
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:17147637"
FT /id="VSP_041717"
FT VAR_SEQ 260..380
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17147637"
FT /id="VSP_041718"
FT MUTAGEN 38
FT /note="E->K: In ebs4-3; incomplete assembly of glycans and
FT compromised endoplasmic reticulum-associated degradation
FT (ERAD) of defective proteins."
FT /evidence="ECO:0000269|PubMed:20023196"
FT MUTAGEN 307
FT /note="S->P: In ebs4-2; incomplete assembly of glycans and
FT compromised endoplasmic reticulum-associated degradation
FT (ERAD) of defective proteins."
FT /evidence="ECO:0000269|PubMed:20023196"
SQ SEQUENCE 497 AA; 57192 MW; 7A37B1757AA8BF88 CRC64;
MPTDSKMAKF LQSYGYDLIL GSVAAIYVVM APYTKVEESF NVQSMHDILY HRHHLDSYDH
LEFPGVVPRT FIGAFIVSVF ASPVVSIISC LGFPKVYSLV AARLVLGCII LSTLRFFRIQ
IKKKFGNQVE TFFVLFTSLQ FHFLFYCTRP LPNILALGLV NLAYGNWLKG NFYPALSFLI
FATVIFRCDT MLLLGPIGLE LLLTKSISFW KALKYCVGTA LLAVGLTIFV DSIMWKKFVW
PEFEVFWFNS ILNRSSDWGT HSIHWYFTSA LPRSLLVAYP LSLLGTLVDR RVPFFIVPVL
SFVILYSKLP HKELRFIISS VPMFNLSAAV AASRIYNNRK KTIWKLVNMV MLAFFAISAG
CTVVTFMASY YNYPSGYALK RLHQIGHPAN VAGEEWVHID TFGAMNGISR FCEDDFPWRY
SKEEEIVVEE LRNRNFTYLV NEHSSVDGYK CLFYEEGFER LELRRGFPPI VLVKKAKVYL
HREMKKEDPF HKKWPGC
