DPM1_ARATH
ID DPM1_ARATH Reviewed; 246 AA.
AC Q9LM93; Q8LDI9;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1 {ECO:0000305};
DE EC=2.4.1.83 {ECO:0000269|PubMed:21558543};
DE AltName: Full=Dol-P-Man synthase1 {ECO:0000303|PubMed:21558543};
DE AltName: Full=Dolichol-phosphate mannose synthase subunit 1 {ECO:0000305};
DE Short=DPM synthase subunit 1 {ECO:0000305};
GN Name=DPMS1 {ECO:0000303|PubMed:21558543};
GN OrderedLocusNames=At1g20575 {ECO:0000312|Araport:AT1G20575};
GN ORFNames=F2D10.6 {ECO:0000312|EMBL:AAF80640.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21558543; DOI=10.1105/tpc.111.083634;
RA Jadid N., Mialoundama A.S., Heintz D., Ayoub D., Erhardt M., Mutterer J.,
RA Meyer D., Alioua A., Van Dorsselaer A., Rahier A., Camara B., Bouvier F.;
RT "DOLICHOL PHOSPHATE MANNOSE SYNTHASE1 mediates the biogenesis of isoprenyl-
RT linked glycans and influences development, stress response, and ammonium
RT hypersensitivity in Arabidopsis.";
RL Plant Cell 23:1985-2005(2011).
CC -!- FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate
CC to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl
CC donor in pathways leading to N-glycosylation, glycosyl
CC phosphatidylinositol membrane anchoring, and O-mannosylation of
CC proteins; catalytic subunit of the dolichol-phosphate mannose (DPM)
CC synthase complex. Plays a role in plant development and physiology,
CC sensitivity to ammonium stress and endoplasmic reticulum stress
CC response. {ECO:0000269|PubMed:21558543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83;
CC Evidence={ECO:0000269|PubMed:21558543};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase
CC complex composed of DPMS1, DPMS2 and DPMS3; in the complex interacts
CC directly with DPMS3. {ECO:0000269|PubMed:21558543}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21558543}; Peripheral membrane protein
CC {ECO:0000305|PubMed:21558543}. Note=Anchored to the ER membrane by
CC DPMS2 and DPMS3 of the dolichol-phosphate mannose (DPM) synthase
CC complex. {ECO:0000305|PubMed:21558543}.
CC -!- DISRUPTION PHENOTYPE: Reduced root growth. Slight reduction of
CC chlorophyll content. Wrinkled seed coat. Hypersensitivity to ammonium.
CC {ECO:0000269|PubMed:21558543}.
CC -!- MISCELLANEOUS: Plants over-expressing DPMS1 show altered stem branch
CC diameter and morphology, perturbation of the vascular bundle
CC arrangements, wrinkled seed coat and constitutive endoplasmic reticulum
CC stress response. {ECO:0000269|PubMed:21558543}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63196.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KJ138997; AHL38937.1; -; mRNA.
DR EMBL; AC069251; AAF80640.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29989.1; -; Genomic_DNA.
DR EMBL; BT005875; AAO64810.1; -; mRNA.
DR EMBL; AK175559; BAD43322.1; -; mRNA.
DR EMBL; AK227450; BAE99453.1; -; mRNA.
DR EMBL; AY085986; AAM63196.1; ALT_INIT; mRNA.
DR PIR; H86338; H86338.
DR RefSeq; NP_564118.1; NM_101908.4.
DR AlphaFoldDB; Q9LM93; -.
DR SMR; Q9LM93; -.
DR STRING; 3702.AT1G20575.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9LM93; -.
DR PRIDE; Q9LM93; -.
DR ProteomicsDB; 220398; -.
DR EnsemblPlants; AT1G20575.1; AT1G20575.1; AT1G20575.
DR GeneID; 838646; -.
DR Gramene; AT1G20575.1; AT1G20575.1; AT1G20575.
DR KEGG; ath:AT1G20575; -.
DR Araport; AT1G20575; -.
DR TAIR; locus:505006134; AT1G20575.
DR eggNOG; KOG2978; Eukaryota.
DR HOGENOM; CLU_033536_13_3_1; -.
DR OMA; TAYIHGF; -.
DR OrthoDB; 1445102at2759; -.
DR PhylomeDB; Q9LM93; -.
DR BioCyc; ARA:AT1G20575-MON; -.
DR BioCyc; MetaCyc:AT1G20575-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9LM93; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LM93; baseline and differential.
DR GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; IPI:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
DR GO; GO:0060359; P:response to ammonium ion; IMP:TAIR.
DR CDD; cd06442; DPM1_like; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398; PTHR43398; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..246
FT /note="Dolichol-phosphate mannosyltransferase subunit 1"
FT /id="PRO_0000440169"
FT CONFLICT 22
FT /note="Y -> F (in Ref. 6; AAM63196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 27676 MW; 3EE65927B87B8A9C CRC64;
MADEMETKGE KKYKYSIIIP TYNERLNIAI IVYLIFKHLR DVDFEIIVVD DGSPDGTQEI
VKQLQQLYGE DRILLRARAK KLGLGTAYIH GLKHATGDFV VIMDADLSHH PKYLPSFIKK
QLETNASIVT GTRYVKGGGV HGWNLMRKLT SRGANVLAQT LLWPGVSDLT GSFRLYKKSA
LEDVISSCVS KGYVFQMEMI VRATRKGYHI EEVPITFVDR VFGTSKLGGS EIVEYLKGLV
YLLLTT
