DPM3_ARATH
ID DPM3_ARATH Reviewed; 89 AA.
AC Q8LEQ4; Q9LNG6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dolichol-phosphate mannose synthase subunit 3 {ECO:0000305};
DE Short=DPM synthase subunit 3 {ECO:0000305};
DE AltName: Full=Dol-P-Man synthase1 {ECO:0000303|PubMed:21558543};
DE AltName: Full=Dolichol phosphate-mannose biosynthesis regulatory protein {ECO:0000305};
GN Name=DPMS3 {ECO:0000303|PubMed:21558543};
GN OrderedLocusNames=At1g48140 {ECO:0000312|Araport:AT1G48140};
GN ORFNames=F21D18.14 {ECO:0000312|EMBL:AAF79537.1};
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 [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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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].
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 [6]
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: Regulates the biosynthesis of dolichol phosphate-mannose.
CC Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase
CC complex; essential for the ER localization and stable expression of
CC DPMS1. {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 DPMS1 and DPMS2. {ECO:0000269|PubMed:21558543}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21558543}; Multi-pass membrane protein
CC {ECO:0000255}. Note=May serve as regulatory subunit and membrane anchor
CC for DPMS1. {ECO:0000269|PubMed:21558543}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:21558543}.
CC -!- SIMILARITY: Belongs to the DPM3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79537.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC023673; AAF79537.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32253.1; -; Genomic_DNA.
DR EMBL; AK118069; BAC42700.1; -; mRNA.
DR EMBL; BT005626; AAO64046.1; -; mRNA.
DR EMBL; AY085296; AAM62528.1; -; mRNA.
DR PIR; E96521; E96521.
DR RefSeq; NP_564521.1; NM_103710.3.
DR AlphaFoldDB; Q8LEQ4; -.
DR IntAct; Q8LEQ4; 4.
DR STRING; 3702.AT1G48140.1; -.
DR PaxDb; Q8LEQ4; -.
DR PRIDE; Q8LEQ4; -.
DR EnsemblPlants; AT1G48140.1; AT1G48140.1; AT1G48140.
DR GeneID; 841232; -.
DR Gramene; AT1G48140.1; AT1G48140.1; AT1G48140.
DR KEGG; ath:AT1G48140; -.
DR Araport; AT1G48140; -.
DR TAIR; locus:2023762; AT1G48140.
DR eggNOG; ENOG502S473; Eukaryota.
DR HOGENOM; CLU_170636_0_0_1; -.
DR InParanoid; Q8LEQ4; -.
DR OMA; IPQSHTW; -.
DR OrthoDB; 1612544at2759; -.
DR PhylomeDB; Q8LEQ4; -.
DR BioCyc; ARA:AT1G48140-MON; -.
DR BioCyc; MetaCyc:AT1G48140-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8LEQ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LEQ4; 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:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR GO; GO:0097502; P:mannosylation; IEA:GOC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013174; DPM3.
DR PANTHER; PTHR16433; PTHR16433; 1.
DR Pfam; PF08285; DPM3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..89
FT /note="Dolichol-phosphate mannose synthase subunit 3"
FT /id="PRO_0000440171"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 89 AA; 9811 MW; 72C1165F44763B13 CRC64;
MKHIVKILSL LVAISAFWIG LLQAAIIPRS HTWLLPIYFV VSLGCYGLLM VGVGLMQFPT
CPQEAVLLQK DIAEAKDFFK HKGVDVGSN
