PLM_ARATH
ID PLM_ARATH Reviewed; 421 AA.
AC Q9XIG2; C0Z2F1; Q56YW4; Q8LD82;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein PHLOEM UNLOADING MODULATOR {ECO:0000303|PubMed:31182845};
DE EC=2.7.8.- {ECO:0000269|PubMed:31182845};
GN Name=PLM {ECO:0000303|PubMed:31182845};
GN OrderedLocusNames=At1g43580 {ECO:0000312|Araport:AT1G43580};
GN ORFNames=T10P12.6 {ECO:0000312|EMBL:AAD39274.1};
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] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 190-421.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP REVIEW ON SPHINGOLIPIDS.
RX PubMed=23499054; DOI=10.1016/j.pbi.2013.02.009;
RA Markham J.E., Lynch D.V., Napier J.A., Dunn T.M., Cahoon E.B.;
RT "Plant sphingolipids: function follows form.";
RL Curr. Opin. Plant Biol. 16:350-357(2013).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=31182845; DOI=10.1038/s41477-019-0429-5;
RA Yan D., Yadav S.R., Paterlini A., Nicolas W.J., Petit J.D., Brocard L.,
RA Belevich I., Grison M.S., Vaten A., Karami L., El-Showk S., Lee J.Y.,
RA Murawska G.M., Mortimer J., Knoblauch M., Jokitalo E., Markham J.E.,
RA Bayer E.M., Helariutta Y.;
RT "Sphingolipid biosynthesis modulates plasmodesmal ultrastructure and phloem
RT unloading.";
RL Nat. Plants 5:604-615(2019).
RN [9]
RP REVIEW.
RX PubMed=32407692; DOI=10.1016/j.tplants.2020.03.007;
RA Mortimer J.C., Scheller H.V.;
RT "Synthesis and function of complex sphingolipid glycosylation.";
RL Trends Plant Sci. 25:522-524(2020).
CC -!- FUNCTION: Catalyzes the biosynthesis of sphingolipids with very long-
CC chain fatty acid (VLCFA) (PubMed:31182845). Required for the formation
CC of plasmodesmal cytoplasmic sleeve during the transition from type I to
CC type II plasmodesmata to modulate post-sieve elements (SE) unloading
CC and symplastic cell-to-cell molecular trafficking at the phloem pole
CC pericycle (PPP)-endodermis interface in roots (PubMed:31182845).
CC {ECO:0000269|PubMed:31182845}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:31182845}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XIG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XIG2-2; Sequence=VSP_060914;
CC -!- DISRUPTION PHENOTYPE: Enhanced plasmodesmata-mediated symplastic
CC transport through the phloem pole pericycle (PPP)-endodermis interface
CC due to a defect in the formation of the endoplasmic reticulum (ER)-
CC plasma membrane tethers during plasmodesmal morphogenesis and
CC associated with pores lacking cytoplasmic sleeve.
CC {ECO:0000269|PubMed:31182845}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; AC007203; AAD39274.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31971.1; -; Genomic_DNA.
DR EMBL; AY090374; AAL91277.1; -; mRNA.
DR EMBL; AK318765; BAH56880.1; -; mRNA.
DR EMBL; AY086152; AAM63357.1; -; mRNA.
DR EMBL; AK221206; BAD93747.1; -; mRNA.
DR PIR; C96499; C96499.
DR RefSeq; NP_564484.1; NM_103483.3. [Q9XIG2-1]
DR AlphaFoldDB; Q9XIG2; -.
DR STRING; 3702.AT1G43580.1; -.
DR PaxDb; Q9XIG2; -.
DR PRIDE; Q9XIG2; -.
DR ProteomicsDB; 187975; -.
DR EnsemblPlants; AT1G43580.1; AT1G43580.1; AT1G43580. [Q9XIG2-1]
DR GeneID; 840942; -.
DR Gramene; AT1G43580.1; AT1G43580.1; AT1G43580. [Q9XIG2-1]
DR KEGG; ath:AT1G43580; -.
DR Araport; AT1G43580; -.
DR TAIR; locus:2194671; AT1G43580.
DR eggNOG; KOG3058; Eukaryota.
DR HOGENOM; CLU_055733_0_0_1; -.
DR InParanoid; Q9XIG2; -.
DR OMA; RTMTFVA; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q9XIG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIG2; baseline and differential.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; IBA:GO_Central.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009663; P:plasmodesma organization; IMP:UniProtKB.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IMP:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..421
FT /note="Protein PHLOEM UNLOADING MODULATOR"
FT /id="PRO_0000452150"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 94..376
FT /note="Missing (in isoform 2)"
FT /id="VSP_060914"
FT CONFLICT 15
FT /note="V -> A (in Ref. 5; AAM63357)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="M -> I (in Ref. 5; AAM63357)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="S -> N (in Ref. 5; AAM63357)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> T (in Ref. 5; AAM63357)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="S -> N (in Ref. 5; AAM63357)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="S -> P (in Ref. 5; AAM63357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47120 MW; E4617CD916688D1B CRC64;
MTKGGLGIAA MSYVVIDYMR YVSPVWHSRL MPVLWSVLAI AVVTRVLFYK HWSKELRAAI
PFLGSIVFLL CALLFEALCV RSVTAVLGLD WHRETPPLPD TGQWFLLALN ESLPGTLVEI
LRAHIIGLHH FLMLFIMLGF SVVFDSVKAP GLGLGARYIF TMGVGRLLRA ITFVSTILPS
ARPWCASARF NNVPSQPHRW AQKYYVPYAN DPAAIRKLLH WDAAYADPGS YIGDYRADWG
SMSFLSEFLR PSYSEGSSWF ALLKKAGGGC NDLMYSGHML VAVLTAMAWT EAYGGFSSAM
IWLFVAHSAQ REIRERHHYT VDCIVAIYVG ILLWKMTGFI WSAERKTKQT KLEKIQNSLI
HAAKDGDIET VRRLVEEIEV SSRVEKQSKV ISNRTMTVFA CATVITTLTI VILALTLTSD
G
