EVN_ARATH
ID EVN_ARATH Reviewed; 569 AA.
AC F4J4C8; Q8VXX8; Q9LXH2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Dolichol kinase EVAN {ECO:0000303|PubMed:25919390};
DE EC=2.7.1.108;
GN Name=EVN {ECO:0000303|PubMed:25919390};
GN OrderedLocusNames=At3g45040 {ECO:0000312|EMBL:AEE77982.1};
GN ORFNames=F14D17.110 {ECO:0000312|EMBL:CAB89319.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25919390; DOI=10.1371/journal.pbio.1002139;
RA Lindner H., Kessler S.A., Mueller L.M., Shimosato-Asano H.,
RA Boisson-Dernier A., Grossniklaus U.;
RT "TURAN and EVAN mediate pollen tube reception in Arabidopsis Synergids
RT through protein glycosylation.";
RL PLoS Biol. 13:E1002139-E1002139(2015).
CC -!- FUNCTION: Essential for pollen development. Involved in protein N-
CC glycosylation in the endoplasmic reticulum (ER), especially in the
CC female gametophyte. Mediates pollen tube (PT) reception in synergids
CC through protein glycosylation. {ECO:0000269|PubMed:25919390}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP
CC + H(+); Xref=Rhea:RHEA:13133, Rhea:RHEA-COMP:9517, Rhea:RHEA-
CC COMP:9521, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58069; EC=2.7.1.108;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25919390}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Pollen tube (PT) overgrowth inside the female
CC gametophyte (FG) without PT rupture. Degenerated pollen grains before
CC maturation, during the early tricellular stage.
CC {ECO:0000269|PubMed:25919390}.
CC -!- SIMILARITY: Belongs to the polyprenol kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB89319.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353992; CAB89319.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77982.1; -; Genomic_DNA.
DR EMBL; AY074371; AAL67067.1; -; mRNA.
DR PIR; T48980; T48980.
DR RefSeq; NP_190090.2; NM_114373.4.
DR AlphaFoldDB; F4J4C8; -.
DR STRING; 3702.AT3G45040.1; -.
DR iPTMnet; F4J4C8; -.
DR PaxDb; F4J4C8; -.
DR EnsemblPlants; AT3G45040.1; AT3G45040.1; AT3G45040.
DR GeneID; 823639; -.
DR Gramene; AT3G45040.1; AT3G45040.1; AT3G45040.
DR KEGG; ath:AT3G45040; -.
DR Araport; AT3G45040; -.
DR TAIR; locus:2075959; AT3G45040.
DR eggNOG; KOG2468; Eukaryota.
DR HOGENOM; CLU_027611_1_0_1; -.
DR InParanoid; F4J4C8; -.
DR OrthoDB; 1533260at2759; -.
DR BRENDA; 2.7.1.108; 399.
DR PRO; PR:F4J4C8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J4C8; baseline and differential.
DR Genevisible; F4J4C8; AT.
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:0004168; F:dolichol kinase activity; ISS:TAIR.
DR GO; GO:0043048; P:dolichyl monophosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0010483; P:pollen tube reception; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IMP:TAIR.
DR InterPro; IPR026566; DOLK.
DR InterPro; IPR032974; Polypren_kinase.
DR PANTHER; PTHR13205; PTHR13205; 1.
DR PANTHER; PTHR13205:SF19; PTHR13205:SF19; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Kinase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..569
FT /note="Dolichol kinase EVAN"
FT /id="PRO_0000433635"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..67
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..147
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..207
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..296
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..369
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..440
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..508
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 487..503
FT /note="CTP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ8"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 411
FT /note="I -> V (in Ref. 3; AAL67067)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="P -> T (in Ref. 3; AAL67067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 63136 MW; 191B51C3CEB49395 CRC64;
MKTTATSFVT GERVVVFVVV SRILLSLPLS LISHGFSLFL LSLSAFLVEI RVETSPFLLS
HFSSRRGASS GILLGAVTLP SVMISKLVQL SRAISIHEAE QDELAHVTMQ YWAASASCCA
ILIYLSVIMS QVRKDESLSS SSIWLTRVSL TGTVLYGVAC FVSLSMISHT GLNTSLKMLW
MLFHGLAAVK LIRHLLCTFP SCASIGEALL VTSGLVLYFG DFLACTIAKI FEKLIPVDLV
SISYGIKRTE TGIIVQGLLL GLLLFPMVFR FVLHIYESSL RKRDARQRNC SDAAKSVLFF
VSLLFFMVVA VPSWMQFVHD FNQHPFLWVL TFVFSEPLKR LSLCIYWILL IVVSVSRFYN
ISRSSKVERI LLRKYYHLMA VLMFLPALVL QPKFLDLAFG AALAVFVALE IIRIWRIQPL
GEPLHQFMNA FTDHRDSEHL IVSHFSLLLG CALPIWMSSG FNDRALSPFA GILSLGIGDT
MASMVGHKYG VLRWSKTGKK TVEGTAAGIT SMMAVCFVLV PILASMGYIL SQGWWSLLVA
VTATGMLEAY TAQLDNAFIP LVFYSLLCL
