ENL2_ARATH
ID ENL2_ARATH Reviewed; 349 AA.
AC Q9T076; Q5PNT5; Q8LBE5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Early nodulin-like protein 2;
DE AltName: Full=Phytocyanin-like protein;
DE Flags: Precursor;
GN OrderedLocusNames=At4g27520; ORFNames=T29A15.10;
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 MRNA].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND GPI-ANCHOR [LARGE SCALE ANALYSIS].
RX PubMed=14517339; DOI=10.1074/mcp.m300079-mcp200;
RA Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,
RA Jensen O.N.;
RT "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane
RT proteins.";
RL Mol. Cell. Proteomics 2:1261-1270(2003).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF083668; AAN60227.1; -; mRNA.
DR EMBL; AL035602; CAB38264.1; -; Genomic_DNA.
DR EMBL; AL161571; CAB81402.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85353.1; -; Genomic_DNA.
DR EMBL; AF325035; AAG40387.1; -; mRNA.
DR EMBL; BT000767; AAN31906.1; -; mRNA.
DR EMBL; AY087260; AAM64815.1; -; mRNA.
DR EMBL; BT020362; AAV85717.1; -; mRNA.
DR PIR; T05857; T05857.
DR RefSeq; NP_194482.1; NM_118887.3.
DR AlphaFoldDB; Q9T076; -.
DR SMR; Q9T076; -.
DR BioGRID; 14148; 1.
DR STRING; 3702.AT4G27520.1; -.
DR PaxDb; Q9T076; -.
DR PRIDE; Q9T076; -.
DR ProteomicsDB; 220319; -.
DR EnsemblPlants; AT4G27520.1; AT4G27520.1; AT4G27520.
DR GeneID; 828861; -.
DR Gramene; AT4G27520.1; AT4G27520.1; AT4G27520.
DR KEGG; ath:AT4G27520; -.
DR Araport; AT4G27520; -.
DR TAIR; locus:2137672; AT4G27520.
DR eggNOG; ENOG502RZ81; Eukaryota.
DR HOGENOM; CLU_058719_0_0_1; -.
DR InParanoid; Q9T076; -.
DR OMA; APGQKKS; -.
DR OrthoDB; 1220710at2759; -.
DR PRO; PR:Q9T076; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T076; baseline and differential.
DR Genevisible; Q9T076; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd11019; OsENODL1_like; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR041846; ENL_dom.
DR InterPro; IPR039391; Phytocyanin.
DR InterPro; IPR003245; Phytocyanin_dom.
DR PANTHER; PTHR33021; PTHR33021; 2.
DR Pfam; PF02298; Cu_bind_like; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS51485; PHYTOCYANIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..325
FT /note="Early nodulin-like protein 2"
FT /id="PRO_0000002880"
FT PROPEP 326..349
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000002881"
FT DOMAIN 29..130
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT REGION 136..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 325
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 349 AA; 35064 MW; B267C39C52C3AE90 CRC64;
MTFLKMKSLS FFFTILLSLS TLFTISNARK FNVGGSGAWV TNPPENYESW SGKNRFLVHD
TLYFSYAKGA DSVLEVNKAD YDACNTKNPI KRVDDGDSEI SLDRYGPFYF ISGNEDNCKK
GQKLNVVVIS ARIPSTAQSP HAAAPGSSTP GSMTPPGGAH SPKSSSPVSP TTSPPGSTTP
PGGAHSPKSS SAVSPATSPP GSMAPKSGSP VSPTTSPPAP PKSTSPVSPS SAPMTSPPAP
MAPKSSSTIP PSSAPMTSPP GSMAPKSSSP VSNSPTVSPS LAPGGSTSSS PSDSPSGSAM
GPSGDGPSAA GDISTPAGAP GQKKSSANGM TVMSITTVLS LVLTIFLSA
