P24D3_ARATH
ID P24D3_ARATH Reviewed; 217 AA.
AC Q6IDL4;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24delta3;
DE AltName: Full=p24 family protein delta1a;
DE Short=p24delta1a;
DE AltName: Full=p24 family protein delta3;
DE Short=p24delta3;
DE Flags: Precursor;
GN OrderedLocusNames=At1g09580; ORFNames=F14J9.28;
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DOMAIN, MUTAGENESIS OF 210-TYR-PHE-211 AND 214-LYS-LYS-215, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=15653796; DOI=10.1093/pcp/pch200;
RA Contreras I., Yang Y., Robinson D.G., Aniento F.;
RT "Sorting signals in the cytosolic tail of plant p24 proteins involved in
RT the interaction with the COPII coat.";
RL Plant Cell Physiol. 45:1779-1786(2004).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22577184; DOI=10.1093/jxb/ers112;
RA Montesinos J.C., Sturm S., Langhans M., Hillmer S., Marcote M.J.,
RA Robinson D.G., Aniento F.;
RT "Coupled transport of Arabidopsis p24 proteins at the ER-Golgi interface.";
RL J. Exp. Bot. 63:4243-4261(2012).
RN [6]
RP GENE FAMILY, SUBCELLULAR LOCATION, AND COILED-COIL DOMAIN.
RX PubMed=22132757; DOI=10.1111/j.1600-0854.2011.01317.x;
RA Chen J., Qi X., Zheng H.;
RT "Subclass-specific localization and trafficking of Arabidopsis p24 proteins
RT in the ER-Golgi interface.";
RL Traffic 13:400-415(2012).
CC -!- FUNCTION: Involved in vesicular protein trafficking. Mainly functions
CC in the early secretory pathway. Thought to act as cargo receptor at the
CC lumenal side for incorporation of secretory cargo molecules into
CC transport vesicles and to be involved in vesicle coat formation at the
CC cytoplasmic side (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Probably oligomerizes with other members of the EMP24/GP25L
CC family (By similarity). Associates with the COPI vesicle coat
CC (coatomer). Associates with the COPII vesicle coat (coatomer).
CC {ECO:0000250, ECO:0000269|PubMed:15653796}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15653796, ECO:0000269|PubMed:22132757}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:15653796,
CC ECO:0000269|PubMed:22132757}. Note=Cycles between the endoplasmic
CC reticulum and Golgi via COPI and COPII dependent pathways. Mainly
CC located in endoplasmic reticulum.
CC -!- DOMAIN: The cytoplasmic C-terminal domain contains a functional
CC dilysine-retrieval motif, which is involved in the retrograde Golgi-to-
CC ER transport of the protein. {ECO:0000269|PubMed:15653796}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; AC003970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE28465.1; -; Genomic_DNA.
DR EMBL; BT010830; AAR24197.1; -; mRNA.
DR RefSeq; NP_172429.1; NM_100830.5.
DR AlphaFoldDB; Q6IDL4; -.
DR SMR; Q6IDL4; -.
DR BioGRID; 22726; 5.
DR IntAct; Q6IDL4; 4.
DR STRING; 3702.AT1G09580.1; -.
DR PaxDb; Q6IDL4; -.
DR PRIDE; Q6IDL4; -.
DR ProteomicsDB; 248783; -.
DR EnsemblPlants; AT1G09580.1; AT1G09580.1; AT1G09580.
DR GeneID; 837485; -.
DR Gramene; AT1G09580.1; AT1G09580.1; AT1G09580.
DR KEGG; ath:AT1G09580; -.
DR Araport; AT1G09580; -.
DR TAIR; locus:2012335; AT1G09580.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_2_1; -.
DR InParanoid; Q6IDL4; -.
DR OMA; HGVEARN; -.
DR OrthoDB; 1370889at2759; -.
DR PhylomeDB; Q6IDL4; -.
DR PRO; PR:Q6IDL4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6IDL4; baseline and differential.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Glycoprotein;
KW Membrane; Methylation; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..217
FT /note="Transmembrane emp24 domain-containing protein
FT p24delta3"
FT /id="PRO_0000419783"
FT TOPO_DOM 31..184
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..152
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 138..160
FT /evidence="ECO:0000255"
FT MOTIF 210..217
FT /note="COPI vesicle coat-binding"
FT MOTIF 210..211
FT /note="COPII vesicle coat-binding"
FT MOD_RES 170
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250"
FT MOD_RES 175
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 210..211
FT /note="YF->AA: Disrupts association with COPII vesicle
FT coat. Slightly reduces association with COPI vesicle coat."
FT /evidence="ECO:0000269|PubMed:15653796"
FT MUTAGEN 214..215
FT /note="KK->SS: Disrupts association with COPI vesicle coat
FT but favors association with COPII vesicle coat."
FT /evidence="ECO:0000269|PubMed:15653796"
SQ SEQUENCE 217 AA; 24607 MW; 918551FBD64328DC CRC64;
MKMTAKMRRE FPTAFLLLFL VPVMIPVGEA VWLDVPPTGT KCVSEEIQSN VVVLADYLII
SEDHEVMPTI SVKVTSPYGN NLHNMENVTH GQFAFTTQES GNYLACFWAD EKSHGNKNVS
INIDWRTGIA AKDWASIAKK EKIEGVELEI RKLEGAVEAI HENILYLRNR EADMRTMSEK
TNSRVAWYSI MSLGVCIAVS GFQVLYLKQY FEKKKLI
