P24DB_ARATH
ID P24DB_ARATH Reviewed; 225 AA.
AC Q9LJV9;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24delta11;
DE AltName: Full=p24 family protein delta11;
DE Short=p24delta11;
DE AltName: Full=p24 family protein delta2e;
DE Short=p24delta2e;
DE Flags: Precursor;
GN OrderedLocusNames=At3g29070; ORFNames=MRI12.5;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [4]
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. Associates with the COPI vesicle coat (coatomer). Associates
CC with the COPII vesicle coat (coatomer). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22132757}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:22132757}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000269|PubMed:22132757}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:22132757}. Golgi apparatus, Golgi stack
CC membrane {ECO:0000269|PubMed:22132757}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:22132757}. Note=Cycles between the
CC endoplasmic reticulum and Golgi via COPI and COPII dependent pathways.
CC {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; AP000388; BAB02949.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77531.1; -; Genomic_DNA.
DR RefSeq; NP_189550.2; NM_113829.3.
DR AlphaFoldDB; Q9LJV9; -.
DR SMR; Q9LJV9; -.
DR BioGRID; 7880; 1.
DR STRING; 3702.AT3G29070.1; -.
DR PaxDb; Q9LJV9; -.
DR PRIDE; Q9LJV9; -.
DR ProteomicsDB; 248787; -.
DR EnsemblPlants; AT3G29070.1; AT3G29070.1; AT3G29070.
DR GeneID; 822551; -.
DR Gramene; AT3G29070.1; AT3G29070.1; AT3G29070.
DR KEGG; ath:AT3G29070; -.
DR Araport; AT3G29070; -.
DR TAIR; locus:2092788; AT3G29070.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_2_1; -.
DR InParanoid; Q9LJV9; -.
DR OMA; VELEWRT; -.
DR OrthoDB; 1370889at2759; -.
DR PhylomeDB; Q9LJV9; -.
DR PRO; PR:Q9LJV9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJV9; baseline and differential.
DR Genevisible; Q9LJV9; AT.
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:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Glycoprotein;
KW Golgi apparatus; Membrane; Methylation; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..225
FT /note="Transmembrane emp24 domain-containing protein
FT p24delta11"
FT /id="PRO_0000419791"
FT TOPO_DOM 36..193
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..160
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 175..188
FT /evidence="ECO:0000255"
FT MOTIF 218..225
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000250"
FT MOTIF 218..219
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 178
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 225 AA; 25970 MW; D789D4AE0B56EB9F CRC64;
MDLLPSRYKI HKTKLRWILT MMTMMMMMVM RRGESMRLDM ESGNTKCISD DIKTNYMTVG
TYSIVNPNEG HHLPPSHKLF VTVSSPKGKS HHHAENVESG KFVFTAEETG DYMTCFVAPG
YRPTAKFAVD FEWKSGVEAK DWTTIAKRGQ ITMLEVEVRK LLDVTETIHE EMFQLIERER
EMQELNRSTN SRMAALSLLS FVVTMSVAGL QLRHLKSFLE RKKLL
