P24D8_ARATH
ID P24D8_ARATH Reviewed; 213 AA.
AC O81045; Q6AWV0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24delta8;
DE AltName: Full=p24 family protein delta2b;
DE Short=p24delta2b;
DE AltName: Full=p24 family protein delta8;
DE Short=p24delta8;
DE Flags: Precursor;
GN OrderedLocusNames=At2g03290; ORFNames=T18E12.3, T4M8.28;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 36-213.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH ARF1 AND COATOMER, DOMAIN, MUTAGENESIS OF 206-PHE-PHE-207
RP AND 210-LYS-LYS-211, AND FUNCTION.
RX PubMed=15125774; DOI=10.1111/j.1365-313x.2004.02075.x;
RA Contreras I., Ortiz-Zapater E., Aniento F.;
RT "Sorting signals in the cytosolic tail of membrane proteins involved in the
RT interaction with plant ARF1 and coatomer.";
RL Plant J. 38:685-698(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). On Golgi membranes, acts as primary
CC receptor for ARF1-GDP which is involved in COPI-vesicle formation.
CC {ECO:0000250, ECO:0000269|PubMed:15125774}.
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 Interacts with ARF1 (GDP-bound). {ECO:0000250,
CC ECO:0000269|PubMed:15125774}.
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 -!- 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:15125774}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT85744.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005313; AAM15035.1; -; Genomic_DNA.
DR EMBL; AC006284; AAD17445.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05684.1; -; Genomic_DNA.
DR EMBL; BT015148; AAT85744.1; ALT_INIT; mRNA.
DR EMBL; BT015664; AAU15163.1; -; mRNA.
DR PIR; T02697; T02697.
DR RefSeq; NP_178428.3; NM_126380.5.
DR AlphaFoldDB; O81045; -.
DR SMR; O81045; -.
DR STRING; 3702.AT2G03290.1; -.
DR PaxDb; O81045; -.
DR PRIDE; O81045; -.
DR ProteomicsDB; 248683; -.
DR EnsemblPlants; AT2G03290.1; AT2G03290.1; AT2G03290.
DR GeneID; 814858; -.
DR Gramene; AT2G03290.1; AT2G03290.1; AT2G03290.
DR KEGG; ath:AT2G03290; -.
DR Araport; AT2G03290; -.
DR TAIR; locus:2056976; AT2G03290.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_2_1; -.
DR InParanoid; O81045; -.
DR OMA; VMMEYQV; -.
DR OrthoDB; 1294924at2759; -.
DR PhylomeDB; O81045; -.
DR PRO; PR:O81045; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81045; baseline and differential.
DR Genevisible; O81045; 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 1: Evidence at protein 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..213
FT /note="Transmembrane emp24 domain-containing protein
FT p24delta8"
FT /id="PRO_0000419788"
FT TOPO_DOM 23..180
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..148
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 202..213
FT /note="Interaction with ARF1"
FT /evidence="ECO:0000250"
FT COILED 163..176
FT /evidence="ECO:0000255"
FT MOTIF 206..213
FT /note="COPI vesicle coat-binding"
FT MOTIF 206..207
FT /note="COPII vesicle coat-binding"
FT MOD_RES 166
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 206..207
FT /note="FF->AA: Slightly reduces association with COPI
FT vesicle coat and interaction with ARF1."
FT /evidence="ECO:0000269|PubMed:15125774"
FT MUTAGEN 210..211
FT /note="KK->SS: Disrupts association with COPI vesicle coat
FT and interaction with ARF1."
FT /evidence="ECO:0000269|PubMed:15125774"
SQ SEQUENCE 213 AA; 24565 MW; A02797B7F9E6D42A CRC64;
MDLCRSSILL LIIALLSPRT LSMRYELKSS KTKCIGEEIH ENAMSIGKYF IVNPNEDNHP
LPDSHKIIVK VMPPQGKNLH EADKVEAGQF SFTAYENGSY VACITAIDYK PETTLTIDFD
WKTGVHSKEW TNVAKKSQVD MMEYQVKTLM DTVISIHEEM YYLREREEEM QELNRSTNSK
MAWLSFGSLV VCLSVAGLQF WHLKTFFEKK KLI
