P24D6_ARATH
ID P24D6_ARATH Reviewed; 217 AA.
AC F4J4Y0; Q9SG84;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24delta6;
DE AltName: Full=p24 family protein delta1d;
DE Short=p24delta1d;
DE AltName: Full=p24 family protein delta6;
DE Short=p24delta6;
DE Flags: Precursor;
GN OrderedLocusNames=At3g10780; ORFNames=T7M13.14;
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=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 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, MUTAGENESIS OF TYR-210, AND COILED-COIL
RP 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}. Note=Cycles between the endoplasmic
CC reticulum and Golgi via COPI and COPII dependent pathways (By
CC similarity). Mainly located in endoplasmic reticulum. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011708; AAF19571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74954.1; -; Genomic_DNA.
DR RefSeq; NP_187689.2; NM_111915.3.
DR AlphaFoldDB; F4J4Y0; -.
DR SMR; F4J4Y0; -.
DR STRING; 3702.AT3G10780.1; -.
DR PaxDb; F4J4Y0; -.
DR PRIDE; F4J4Y0; -.
DR ProteomicsDB; 248785; -.
DR EnsemblPlants; AT3G10780.1; AT3G10780.1; AT3G10780.
DR GeneID; 820247; -.
DR Gramene; AT3G10780.1; AT3G10780.1; AT3G10780.
DR KEGG; ath:AT3G10780; -.
DR Araport; AT3G10780; -.
DR TAIR; locus:2103222; AT3G10780.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_2_1; -.
DR InParanoid; F4J4Y0; -.
DR OMA; RIREAYM; -.
DR OrthoDB; 1370889at2759; -.
DR PRO; PR:F4J4Y0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J4Y0; baseline and differential.
DR Genevisible; F4J4Y0; 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: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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..217
FT /note="Transmembrane emp24 domain-containing protein
FT p24delta6"
FT /id="PRO_0000419786"
FT TOPO_DOM 27..186
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..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 /evidence="ECO:0000250"
FT MOTIF 210..211
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000250"
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 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 210
FT /note="Y->F: Does not affect the subcellular location."
FT /evidence="ECO:0000269|PubMed:22132757"
SQ SEQUENCE 217 AA; 24230 MW; 50E4551419456984 CRC64;
MAISPVLFIG LIYLAGGGSL FPGVEAIWLT VPESGERCVY EEIQANVVVV LDYICIDDAF
TQLGPTLDVR VTSPYGKELY KIANVTHGQA AFTTSESGTF LACLAMHHDQ SHHSVNSSVI
VSLDWKMGIR AKDWDSVAKK EKIEGVELEI RRSTEYASAI RANILYLRIR EAYMREINEK
TNTRVNQLGL MSLGVAIVVS ISQVLYLKRY FLKKKLI
