P24D5_ARATH
ID P24D5_ARATH Reviewed; 216 AA.
AC Q8RWM6; Q9SFE6;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24delta5;
DE AltName: Full=Atp24;
DE AltName: Full=p24 family protein delta1c;
DE Short=p24delta1c;
DE AltName: Full=p24 family protein delta5;
DE Short=p24delta5;
DE Flags: Precursor;
GN OrderedLocusNames=At1g21900; ORFNames=T26F17.12;
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;
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 [4]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 209-TYR-PHE-210 AND
RP 213-LYS-LYS-214.
RX PubMed=18266912; DOI=10.1111/j.1600-0854.2008.00719.x;
RA Langhans M., Marcote M.J., Pimpl P., Virgili-Lopez G., Robinson D.G.,
RA Aniento F.;
RT "In vivo trafficking and localization of p24 proteins in plant cells.";
RL Traffic 9:770-785(2008).
RN [5]
RP GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, INTERACTION WITH P24BETA2,
RP AND FUNCTION.
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). Interacts with p24beta2 at
CC endoplasmic reticulum export sites for endoplasmic reticulum exit and
CC coupled transport to the Golgi apparatus. Once in the Golgi, interacts
CC very efficiently with the COPI machinery for retrograde transport back
CC to the endoplasmic reticulum. {ECO:0000250,
CC ECO:0000269|PubMed:22577184}.
CC -!- SUBUNIT: Probably oligomerizes with other members of the EMP24/GP25L
CC family (By similarity). Associates with the COPI vesicle coat
CC (coatomer) (By similarity). Associates with the COPII vesicle coat
CC (coatomer) (By similarity). Interacts with p24beta2. {ECO:0000250,
CC ECO:0000269|PubMed:22577184}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18266912, ECO:0000269|PubMed:22132757,
CC ECO:0000269|PubMed:22577184}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18266912, ECO:0000269|PubMed:22132757,
CC ECO:0000269|PubMed:22577184}. 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:18266912}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16541.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013482; AAF16541.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30170.1; -; Genomic_DNA.
DR EMBL; AY092996; AAM12995.1; -; mRNA.
DR EMBL; AY114612; AAM47931.1; -; mRNA.
DR PIR; C86352; C86352.
DR RefSeq; NP_173608.1; NM_102038.5.
DR AlphaFoldDB; Q8RWM6; -.
DR SMR; Q8RWM6; -.
DR BioGRID; 24031; 4.
DR STRING; 3702.AT1G21900.1; -.
DR PaxDb; Q8RWM6; -.
DR PRIDE; Q8RWM6; -.
DR ProteomicsDB; 248681; -.
DR EnsemblPlants; AT1G21900.1; AT1G21900.1; AT1G21900.
DR GeneID; 838792; -.
DR Gramene; AT1G21900.1; AT1G21900.1; AT1G21900.
DR KEGG; ath:AT1G21900; -.
DR Araport; AT1G21900; -.
DR TAIR; locus:2201098; AT1G21900.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_2_1; -.
DR InParanoid; Q8RWM6; -.
DR OMA; THHPQAN; -.
DR OrthoDB; 1370889at2759; -.
DR PhylomeDB; Q8RWM6; -.
DR PRO; PR:Q8RWM6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWM6; baseline and differential.
DR Genevisible; Q8RWM6; AT.
DR GO; GO:0005801; C:cis-Golgi network; IDA:TAIR.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..216
FT /note="Transmembrane emp24 domain-containing protein
FT p24delta5"
FT /id="PRO_0000419785"
FT TOPO_DOM 28..183
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..151
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 137..159
FT /evidence="ECO:0000255"
FT MOTIF 209..216
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000250"
FT MOTIF 209..210
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 169
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250"
FT MOD_RES 174
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 209..210
FT /note="YF->AA: Does not affect the subcellular location."
FT /evidence="ECO:0000269|PubMed:18266912"
FT MUTAGEN 213..214
FT /note="KK->SS: Redirection of the subcellular location from
FT the endoplasmic reticulum to the prevacuolar compartment
FT (PVC), the vacuole and the plasma membrane."
FT /evidence="ECO:0000269|PubMed:18266912"
SQ SEQUENCE 216 AA; 24346 MW; 6E0384723C652D3E CRC64;
MAINRIAHGS LFLTVVLFFL TVNYGEAIWL TIPTTGGTKC VSEEIQSNVV VLADYYVVDE
HNPENTPAVS SKVTSPYGNN LHHQENVTHG QFAFTTQEAG NYLACFWIDS SHHLANPITL
GVDWKMGIAA KDWDSVAKKE KIEGVELQLR RLEGLVLSIR ENLNYIKDRE AEMREVSETT
NSRVAWFSIM SLGVCVVVVG SQILYLKRYF HKKKLI
