P24DA_ARATH
ID P24DA_ARATH Reviewed; 214 AA.
AC Q8VY92; Q9C791;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24delta10;
DE AltName: Full=p24 family protein delta10;
DE Short=p24delta10;
DE AltName: Full=p24 family protein delta2d;
DE Short=p24delta2d;
DE Flags: Precursor;
GN OrderedLocusNames=At1g69460; ORFNames=F10D13_26;
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].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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, MUTAGENESIS OF PHE-207 AND
RP 211-LYS-LYS-212, SUBUNIT, 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 -!- 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.
CC -!- MISCELLANEOUS: The lumenal coiled-coil domain is required for the Golgi
CC subcellular location.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG60114.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN60269.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC073178; AAG60114.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE34928.1; -; Genomic_DNA.
DR EMBL; AF083711; AAN60269.1; ALT_INIT; mRNA.
DR EMBL; AY072343; AAL61950.1; -; mRNA.
DR EMBL; AY114598; AAM47917.1; -; mRNA.
DR RefSeq; NP_177105.2; NM_105613.5.
DR AlphaFoldDB; Q8VY92; -.
DR SMR; Q8VY92; -.
DR BioGRID; 28499; 14.
DR IntAct; Q8VY92; 13.
DR STRING; 3702.AT1G69460.1; -.
DR PaxDb; Q8VY92; -.
DR PRIDE; Q8VY92; -.
DR ProteomicsDB; 248684; -.
DR EnsemblPlants; AT1G69460.1; AT1G69460.1; AT1G69460.
DR GeneID; 843278; -.
DR Gramene; AT1G69460.1; AT1G69460.1; AT1G69460.
DR KEGG; ath:AT1G69460; -.
DR Araport; AT1G69460; -.
DR TAIR; locus:2007196; AT1G69460.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_2_1; -.
DR InParanoid; Q8VY92; -.
DR OMA; MSHRVRM; -.
DR OrthoDB; 1370889at2759; -.
DR PhylomeDB; Q8VY92; -.
DR PRO; PR:Q8VY92; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VY92; 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; HDA:TAIR.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..214
FT /note="Transmembrane emp24 domain-containing protein
FT p24delta10"
FT /id="PRO_0000419790"
FT TOPO_DOM 25..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..149
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 164..177
FT /evidence="ECO:0000255"
FT MOTIF 207..214
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000250"
FT MOTIF 207..208
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="Omega-N-methylated arginine"
FT /evidence="ECO:0000250"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 207
FT /note="F->Y: Does not affect the subcellular location."
FT /evidence="ECO:0000269|PubMed:22132757"
FT MUTAGEN 211..212
FT /note="KK->SS: Redirection of the subcellular location to
FT multivesicular body (MVB), the prevacuolar compartment
FT (PVC) and the vacuole."
FT /evidence="ECO:0000269|PubMed:22132757"
SQ SEQUENCE 214 AA; 24414 MW; 3F6F4803B3D58D48 CRC64;
MFLQSQKLWT MLLILAIWSP ISHSLHFDLH SGRTKCIAED IKSNSMTVGK YNIDNPHEGQ
ALPQTHKISV KVTSNSGNNY HHAEQVDSGQ FAFSAVEAGD YMACFTAVDH KPEVSLSIDF
EWKTGVQSKS WANVAKKSQV EVMEFEVKSL LDTVNSIHEE MYYLRDREEE MQDLNRSTNT
KMAWLSVLSF FVCIGVAGMQ FLHLKTFFEK KKVI
