P24D9_ARATH
ID P24D9_ARATH Reviewed; 214 AA.
AC Q9LQY3; Q8GWZ7; Q8LFL9;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24delta9;
DE AltName: Full=p24 family protein delta2c;
DE Short=p24delta2c;
DE AltName: Full=p24 family protein delta9;
DE Short=p24delta9;
DE Flags: Precursor;
GN OrderedLocusNames=At1g26690; ORFNames=T24P13.7;
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 Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-214.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-214.
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 [6]
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 [7]
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43132.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006535; AAF87046.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30721.1; -; Genomic_DNA.
DR EMBL; AY084765; AAM67291.1; -; mRNA.
DR EMBL; AK118529; BAC43132.1; ALT_INIT; mRNA.
DR EMBL; BT003733; AAO39961.1; -; mRNA.
DR RefSeq; NP_564256.1; NM_102432.3.
DR AlphaFoldDB; Q9LQY3; -.
DR SMR; Q9LQY3; -.
DR STRING; 3702.AT1G26690.1; -.
DR PaxDb; Q9LQY3; -.
DR PRIDE; Q9LQY3; -.
DR ProteomicsDB; 248786; -.
DR EnsemblPlants; AT1G26690.1; AT1G26690.1; AT1G26690.
DR GeneID; 839210; -.
DR Gramene; AT1G26690.1; AT1G26690.1; AT1G26690.
DR KEGG; ath:AT1G26690; -.
DR Araport; AT1G26690; -.
DR TAIR; locus:2200630; AT1G26690.
DR eggNOG; KOG1691; Eukaryota.
DR HOGENOM; CLU_066963_3_2_1; -.
DR InParanoid; Q9LQY3; -.
DR OMA; GVTCAWQ; -.
DR OrthoDB; 1370889at2759; -.
DR PhylomeDB; Q9LQY3; -.
DR PRO; PR:Q9LQY3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQY3; baseline and differential.
DR Genevisible; Q9LQY3; 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; Golgi apparatus;
KW Membrane; Methylation; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..214
FT /note="Transmembrane emp24 domain-containing protein
FT p24delta9"
FT /id="PRO_0000419789"
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 CONFLICT 110
FT /note="H -> Q (in Ref. 3; AAM67291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24397 MW; 40AE17857AEBBFFC CRC64;
MFLRSLNLCT ILLFLAISSQ VSQSLHFELQ SGRTKCISED IKSNSMTVGK YTVVNPNEAH
PSPQSHKISI RVTSSYGNTY HHAEDVESGQ FAFTAVESGD YMACYTAVDH KPEVTLSIDF
DWRTGVQSKS WSSVAKKSQV EVMEFDVKRL IETVNSIHEE MFYLREREEE MQNLNRATNS
KMAWLSFLSL FVCLGVAGMQ FVHLKTFFEK KKVI
