P24B2_ARATH
ID P24B2_ARATH Reviewed; 208 AA.
AC Q9S7M9; Q8L987;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transmembrane emp24 domain-containing protein p24beta2;
DE AltName: Full=p24 family protein beta1;
DE Short=p24beta1;
DE AltName: Full=p24 family protein beta2;
DE Short=p24beta2;
DE Flags: Precursor;
GN OrderedLocusNames=At3g07680; ORFNames=F17A17.2, MLP3.13;
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 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 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 [5]
RP GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, INTERACTION WITH
RP P24DELTA5, 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, COILED-COIL DOMAIN, DOMAIN, AND
RP MUTAGENESIS OF 199-PHE--VAL-208 AND ARG-207.
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 but also in post-Golgi membranes.
CC Thought to act as cargo receptor at the lumenal side for incorporation
CC of secretory cargo molecules into transport vesicles and to be involved
CC in vesicle coat formation at the cytoplasmic side (By similarity).
CC Interacts with p24delta5 at endoplasmic reticulum export sites for
CC endoplasmic reticulum exit and coupled transport to the Golgi
CC apparatus. {ECO:0000250, 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 p24delta5. {ECO:0000250,
CC ECO:0000269|PubMed:22577184}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
CC Single-pass type I membrane protein. Golgi apparatus, Golgi stack
CC membrane; Single-pass type I membrane protein. Note=Cycles between the
CC endoplasmic reticulum and Golgi via COPI and COPII dependent pathways.
CC -!- DOMAIN: The cytoplasmic C-terminal domain contains an Arg-Val motif,
CC which is involved in the anterograde ER-to-Golgi transport of the
CC protein. {ECO:0000269|PubMed:22132757}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; AC009176; AAF13086.1; -; Genomic_DNA.
DR EMBL; AC013483; AAF21178.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74586.1; -; Genomic_DNA.
DR EMBL; AF360268; AAK25978.1; -; mRNA.
DR EMBL; AY040079; AAK64137.1; -; mRNA.
DR EMBL; AY088581; AAM66112.1; -; mRNA.
DR RefSeq; NP_187425.1; NM_111647.5.
DR AlphaFoldDB; Q9S7M9; -.
DR SMR; Q9S7M9; -.
DR BioGRID; 5294; 27.
DR IntAct; Q9S7M9; 25.
DR STRING; 3702.AT3G07680.1; -.
DR PaxDb; Q9S7M9; -.
DR PRIDE; Q9S7M9; -.
DR ProteomicsDB; 248858; -.
DR DNASU; 819959; -.
DR EnsemblPlants; AT3G07680.1; AT3G07680.1; AT3G07680.
DR GeneID; 819959; -.
DR Gramene; AT3G07680.1; AT3G07680.1; AT3G07680.
DR KEGG; ath:AT3G07680; -.
DR Araport; AT3G07680; -.
DR TAIR; locus:2091107; AT3G07680.
DR eggNOG; KOG1692; Eukaryota.
DR HOGENOM; CLU_066963_1_1_1; -.
DR InParanoid; Q9S7M9; -.
DR OMA; ADSSWHY; -.
DR OrthoDB; 1328081at2759; -.
DR PhylomeDB; Q9S7M9; -.
DR PRO; PR:Q9S7M9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S7M9; baseline and differential.
DR Genevisible; Q9S7M9; AT.
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:TAIR.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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 InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; ER-Golgi transport; Glycoprotein; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..208
FT /note="Transmembrane emp24 domain-containing protein
FT p24beta2"
FT /id="PRO_0000419792"
FT TOPO_DOM 22..176
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..116
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 134..149
FT /evidence="ECO:0000255"
FT MOTIF 198..208
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 198..199
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 207..208
FT /note="Required for the export from the endoplasmic
FT reticulum to the Golgi"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 199..208
FT /note="Missing: Abolishes the export from the endoplasmic
FT reticulum to the Golgi."
FT /evidence="ECO:0000269|PubMed:22132757"
FT MUTAGEN 207
FT /note="R->A: Abolishes the export from the endoplasmic
FT reticulum to the Golgi."
FT /evidence="ECO:0000269|PubMed:22132757"
FT CONFLICT 5
FT /note="G -> A (in Ref. 4; AAM66112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 24331 MW; 71EFA7E07CABF668 CRC64;
MSLKGTIVLL GLLWSFQATL GIRFVIDREE CFSHKAEYEG DTLHVSFVVI KSDSQWHFNE
DGVDLVIHGP TGEQIHDFRE QISAKHDFVV QKKGVYRFCF TNKSPYHETI DFDVQLGHFA
YYDQHAKDEH FTPLMEQISK LEEALYNIQF EQHWLEAQTD RQAIVNENMS KRAVHKALFE
SFALIGASFL QVYLLRRLFE RKLGMSRV
