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P24D7_ARATH
ID   P24D7_ARATH             Reviewed;         212 AA.
AC   Q8GYG1; Q9LMF7; Q9XI86;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Transmembrane emp24 domain-containing protein p24delta7;
DE   AltName: Full=p24 family protein delta2a;
DE            Short=p24delta2a;
DE   AltName: Full=p24 family protein delta7;
DE            Short=p24delta7;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g14010; ORFNames=F16A14.23, F7A19.10;
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=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   [4]
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   [5]
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=AAD39287.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF79411.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007576; AAD39287.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC068197; AAF79411.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29098.1; -; Genomic_DNA.
DR   EMBL; AK117657; BAC42310.1; -; mRNA.
DR   PIR; D86273; D86273.
DR   RefSeq; NP_172854.1; NM_101267.4.
DR   AlphaFoldDB; Q8GYG1; -.
DR   SMR; Q8GYG1; -.
DR   STRING; 3702.AT1G14010.1; -.
DR   PaxDb; Q8GYG1; -.
DR   PRIDE; Q8GYG1; -.
DR   ProteomicsDB; 248682; -.
DR   EnsemblPlants; AT1G14010.1; AT1G14010.1; AT1G14010.
DR   GeneID; 837961; -.
DR   Gramene; AT1G14010.1; AT1G14010.1; AT1G14010.
DR   KEGG; ath:AT1G14010; -.
DR   Araport; AT1G14010; -.
DR   TAIR; locus:2014864; AT1G14010.
DR   eggNOG; KOG1691; Eukaryota.
DR   HOGENOM; CLU_066963_3_2_1; -.
DR   InParanoid; Q8GYG1; -.
DR   OMA; SAAFYFH; -.
DR   OrthoDB; 1370889at2759; -.
DR   PhylomeDB; Q8GYG1; -.
DR   PRO; PR:Q8GYG1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8GYG1; 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   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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..212
FT                   /note="Transmembrane emp24 domain-containing protein
FT                   p24delta7"
FT                   /id="PRO_0000419787"
FT   TOPO_DOM        23..179
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..147
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   COILED          162..175
FT                   /evidence="ECO:0000255"
FT   MOTIF           205..212
FT                   /note="COPI vesicle coat-binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           205..206
FT                   /note="COPII vesicle coat-binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         165
FT                   /note="Omega-N-methylated arginine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  24156 MW;  B5367242110360C0 CRC64;
     MNHRRSSIVL LILSILSPVT LSIRYELLSG HTKCISEEIH ANAMTIGKYS IINPHEDHPL
     PSSHKVTVRV TSPQGTAYHE SDGVESGQFS FVAVETGDYI SCFSAVDHKP ETTLIIDFDW
     RTGIHTKDWS NVAKKSQVET MEFEVKKLFE TVNGIHDEMF YLRDREEEMH NLNIATNSKM
     AWLSFVSLAV CLSVAGLQFW HLKTFFQKKK LI
 
 
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