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P24B3_ARATH
ID   P24B3_ARATH             Reviewed;         214 AA.
AC   Q9LIL4;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Transmembrane emp24 domain-containing protein p24beta3;
DE   AltName: Full=p24 family protein beta2;
DE            Short=p24beta2;
DE   AltName: Full=p24 family protein beta3;
DE            Short=p24beta3;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g22845; ORFNames=MWI23.22;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [3]
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   [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, 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 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       {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: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000269|PubMed:22132757}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:22132757}. Golgi apparatus, Golgi stack membrane
CC       {ECO:0000269|PubMed:22132757}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:22132757}. Note=Cycles between the endoplasmic
CC       reticulum and Golgi via COPI and COPII dependent pathways.
CC       {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR   EMBL; AP001300; BAB03029.1; -; Genomic_DNA.
DR   EMBL; AB022223; BAB03029.1; JOINED; Genomic_DNA.
DR   EMBL; CP002686; AEE76683.1; -; Genomic_DNA.
DR   EMBL; AY070742; AAL50082.1; -; mRNA.
DR   EMBL; AY093742; AAM10366.1; -; mRNA.
DR   RefSeq; NP_188924.3; NM_113184.5.
DR   AlphaFoldDB; Q9LIL4; -.
DR   SMR; Q9LIL4; -.
DR   BioGRID; 7188; 3.
DR   IntAct; Q9LIL4; 3.
DR   STRING; 3702.AT3G22845.1; -.
DR   SwissPalm; Q9LIL4; -.
DR   PaxDb; Q9LIL4; -.
DR   PRIDE; Q9LIL4; -.
DR   ProteomicsDB; 248859; -.
DR   EnsemblPlants; AT3G22845.1; AT3G22845.1; AT3G22845.
DR   GeneID; 821856; -.
DR   Gramene; AT3G22845.1; AT3G22845.1; AT3G22845.
DR   KEGG; ath:AT3G22845; -.
DR   Araport; AT3G22845; -.
DR   TAIR; locus:2094364; AT3G22845.
DR   eggNOG; KOG1692; Eukaryota.
DR   HOGENOM; CLU_066963_1_1_1; -.
DR   InParanoid; Q9LIL4; -.
DR   OMA; NAEDCFY; -.
DR   OrthoDB; 1328081at2759; -.
DR   PhylomeDB; Q9LIL4; -.
DR   PRO; PR:Q9LIL4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LIL4; baseline and differential.
DR   Genevisible; Q9LIL4; AT.
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:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; HDA: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:0000325; C:plant-type vacuole; HDA:TAIR.
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   2: Evidence at transcript level;
KW   Coiled coil; ER-Golgi transport; Glycoprotein; Golgi apparatus; Membrane;
KW   Methylation; Protein transport; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..214
FT                   /note="Transmembrane emp24 domain-containing protein
FT                   p24beta3"
FT                   /id="PRO_0000419793"
FT   TOPO_DOM        28..178
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..122
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   COILED          140..158
FT                   /evidence="ECO:0000255"
FT   MOTIF           204..214
FT                   /note="COPI vesicle coat-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           204..205
FT                   /note="COPII vesicle coat-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           213..214
FT                   /note="Required for the export from the endoplasmic
FT                   reticulum to the Golgi"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         164
FT                   /note="Omega-N-methylated arginine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         169
FT                   /note="Omega-N-methylated arginine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   214 AA;  24282 MW;  5C0C31625AF7A134 CRC64;
     MERRQAKIHV FVLIGLILLN SINQISSLSV TVNDEECVQE YVLYEGDTVS GNFVVVDHDI
     FWGSDHPGLD FTVTSPAGNI VQTLKGTSGD KFEFKAPKSG MYKFCFHNPY STPETVSFYI
     HVGHIPNEHD LAKDEHLDPV NVKIAELREA LESVVAEQKY LKARDTRHRH TNESTRKRVI
     FYTVGEYIFL AAASGLQVLY IRKLFSKSVA YNRV
 
 
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