| Tag | Content |
|---|
| CPLM ID | CPLM-001032 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Coatomer subunit beta' |
Protein Synonyms/Alias | Beta'-coat protein; Beta'-COP |
Gene Name | beta'Cop |
Gene Synonyms/Alias | CG6699 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 629 | RVAHFLEKQGFKSQA | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). |
Sequence Annotation | REPEAT 13 54 WD 1.
REPEAT 55 94 WD 2.
REPEAT 97 136 WD 3.
REPEAT 140 180 WD 4.
REPEAT 183 224 WD 5.
REPEAT 227 266 WD 6.
REPEAT 352 390 WD 7. |
Keyword | Complete proteome; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane; Protein transport; Reference proteome; Repeat; Transport; WD repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 914 AA |
Protein Sequence | MPLKLDIKRR LTSRSDRVKC VDLHPAEPWM LCALYNGHVH IMNYENQQMV KDFEVCDVPV 60
RSARFVARKN WILTGSDDMQ IRVFNYNTLE KVHSFEAHSD YLRCIAVHPT QPLVLTSSDD 120
MLIKLWNWEK MWACQRVFEG HTHYVMQIVF NPKDNNTFAS ASLDRTVKVW QLGSNFANFT 180
LEGHEKGVNC VDYYHGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NISAVCFHPE 240
LPIVLTGSED GTVRIWHSGT YRLETCLNYG FERVWTISSM RGTNNVALGY DEGSIIIKVG 300
REEPAMSMDV VGSKIIWAKH SEMQQVNLKT IADGTEIKDG ERLPVATKDM GACEIYPQTI 360
AHNPNGRFVV VCGDGEYIIY TSMALRNKAF GSAQEFVWAL ESNEYAIREN NGTVRLFRNF 420
KERKSFTPEY GAESIYGGYY FGVKTSSGLA FYDWETLQLV RRIEVQPKNV FWNESGSLVC 480
LATDDSYFVL GVDTAQVANA VETKEGLEDD GVESAFNVLG EVSECVKTGL WVGDCFIYTN 540
SVNRINYYVG GEIVTVSHLD RTMYLLGYVP KDNRIYLGDK ELNVISFCLQ LSVLEYQTAV 600
MRRDFERADV VLPTIPKEHR TRVAHFLEKQ GFKSQALQVS TDADHKFDLA LQIGDLEIAL 660
KLARESENSQ KWSQLADVAS SKNNMSLVKE CMQKANDLSG LLLLSTASGD AQLLEVVGAA 720
GSAQGHHNLA FLSAFLRSDV ERCLEILIET NRLPEAAFFA RTYLPSQMSR IVELWREKLG 780
KVNEKAGQSL ADPAQYTNLF PGLGDALRVE QHLQEERARK APARLAANLP LNSERHPLQE 840
LFAAEQGAAG QHLEEKVKPA YVPAQAVVSS SQVAEPTSAA DDDDDLDLEI DGITLDDNID 900
TTDVNLDDDF LSDD 914 |
Gene Ontology | GO:0030126; C:COPI vesicle coat; NAS:UniProtKB. GO:0005795; C:Golgi stack; IDA:FlyBase. GO:0005198; F:structural molecule activity; IEA:InterPro. GO:0006888; P:ER to Golgi vesicle-mediated transport; NAS:UniProtKB. GO:0006886; P:intracellular protein transport; IEA:InterPro. GO:0010883; P:regulation of lipid storage; IDA:FlyBase. GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; NAS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |