| Tag | Content |
|---|
| CPLM ID | CPLM-007729 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Coatomer subunit beta |
Protein Synonyms/Alias | Beta-coat protein; Beta-COP |
Gene Name | betaCop |
Gene Synonyms/Alias | CG6223 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 877 | TDLHEYLKHLLKSTN | 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. Required for limiting lipid storage in lipid droplets. |
Sequence Annotation | REPEAT 129 166 HEAT 1.
REPEAT 238 275 HEAT 2.
REPEAT 314 351 HEAT 3.
REPEAT 393 430 HEAT 4.
REPEAT 466 506 HEAT 5. |
Keyword | Complete proteome; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane; Protein transport; Reference proteome; Repeat; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 964 AA |
Protein Sequence | MTSQVPCYTI INSPDLEVTN EMQLKRDLEK GDTNVKIETL KRVIKLLLNG ERYPGLIMTI 60
IRFVLPVQNH TIKKLLLIFW EIVPKTSADG KLLQEMILVC DAYRKDLQHP NEFLRGSTLR 120
FLCKLKEPEL LEPLMPAIRA CLDHRHSYVR RNAVLAIFTI YKNFDWLVPD GPELIASFLD 180
TQQDMSCKRN AFLMLLHADQ ERALNYLASC IDQVHTFGDI LQLVIVELIY KVCHANPAER 240
SRFIRCIYNL LNSSSNAVRY ESAGTLITLS LAPTAIKAAA SCYIELVVKE SDNNVKLIVL 300
DRLVAMKEHE GMEKVMQDLV MDVLRVLAAP DIEVRRKTLA LALDLVYSRN IGEMVLVLKK 360
EVAKTHNVEH EDTGKYRQLL VRTLHTCSIK FPDVAANVIP VLVEFLSDTN ELAAADVLIF 420
IREAIQKFPA LRALIIEHLI EAFPQIKSSK IHRAAVWILG EYVEGSQILE VIAVIQQTLG 480
EVPMVEAEQR RLAGDQTEEQ KQQQGSAGGN AAGSAAEGSG SGNASNKVTS DGTYATQSAY 540
SLAPVAKAEK RPPLRQYLMD GDFFIGAALS ATLTKLALRY AELETEARAQ NRLTTQVMLI 600
MSSILHLGKS GFPSKPITND DTDRIFVCLR TLSERTPEAI SVFTLYCREA LGKMLDAQHD 660
EDQRMLKEKQ KATAKVQPDD PVLFAQLSNG RDNQLGENVF ESSLNQALAG SKNAQLSDVA 720
SPNSKLNKVT QLTGFSDPVY AEAYVNVNQY DIVLDVLIVN QTNDTLQNCT LELATLGDLK 780
LVERPHPVVL APHDFCNIKA NVKVSSTENG IIFGNIVYET ALNTNVVVLN TIHIDIMDYI 840
IPASCTDTEF RQMWQDFEWE NKVTVNTSFT DLHEYLKHLL KSTNMKCLTP EKALSGQCGF 900
MAANMYAKSI FGENALANLS IEKPVDDPDS KVTGHIRIRA KSQGMALSLG DKISSSQKQS 960
VQAA 964 |
Gene Ontology | GO:0030126; C:COPI vesicle coat; IEA:InterPro. GO:0005794; C:Golgi apparatus; IDA:FlyBase. GO:0005198; F:structural molecule activity; IEA:InterPro. GO:0000902; P:cell morphogenesis; IMP:FlyBase. GO:0006886; P:intracellular protein transport; IEA:InterPro. GO:0006911; P:phagocytosis, engulfment; IMP:FlyBase. GO:0010883; P:regulation of lipid storage; IDA:FlyBase. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |