Search Results

Overview

Uniprot IDP53621
Protein NameCoatomer subunit alpha
Gene NameCOPA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
170 DISGLRKKNLSPGAV
574 PIYVTRVKGNNVYCL
600 DPTEFKFKLALINRK
607 KLALINRKYDEVLHM
8 MLTKFETKSARVKGL
825 FEGTIASKGKGGALA
827 GTIASKGKGGALAAD

Function

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. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity)

Protein Sequence

10 MLTKFETKSA 20 RVKGLSFHPK 30 RPWILTSLHN 40 GVIQLWDYRM 50 CTLIDKFDEH 60 DGPVRGIDFH 70 KQQPLFVSGG 80 DDYKIKVWNY 90 KLRRCLFTLL 100 GHLDYIRTTF 110 FHHEYPWILS 120 ASDDQTIRVW 130 NWQSRTCVCV 140 LTGHNHYVMC 150 AQFHPTEDLV 160 VSASLDQTVR 170 VWDISGLRKK 180 NLSPGAVESD 190 VRGITGVDLF 200 GTTDAVVKHV 210 LEGHDRGVNW 220 AAFHPTMPLI 230 VSGADDRQVK 240 IWRMNESKAW 250 EVDTCRGHYN 260 NVSCAVFHPR 270 QELILSNSED 280 KSIRVWDMSK 290 RTGVQTFRRD 300 HDRFWVLAAH 310 PNLNLFAAGH 320 DGGMIVFKLE 330 RERPAYAVHG 340 NMLHYVKDRF 350 LRQLDFNSSK 360 DVAVMQLRSG 370 SKFPVFNMSY 380 NPAENAVLLC 390 TRASNLENST 400 YDLYTIPKDA 410 DSQNPDAPEG 420 KRSSGLTAVW 430 VARNRFAVLD 440 RMHSLLIKNL 450 KNEITKKVQV 460 PNCDEIFYAG 470 TGNLLLRDAD 480 SITLFDVQQK 490 RTLASVKISK 500 VKYVIWSADM 510 SHVALLAKHA 520 IVICNRKLDA 530 LCNIHENIRV 540 KSGAWDESGV 550 FIYTTSNHIK 560 YAVTTGDHGI 570 IRTLDLPIYV 580 TRVKGNNVYC 590 LDRECRPRVL 600 TIDPTEFKFK 610 LALINRKYDE 620 VLHMVRNAKL 630 VGQSIIAYLQ 640 KKGYPEVALH 650 FVKDEKTRFS 660 LALECGNIEI 670 ALEAAKALDD 680 KNCWEKLGEV 690 ALLQGNHQIV 700 EMCYQRTKNF 710 DKLSFLYLIT 720 GNLEKLRKMM 730 KIAEIRKDMS 740 GHYQNALYLG 750 DVSERVRILK 760 NCGQKSLAYL 770 TAATHGLDEE 780 AESLKETFDP 790 EKETIPDIDP 800 NAKLLQPPAP 810 IMPLDTNWPL 820 LTVSKGFFEG 830 TIASKGKGGA 840 LAADIDIDTV 850 GTEGWGEDAE 860 LQLDEDGFVE 870 ATEGLGDDAL 880 GKGQEEGGGW 890 DVEEDLELPP 900 ELDISPGAAG 910 GAEDGFFVPP 920 TKGTSPTQIW 930 CNNSQLPVDH 940 ILAGSFETAM 950 RLLHDQVGVI 960 QFGPYKQLFL 970 QTYARGRTTY 980 QALPCLPSMY 990 GYPNRNWKDA 1000 GLKNGVPAVG 1010 LKLNDLIQRL 1020 QLCYQLTTVG 1030 KFEEAVEKFR 1040 SILLSVPLLV 1050 VDNKQEIAEA 1060 QQLITICREY 1070 IVGLSVETER 1080 KKLPKETLEQ 1090 QKRICEMAAY 1100 FTHSNLQPVH 1110 MILVLRTALN 1120 LFFKLKNFKT 1130 AATFARRLLE 1140 LGPKPEVAQQ 1150 TRKILSACEK 1160 NPTDAYQLNY 1170 DMHNPFDICA 1180 ASYRPIYRGK 1190 PVEKCPLSGA 1200 CYSPEFKGQI 1210 CRVTTVTEIG 1220 KDVIGLRISP LQFR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030126 COPI vesicle coat
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0000139 Golgi membrane
Cellular Component GO:0030426 growth cone
Cellular Component GO:0016020 membrane
Cellular Component GO:0030133 transport vesicle
Molecular Function GO:0005179 hormone activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0005198 structural molecule activity
Biological Process GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport
Biological Process GO:0006891 intra-Golgi vesicle-mediated transport
Biological Process GO:0006886 intracellular protein transport
Biological Process GO:0030157 pancreatic juice secretion
Biological Process GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.