Search Results

Overview

Uniprot IDP48444
Protein NameCoatomer subunit delta
Gene NameARCN1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 LAAAVCTKAGKAIVS
164 AEMRRKAKELQQARR
224 ARPSGPSKALKLGAK
227 SGPSKALKLGAKGKE
233 LKLGAKGKEVDNFVD
241 EVDNFVDKLKSEGET
243 DNFVDKLKSEGETIM
256 IMSSSMGKRTSEATK
335 QTHPNVDKKLFTAES
44 PKLMNTGKQHTFVET

Function

Component of the coatomer, 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. The 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 MVLLAAAVCT 20 KAGKAIVSRQ 30 FVEMTRTRIE 40 GLLAAFPKLM 50 NTGKQHTFVE 60 TESVRYVYQP 70 MEKLYMVLIT 80 TKNSNILEDL 90 ETLRLFSRVI 100 PEYCRALEEN 110 EISEHCFDLI 120 FAFDEIVALG 130 YRENVNLAQI 140 RTFTEMDSHE 150 EKVFRAVRET 160 QEREAKAEMR 170 RKAKELQQAR 180 RDAERQGKKA 190 PGFGGFGSSA 200 VSGGSTAAMI 210 TETIIETDKP 220 KVAPAPARPS 230 GPSKALKLGA 240 KGKEVDNFVD 250 KLKSEGETIM 260 SSSMGKRTSE 270 ATKMHAPPIN 280 MESVHMKIEE 290 KITLTCGRDG 300 GLQNMELHGM 310 IMLRISDDKY 320 GRIRLHVENE 330 DKKGVQLQTH 340 PNVDKKLFTA 350 ESLIGLKNPE 360 KSFPVNSDVG 370 VLKWRLQTTE 380 ESFIPLTINC 390 WPSESGNGCD 400 VNIEYELQED 410 NLELNDVVIT 420 IPLPSGVGAP 430 VIGEIDGEYR 440 HDSRRNTLEW 450 CLPVIDAKNK 460 SGSLEFSIAG 470 QPNDFFPVQV 480 SFVSKKNYCN 490 IQVTKVTQVD 500 GNSPVRFSTE 510 TTFLVDKYEI L

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030126 COPI vesicle coat
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0000139 Golgi membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0030133 transport vesicle
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport
Biological Process GO:0051645 Golgi localization
Biological Process GO:0006886 intracellular protein transport
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] 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.

[6] 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.