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Overview

Uniprot IDQ9Y678
Protein NameCoatomer subunit gamma-1
Gene NameCOPG1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
600 STPITAVKQPEKVAA
604 TAVKQPEKVAATRQE
733 CMMKFTVKDCDPTTG

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. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity)

Protein Sequence

10 MLKKFDKKDE 20 ESGGGSNPFQ 30 HLEKSAVLQE 40 ARVFNETPIN 50 PRKCAHILTK 60 ILYLINQGEH 70 LGTTEATEAF 80 FAMTKLFQSN 90 DPTLRRMCYL 100 TIKEMSCIAE 110 DVIIVTSSLT 120 KDMTGKEDNY 130 RGPAVRALCQ 140 ITDSTMLQAI 150 ERYMKQAIVD 160 KVPSVSSSAL 170 VSSLHLLKCS 180 FDVVKRWVNE 190 AQEAASSDNI 200 MVQYHALGLL 210 YHVRKNDRLA 220 VNKMISKVTR 230 HGLKSPFAYC 240 MMIRVASKQL 250 EEEDGSRDSP 260 LFDFIESCLR 270 NKHEMVVYEA 280 ASAIVNLPGC 290 SAKELAPAVS 300 VLQLFCSSPK 310 AALRYAAVRT 320 LNKVAMKHPS 330 AVTACNLDLE 340 NLVTDSNRSI 350 ATLAITTLLK 360 TGSESSIDRL 370 MKQISSFMSE 380 ISDEFKVVVV 390 QAISALCQKY 400 PRKHAVLMNF 410 LFTMLREEGG 420 FEYKRAIVDC 430 IISIIEENSE 440 SKETGLSHLC 450 EFIEDCEFTV 460 LATRILHLLG 470 QEGPKTTNPS 480 KYIRFIYNRV 490 VLEHEEVRAG 500 AVSALAKFGA 510 QNEEMLPSIL 520 VLLKRCVMDD 530 DNEVRDRATF 540 YLNVLEQKQK 550 ALNAGYILNG 560 LTVSIPGLER 570 ALQQYTLEPS 580 EKPFDLKSVP 590 LATAPMAEQR 600 TESTPITAVK 610 QPEKVAATRQ 620 EIFQEQLAAV 630 PEFRGLGPLF 640 KSSPEPVALT 650 ESETEYVIRC 660 TKHTFTNHMV 670 FQFDCTNTLN 680 DQTLENVTVQ 690 MEPTEAYEVL 700 CYVPARSLPY 710 NQPGTCYTLV 720 ALPKEDPTAV 730 ACTFSCMMKF 740 TVKDCDPTTG 750 ETDDEGYEDE 760 YVLEDLEVTV 770 ADHIQKVMKL 780 NFEAAWDEVG 790 DEFEKEETFT 800 LSTIKTLEEA 810 VGNIVKFLGM 820 HPCERSDKVP 830 DNKNTHTLLL 840 AGVFRGGHDI 850 LVRSRLLLLD 860 TVTMQVTARS 870 LEELPVDIIL ASVG

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030126 COPI vesicle coat
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0005793 endoplasmic reticulum-Golgi intermediate compartment
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0000139 Golgi membrane
Cellular Component GO:0030133 transport vesicle
Molecular Function GO:0005198 structural molecule activity
Biological Process GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport
Biological Process GO:0051683 establishment of Golgi localization
Biological Process GO:0006891 intra-Golgi vesicle-mediated transport
Biological Process GO:0006886 intracellular protein transport
Biological Process GO:0072384 organelle transport along microtubule
Biological Process GO:0009306 protein secretion
Biological Process GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum

Reference

[1] 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.

[2] 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.