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Overview

Uniprot ID	Q9NPQ8
Protein Name	Chaperone Ric-8A
Gene Name	RIC8A
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
450	TDEYKEAKASINPVT
489	KLVTMFDKLSRNRVI

Function

Chaperone that specifically binds and folds nascent G alpha proteins prior to G protein heterotrimer formation, promoting their stability and activity: folds GNAI1, GNAO1, GNA13 and GNAQ (By similarity). Does not fold G(s) G-alpha proteins GNAS nor GNAL (By similarity). Also acts as a guanine nucleotide exchange factor (GEF) for G alpha proteins by stimulating exchange of bound GDP for free GTP (By similarity). Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein (GNAI1), possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex (By similarity). Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation (PubMed:16629901)

Protein Sequence

10 MEPRAVAEAV 20 ETGEEDVIME 30 ALRSYNQEHS 40 QSFTFDDAQQ 50 EDRKRLAELL 60 VSVLEQGLPP 70 SHRVIWLQSV 80 RILSRDRNCL 90 DPFTSRQSLQ 100 ALACYADISV 110 SEGSVPESAD 120 MDVVLESLKC 130 LCNLVLSSPV 140 AQMLAAEARL 150 VVKLTERVGL 160 YRERSFPHDV 170 QFFDLRLLFL 180 LTALRTDVRQ 190 QLFQELKGVR 200 LLTDTLELTL 210 GVTPEGNPPP 220 TLLPSQETER 230 AMEILKVLFN 240 ITLDSIKGEV 250 DEEDAALYRH 260 LGTLLRHCVM 270 IATAGDRTEE 280 FHGHAVNLLG 290 NLPLKCLDVL 300 LTLEPHGDST 310 EFMGVNMDVI 320 RALLIFLEKR 330 LHKTHRLKES 340 VAPVLSVLTE 350 CARMHRPARK 360 FLKAQVLPPL 370 RDVRTRPEVG 380 EMLRNKLVRL 390 MTHLDTDVKR 400 VAAEFLFVLC 410 SESVPRFIKY 420 TGYGNAAGLL 430 AARGLMAGGR 440 PEGQYSEDED 450 TDTDEYKEAK 460 ASINPVTGRV 470 EEKPPNPMEG 480 MTEEQKEHEA 490 MKLVTMFDKL 500 SRNRVIQPMG 510 MSPRGHLTSL 520 QDAMCETMEQ 530 QLSSDPDSDP D

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005938	cell cortex
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005886	plasma membrane
Molecular Function	GO:0001965	G-protein alpha-subunit binding
Molecular Function	GO:0005085	guanyl-nucleotide exchange factor activity
Molecular Function	GO:0044183	protein folding chaperone
Biological Process	GO:0007186	G protein-coupled receptor signaling pathway

Reference

[1] 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.

[2] 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.

[3] 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.