Q9R064
uniprot
Q9R064
canonical
amino_acid_sequence
MGSSQSVEIPGGGTEGYHVLRVQENSPGHRAGLEPFFDFIVSISGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPTRPFEEGKKISLPGQMTGTPITPLKDGFTQVQLSSVSPPSLSPPGTAGVEQSLSGLSISSAPPAVSNVLSTGVPTVPLLPPQVNQSLASVPPMNPAATLPSLMPLSAGLPNLPNLPSLSNFNLPAPHIMPGVGLPELGKPGLPPLPSLPPRNVPGIAPLPMPSDFLPSFPLVPEGSSAASAGEPLSSLPAMGPPSDPVMTTAKADTSSLTVDVMSPASKVPTTVEDRVSDCTPAMEKPVSAVTDANASGAS
uniprot
proteins
function
FUNCTION: Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis (PubMed:10487747, PubMed:23940043). May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (By similarity). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity). {ECO:0000250|UniProtKB:Q99JX3, ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:23940043}.
uniprot
proteins
mass_dalton
47221
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: No or few Golgi targeting, accumulates in the cytoplasm."; /evidence="ECO:0000269|PubMed:10487747
uniprot
proteins
post_translational_modification
PTM: Myristoylated (By similarity). Myristoylation is essential for the Golgi targeting (PubMed:10487747). {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q9H8Y8}.; PTM: Phosphorylated in mitotic cells. ER stress-induced phosphorylation at Ser-443 induces monomerization and subsequent relocalization from Golgi to ER which is essential for mediating unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. {ECO:0000250|UniProtKB:Q9H8Y8}.
uniprot
proteins
protein_family
GORASP family
uniprot
proteins
pubmed
10487747
uniprot
proteins
pubmed
11739401
uniprot
proteins
pubmed
11739402
uniprot
proteins
pubmed
15047867
uniprot
proteins
pubmed
23940043
uniprot
proteins
sequence_length
454
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11739401}; Lipid-anchor {ECO:0000269|PubMed:10487747}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H8Y8}. Golgi apparatus {ECO:0000250|UniProtKB:Q9H8Y8}. Note=Detected in the intermediate Golgi, membrane-associated (PubMed:10487747). ER stress triggers its relocalization from Golgi to ER membrane (By similarity). {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747}.
uniprot
proteins