SEC23/YPR181C Summary Help

Standard Name SEC23 1
Systematic Name YPR181C
Feature Type ORF, Verified
Description GTPase-activating protein, stimulates the GTPase activity of Sar1p; component of the Sec23p-Sec24p heterodimer of the COPII vesicle coat, involved in ER to Golgi transport; substrate of Ubp3/Bre5 complex; ubiquitylated by Ub-ligase Rsp5p; proteasome-mediated degradation of Sec23p is regulated by Cdc48p (2, 3, 4, 5 and see Summary Paragraph)
Name Description SECretory
Chromosomal Location
ChrXVI:899667 to 897361 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All SEC23 GO evidence and references
  View Computational GO annotations for SEC23
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 1 genes
Classical genetics
Large-scale survey
173 total interaction(s) for 78 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 53
  • Affinity Capture-RNA: 4
  • Affinity Capture-Western: 32
  • Biochemical Activity: 3
  • Co-fractionation: 5
  • Co-purification: 2
  • FRET: 2
  • Protein-RNA: 1
  • Reconstituted Complex: 23
  • Two-hybrid: 11

Genetic Interactions
  • Dosage Lethality: 4
  • Dosage Rescue: 7
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 5
  • Positive Genetic: 1
  • Synthetic Growth Defect: 5
  • Synthetic Lethality: 9
  • Synthetic Rescue: 5

Expression Summary
Length (a.a.) 768
Molecular Weight (Da) 85,384
Isoelectric Point (pI) 5.44
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:899667 to 897361 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2307 899667..897361 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006385

Transport of proteins from the endoplasmic reticulum (ER) to the Golgi is mediated by COPII vesicles (6). The COPII vesicle coat is minimally comprised of 5 subunits: the GTPase Sar1p, the Sec23p-Sec24p heterodimer, and the Sec13p-Sec31p complex (7, 8, 3, 9). COPII vesicle coats can also contain heterodimers of Sec23p complexed with either of the Sec24p homologs, Sfb2p or Sfb3p (10, 11, 12). In S. cerevisiae, COPII vesicle formation occurs throughout the ER (13). In most other eukaryotes, COPII vesicle-mediated protein export is localized to specialized regions termed transitional ER (tER) or ER exit sites (ERES) (8).

COPII vesicle formation requires the assembly of the COPII vesicle coat and cargo selection and is regulated by cycles of GTP hydrolysis. The GTP exchange factor (GEF) Sec12p, an ER membrane protein, activates Sar1p by exchanging GDP for GTP. Sar1p-GTP recruits the Sec23p-Sec24p heterodimer. Sec23p is a GTPase activating protein (GAP) for the Sar1p GTPase activity (14, 2, and reviewed in 8). Sec24p, Sfb2p, and Sfb3p, are involved in cargo selection (15, 12, 11). Sar1p, the Sec23p-Sec24p heterodimer, and cargo form the prebudding complex. Improper cargo selection results in GTP hydrolysis and diassembly of the prebudding complex (16). However, once the pre-budding complex is assembled, Sec13p and Sec31p polymerize to form the outer layer or scaffold of the COPII vesicle coat. The Sec13p-Sec31p complex further stimulates the GTPase activity of Sar1p (reviewed in 8).

Although Sar1p, Sec23p, Sec24p, Sec13p, and Sec31p are necessary and sufficient for vesicle formation, additional factors such as Sec16p and Sed4p are also involved in this process. Through interactions with other COPII proteins, Sec16p is thought to facilitate the assembly of the vesicle coat by stabilizing the pre-budding complex (17) while Sed4p regulates the vesicle budding process by stimulating the GTPase activity of Sar1p (18).

Mutations in genes involved in COPII vesicle formation are also impaired in other processes such as ERAD (ER-associated degradation) and autophagy, suggesting that ER to the Golgi transport is a prerequisite for these processes to occur (19, 20, 21, 22).

Mutations in the human homolog of SEC23, Sec23A, cause the autosomal recessive disorder Cranio-lenticulo sutural dysplasia (CLSD), while mutation of Sar1B, one of the two human isoforms of S. cerevisiae Sar1p, cause defects in lipoprotein metabolism including the diseases that are known as the chylomicron retention diseases (CMRDs) (reviewed in 8).

Last updated: 2010-01-07 Contact SGD

References cited on this page View Complete Literature Guide for SEC23
1) Novick P, et al.  (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21(1):205-15
2) Yoshihisa T, et al.  (1993) Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 259(5100):1466-8
3) Barlowe C, et al.  (1994) COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77(6):895-907
4) Duden R  (2003) ER-to-Golgi transport: COP I and COP II function (Review). Mol Membr Biol 20(3):197-207
5) Ossareh-Nazari B, et al.  (2010) The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23. Exp Cell Res 316(20):3351-7
6) Bonifacino JS and Glick BS  (2004) The mechanisms of vesicle budding and fusion. Cell 116(2):153-66
7) Lee MC and Miller EA  (2007) Molecular mechanisms of COPII vesicle formation. Semin Cell Dev Biol 18(4):424-34
8) Hughes H and Stephens DJ  (2008) Assembly, organization, and function of the COPII coat. Histochem Cell Biol 129(2):129-51
9) Fath S, et al.  (2007) Structure and organization of coat proteins in the COPII cage. Cell 129(7):1325-36
10) Peng R, et al.  (2000) Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem 275(15):11521-8
11) Miller E, et al.  (2002) Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 21(22):6105-13
12) Miller EA, et al.  (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4):497-509
13) Rossanese OW, et al.  (1999) Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J Cell Biol 145(1):69-81
14) Barlowe C, et al.  (1993) Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum. J Biol Chem 268(2):873-9
15) Shimoni Y, et al.  (2000) Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol 151(5):973-84
16) Sato K and Nakano A  (2005) Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis. Nat Struct Mol Biol 12(2):167-74
17) Supek F, et al.  (2002) Sec16p potentiates the action of COPII proteins to bud transport vesicles. J Cell Biol 158(6):1029-38
18) Kodera C, et al.  (2011) Sed4p stimulates sar1p GTP hydrolysis and promotes limited coat disassembly. Traffic 12(5):591-9
19) Taxis C, et al.  (2002) ER-golgi traffic is a prerequisite for efficient ER degradation. Mol Biol Cell 13(6):1806-18
20) Hamasaki M, et al.  (2003) The early secretory pathway contributes to autophagy in yeast. Cell Struct Funct 28(1):49-54
21) Fu L and Sztul E  (2003) Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulator. J Cell Biol 160(2):157-63
22) Ishihara N, et al.  (2001) Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell 12(11):3690-702