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Protein

Protein transport protein SEC23

Gene

SEC23

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.22 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Zinc1 Publication1
Metal bindingi61Zinc1 Publication1
Metal bindingi80Zinc1 Publication1
Metal bindingi83Zinc1 Publication1

GO - Molecular functioni

  • GTPase activator activity Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: InterPro
  • intracellular protein transport Source: InterPro
  • macroautophagy Source: SGD
  • positive regulation of GTPase activity Source: FlyBase
  • regulation of COPII vesicle coating Source: SGD
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34306-MONOMER.
ReactomeiR-SCE-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-SCE-5694530. Cargo concentration in the ER.
R-SCE-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein SEC23
Gene namesi
Name:SEC23
Ordered Locus Names:YPR181C
ORF Names:P9705.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR181C.
SGDiS000006385. SEC23.

Subcellular locationi

GO - Cellular componenti

  • COPII vesicle coat Source: SGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002051451 – 768Protein transport protein SEC23Add BLAST768

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Post-translational modificationi

Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiP15303.
PRIDEiP15303.

PTM databases

iPTMnetiP15303.

Interactioni

Subunit structurei

The COPII coat is composed of at least 7 proteins: the SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein SAR1. Forms two other heterodimeric complexes with SFB3 and PDR17. Interacts with BET1, BET3, BOS1, EMP24, GRH1, SEC16, SEC22 and SYS1.18 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SEC16P484155EBI-16584,EBI-16551
SEC24P404824EBI-16584,EBI-16592
SEC31P389684EBI-16584,EBI-20524
SFB2P539535EBI-16584,EBI-17006

Protein-protein interaction databases

BioGridi36353. 131 interactors.
DIPiDIP-2232N.
IntActiP15303. 36 interactors.
MINTiMINT-540233.

Structurei

Secondary structure

1768
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Beta strandi11 – 22Combined sources12
Helixi23 – 28Combined sources6
Beta strandi33 – 37Combined sources5
Beta strandi48 – 51Combined sources4
Turni59 – 61Combined sources3
Beta strandi69 – 72Combined sources4
Turni73 – 76Combined sources4
Beta strandi77 – 79Combined sources3
Turni81 – 83Combined sources3
Beta strandi86 – 88Combined sources3
Helixi91 – 93Combined sources3
Beta strandi98 – 100Combined sources3
Helixi103 – 105Combined sources3
Beta strandi108 – 113Combined sources6
Beta strandi123 – 129Combined sources7
Helixi134 – 149Combined sources16
Beta strandi156 – 168Combined sources13
Beta strandi172 – 183Combined sources12
Helixi190 – 198Combined sources9
Beta strandi221 – 223Combined sources3
Helixi224 – 227Combined sources4
Beta strandi228 – 230Combined sources3
Helixi231 – 243Combined sources13
Helixi262 – 276Combined sources15
Beta strandi283 – 290Combined sources8
Beta strandi294 – 297Combined sources4
Helixi311 – 315Combined sources5
Helixi322 – 339Combined sources18
Beta strandi342 – 348Combined sources7
Helixi355 – 365Combined sources11
Beta strandi369 – 373Combined sources5
Helixi378 – 386Combined sources9
Beta strandi394 – 397Combined sources4
Beta strandi399 – 408Combined sources10
Beta strandi412 – 420Combined sources9
Beta strandi437 – 439Combined sources3
Beta strandi443 – 450Combined sources8
Beta strandi456 – 462Combined sources7
Beta strandi484 – 495Combined sources12
Turni496 – 498Combined sources3
Beta strandi499 – 512Combined sources14
Helixi517 – 521Combined sources5
Helixi525 – 539Combined sources15
Helixi545 – 563Combined sources19
Beta strandi564 – 567Combined sources4
Helixi571 – 573Combined sources3
Turni578 – 581Combined sources4
Helixi582 – 592Combined sources11
Turni594 – 596Combined sources3
Helixi603 – 613Combined sources11
Helixi618 – 625Combined sources8
Beta strandi628 – 632Combined sources5
Beta strandi634 – 636Combined sources3
Helixi645 – 647Combined sources3
Beta strandi653 – 657Combined sources5
Beta strandi659 – 666Combined sources8
Helixi668 – 676Combined sources9
Helixi678 – 680Combined sources3
Helixi682 – 684Combined sources3
Helixi685 – 703Combined sources19
Beta strandi710 – 715Combined sources6
Helixi719 – 721Combined sources3
Helixi722 – 725Combined sources4
Beta strandi740 – 742Combined sources3
Helixi752 – 763Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2OX-ray2.50A/C1-768[»]
1M2VX-ray2.75A1-768[»]
2QTVX-ray2.50A2-768[»]
4BZIelectron microscopy23.00A/D/G1-768[»]
ProteinModelPortaliP15303.
SMRiP15303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15303.

Family & Domainsi

Sequence similaritiesi

Belongs to the SEC23/SEC24 family. SEC23 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006916.
HOGENOMiHOG000231690.
InParanoidiP15303.
KOiK14006.
OMAiEYITARP.
OrthoDBiEOG092C0WSG.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR006900. Sec23/24_helical_dom.
IPR006896. Sec23/24_trunk_dom.
IPR012990. Sec23_24_beta_S.
IPR002035. VWF_A.
IPR006895. Znf_Sec23_Sec24.
[Graphical view]
PfamiPF00626. Gelsolin. 1 hit.
PF08033. Sec23_BS. 1 hit.
PF04815. Sec23_helical. 1 hit.
PF04811. Sec23_trunk. 1 hit.
PF04810. zf-Sec23_Sec24. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82754. SSF82754. 1 hit.
SSF82919. SSF82919. 1 hit.

Sequencei

Sequence statusi: Complete.

P15303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFETNEDIN GVRFTWNVFP STRSDANSNV VPVGCLYTPL KEYDELNVAP
60 70 80 90 100
YNPVVCSGPH CKSILNPYCV IDPRNSSWSC PICNSRNHLP PQYTNLSQEN
110 120 130 140 150
MPLELQSTTI EYITNKPVTV PPIFFFVVDL TSETENLDSL KESIITSLSL
160 170 180 190 200
LPPNALIGLI TYGNVVQLHD LSSETIDRCN VFRGDREYQL EALTEMLTGQ
210 220 230 240 250
KPTGPGGAAS HLPNAMNKVT PFSLNRFFLP LEQVEFKLNQ LLENLSPDQW
260 270 280 290 300
SVPAGHRPLR ATGSALNIAS LLLQGCYKNI PARIILFASG PGTVAPGLIV
310 320 330 340 350
NSELKDPLRS HHDIDSDHAQ HYKKACKFYN QIAQRVAANG HTVDIFAGCY
360 370 380 390 400
DQIGMSEMKQ LTDSTGGVLL LTDAFSTAIF KQSYLRLFAK DEEGYLKMAF
410 420 430 440 450
NGNMAVKTSK DLKVQGLIGH ASAVKKTDAN NISESEIGIG ATSTWKMASL
460 470 480 490 500
SPYHSYAIFF EIANTAANSN PMMSAPGSAD RPHLAYTQFI TTYQHSSGTN
510 520 530 540 550
RIRVTTVANQ LLPFGTPAIA ASFDQEAAAV LMARIAVHKA ETDDGADVIR
560 570 580 590 600
WLDRTLIKLC QKYADYNKDD PQSFRLAPNF SLYPQFTYYL RRSQFLSVFN
610 620 630 640 650
NSPDETAFYR HIFTREDTTN SLIMIQPTLT SFSMEDDPQP VLLDSISVKP
660 670 680 690 700
NTILLLDTFF FILIYHGEQI AQWRKAGYQD DPQYADFKAL LEEPKLEAAE
710 720 730 740 750
LLVDRFPLPR FIDTEAGGSQ ARFLLSKLNP SDNYQDMARG GSTIVLTDDV
760
SLQNFMTHLQ QVAVSGQA
Length:768
Mass (Da):85,385
Last modified:April 1, 1990 - v1
Checksum:i69811913848265FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15474 Genomic DNA. Translation: CAA33501.1.
U25842 Genomic DNA. Translation: AAB68114.1.
BK006949 Genomic DNA. Translation: DAA11597.1.
PIRiS05742. BVBY23.
RefSeqiNP_015507.1. NM_001184278.1.

Genome annotation databases

EnsemblFungiiYPR181C; YPR181C; YPR181C.
GeneIDi856311.
KEGGisce:YPR181C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15474 Genomic DNA. Translation: CAA33501.1.
U25842 Genomic DNA. Translation: AAB68114.1.
BK006949 Genomic DNA. Translation: DAA11597.1.
PIRiS05742. BVBY23.
RefSeqiNP_015507.1. NM_001184278.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2OX-ray2.50A/C1-768[»]
1M2VX-ray2.75A1-768[»]
2QTVX-ray2.50A2-768[»]
4BZIelectron microscopy23.00A/D/G1-768[»]
ProteinModelPortaliP15303.
SMRiP15303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36353. 131 interactors.
DIPiDIP-2232N.
IntActiP15303. 36 interactors.
MINTiMINT-540233.

PTM databases

iPTMnetiP15303.

Proteomic databases

MaxQBiP15303.
PRIDEiP15303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR181C; YPR181C; YPR181C.
GeneIDi856311.
KEGGisce:YPR181C.

Organism-specific databases

EuPathDBiFungiDB:YPR181C.
SGDiS000006385. SEC23.

Phylogenomic databases

GeneTreeiENSGT00390000006916.
HOGENOMiHOG000231690.
InParanoidiP15303.
KOiK14006.
OMAiEYITARP.
OrthoDBiEOG092C0WSG.

Enzyme and pathway databases

BioCyciYEAST:G3O-34306-MONOMER.
ReactomeiR-SCE-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-SCE-5694530. Cargo concentration in the ER.
R-SCE-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

EvolutionaryTraceiP15303.
PROiP15303.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR006900. Sec23/24_helical_dom.
IPR006896. Sec23/24_trunk_dom.
IPR012990. Sec23_24_beta_S.
IPR002035. VWF_A.
IPR006895. Znf_Sec23_Sec24.
[Graphical view]
PfamiPF00626. Gelsolin. 1 hit.
PF08033. Sec23_BS. 1 hit.
PF04815. Sec23_helical. 1 hit.
PF04811. Sec23_trunk. 1 hit.
PF04810. zf-Sec23_Sec24. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF81811. SSF81811. 1 hit.
SSF82754. SSF82754. 1 hit.
SSF82919. SSF82919. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSEC23_YEAST
AccessioniPrimary (citable) accession number: P15303
Secondary accession number(s): D6W4I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.