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Protein

Protein transport protein SEC24

Gene

SEC24

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. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter.13 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi231Zinc2 Publications1
Metal bindingi234Zinc2 Publications1
Metal bindingi253Zinc2 Publications1
Metal bindingi256Zinc2 Publications1

GO - Molecular functioni

  • signal sequence binding Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cargo loading into COPII-coated vesicle Source: SGD
  • intracellular protein transport Source: InterPro
  • macroautophagy 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-31364-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 SEC24
Alternative name(s):
Abnormal nuclear morphology 1
Gene namesi
Name:SEC24
Synonyms:ANU1
Ordered Locus Names:YIL109C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL109C.
SGDiS000001371. SEC24.

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi230R → A: Abolishes binding to and packaging of cargo protein BET1. 1 Publication1
Mutagenesisi231C → S: Lethal. 1 Publication1
Mutagenesisi235R → A: Abolishes binding to and packaging of cargo protein BET1. 1 Publication1
Mutagenesisi559R → M: Abolishes binding to and packaging of cargo protein BET1. 1 Publication1
Mutagenesisi561R → M: Abolishes binding to and packaging of cargo protein BET1. 1 Publication1
Mutagenesisi616L → W: Abolishes binding to and packaging of cargo protein BET1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002051501 – 926Protein transport protein SEC24Add BLAST926

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei178PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40482.
PRIDEiP40482.

PTM databases

iPTMnetiP40482.

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. Interacts with BET1, EMP24, GRH1, SEC22, SED5 and SYS1.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRH1Q044103EBI-16592,EBI-32083
SEC23P153034EBI-16592,EBI-16584
SEC31P389684EBI-16592,EBI-20524

Protein-protein interaction databases

BioGridi34882. 129 interactors.
DIPiDIP-2233N.
IntActiP40482. 23 interactors.
MINTiMINT-476513.

Structurei

Secondary structure

1926
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi64 – 72Combined sources9
Beta strandi140 – 142Combined sources3
Helixi143 – 145Combined sources3
Helixi151 – 155Combined sources5
Helixi165 – 167Combined sources3
Beta strandi168 – 170Combined sources3
Helixi173 – 175Combined sources3
Turni179 – 181Combined sources3
Beta strandi182 – 192Combined sources11
Helixi193 – 199Combined sources7
Beta strandi204 – 207Combined sources4
Beta strandi212 – 214Combined sources3
Turni232 – 234Combined sources3
Beta strandi243 – 245Combined sources3
Turni246 – 249Combined sources4
Beta strandi250 – 252Combined sources3
Turni254 – 256Combined sources3
Beta strandi259 – 261Combined sources3
Helixi264 – 267Combined sources4
Helixi277 – 279Combined sources3
Helixi281 – 284Combined sources4
Beta strandi286 – 291Combined sources6
Helixi294 – 296Combined sources3
Beta strandi305 – 311Combined sources7
Helixi314 – 319Combined sources6
Helixi321 – 332Combined sources12
Turni333 – 335Combined sources3
Beta strandi344 – 358Combined sources15
Helixi362 – 364Combined sources3
Beta strandi374 – 376Combined sources3
Turni390 – 392Combined sources3
Beta strandi393 – 395Combined sources3
Turni396 – 399Combined sources4
Helixi400 – 413Combined sources14
Turni414 – 416Combined sources3
Helixi424 – 435Combined sources12
Turni436 – 438Combined sources3
Beta strandi440 – 448Combined sources9
Helixi471 – 475Combined sources5
Helixi482 – 492Combined sources11
Beta strandi495 – 505Combined sources11
Helixi509 – 517Combined sources9
Turni518 – 520Combined sources3
Beta strandi523 – 527Combined sources5
Helixi534 – 549Combined sources16
Beta strandi554 – 562Combined sources9
Beta strandi566 – 576Combined sources11
Beta strandi578 – 587Combined sources10
Beta strandi594 – 600Combined sources7
Beta strandi606 – 618Combined sources13
Turni620 – 622Combined sources3
Beta strandi624 – 637Combined sources14
Helixi639 – 644Combined sources6
Helixi648 – 665Combined sources18
Helixi668 – 689Combined sources22
Beta strandi696 – 699Combined sources4
Beta strandi702 – 704Combined sources3
Helixi705 – 707Combined sources3
Helixi710 – 718Combined sources9
Turni721 – 723Combined sources3
Helixi730 – 742Combined sources13
Helixi745 – 752Combined sources8
Beta strandi755 – 758Combined sources4
Turni759 – 761Combined sources3
Helixi791 – 793Combined sources3
Beta strandi799 – 803Combined sources5
Beta strandi805 – 812Combined sources8
Helixi818 – 825Combined sources8
Helixi830 – 832Combined sources3
Helixi847 – 860Combined sources14
Beta strandi870 – 875Combined sources6
Helixi885 – 899Combined sources15
Helixi913 – 923Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2VX-ray2.75B1-926[»]
1PCXX-ray2.50A117-926[»]
1PD0X-ray2.60A117-926[»]
1PD1X-ray2.60A117-926[»]
4BZIelectron microscopy23.00E/F/L/M/N/O1-926[»]
ProteinModelPortaliP40482.
SMRiP40482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40482.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni231 – 256Zinc finger-likeAdd BLAST26

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi110 – 114Poly-Gln5
Compositional biasi157 – 160Poly-Pro4

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00590000082962.
HOGENOMiHOG000196365.
InParanoidiP40482.
KOiK14007.
OMAiIMRVRAS.
OrthoDBiEOG092C0DKG.

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.

P40482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHHKKRVYP QAQLQYGQNA TPLQQPAQFM PPQDPAAAGM SYGQMGMPPQ
60 70 80 90 100
GAVPSMGQQQ FLTPAQEQLH QQIDQATTSM NDMHLHNVPL VDPNAYMQPQ
110 120 130 140 150
VPVQMGTPLQ QQQQPMAAPA YGQPSAAMGQ NMRPMNQLYP IDLLTELPPP
160 170 180 190 200
ITDLTLPPPP LVIPPERMLV PSELSNASPD YIRSTLNAVP KNSSLLKKSK
210 220 230 240 250
LPFGLVIRPY QHLYDDIDPP PLNEDGLIVR CRRCRSYMNP FVTFIEQGRR
260 270 280 290 300
WRCNFCRLAN DVPMQMDQSD PNDPKSRYDR NEIKCAVMEY MAPKEYTLRQ
310 320 330 340 350
PPPATYCFLI DVSQSSIKSG LLATTINTLL QNLDSIPNHD ERTRISILCV
360 370 380 390 400
DNAIHYFKIP LDSENNEESA DQINMMDIAD LEEPFLPRPN SMVVSLKACR
410 420 430 440 450
QNIETLLTKI PQIFQSNLIT NFALGPALKS AYHLIGGVGG KIIVVSGTLP
460 470 480 490 500
NLGIGKLQRR NESGVVNTSK ETAQLLSCQD SFYKNFTIDC SKVQITVDLF
510 520 530 540 550
LASEDYMDVA SLSNLSRFTA GQTHFYPGFS GKNPNDIVKF STEFAKHISM
560 570 580 590 600
DFCMETVMRA RGSTGLRMSR FYGHFFNRSS DLCAFSTMPR DQSYLFEVNV
610 620 630 640 650
DESIMADYCY VQVAVLLSLN NSQRRIRIIT LAMPTTESLA EVYASADQLA
660 670 680 690 700
IASFYNSKAV EKALNSSLDD ARVLINKSVQ DILATYKKEI VVSNTAGGAP
710 720 730 740 750
LRLCANLRMF PLLMHSLTKH MAFRSGIVPS DHRASALNNL ESLPLKYLIK
760 770 780 790 800
NIYPDVYSLH DMADEAGLPV QTEDGEATGT IVLPQPINAT SSLFERYGLY
810 820 830 840 850
LIDNGNELFL WMGGDAVPAL VFDVFGTQDI FDIPIGKQEI PVVENSEFNQ
860 870 880 890 900
RVRNIINQLR NHDDVITYQS LYIVRGASLS EPVNHASARE VATLRLWASS
910 920
TLVEDKILNN ESYREFLQIM KARISK
Length:926
Mass (Da):103,636
Last modified:February 1, 1995 - v1
Checksum:i35E2BDD24CC75899
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38125 Genomic DNA. Translation: CAA86271.1.
AY692888 Genomic DNA. Translation: AAT92907.1.
BK006942 Genomic DNA. Translation: DAA08444.1.
PIRiS48463.
RefSeqiNP_012157.3. NM_001179457.3.

Genome annotation databases

EnsemblFungiiYIL109C; YIL109C; YIL109C.
GeneIDi854697.
KEGGisce:YIL109C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38125 Genomic DNA. Translation: CAA86271.1.
AY692888 Genomic DNA. Translation: AAT92907.1.
BK006942 Genomic DNA. Translation: DAA08444.1.
PIRiS48463.
RefSeqiNP_012157.3. NM_001179457.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M2VX-ray2.75B1-926[»]
1PCXX-ray2.50A117-926[»]
1PD0X-ray2.60A117-926[»]
1PD1X-ray2.60A117-926[»]
4BZIelectron microscopy23.00E/F/L/M/N/O1-926[»]
ProteinModelPortaliP40482.
SMRiP40482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34882. 129 interactors.
DIPiDIP-2233N.
IntActiP40482. 23 interactors.
MINTiMINT-476513.

PTM databases

iPTMnetiP40482.

Proteomic databases

MaxQBiP40482.
PRIDEiP40482.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL109C; YIL109C; YIL109C.
GeneIDi854697.
KEGGisce:YIL109C.

Organism-specific databases

EuPathDBiFungiDB:YIL109C.
SGDiS000001371. SEC24.

Phylogenomic databases

GeneTreeiENSGT00590000082962.
HOGENOMiHOG000196365.
InParanoidiP40482.
KOiK14007.
OMAiIMRVRAS.
OrthoDBiEOG092C0DKG.

Enzyme and pathway databases

BioCyciYEAST:G3O-31364-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

EvolutionaryTraceiP40482.
PROiP40482.

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 nameiSEC24_YEAST
AccessioniPrimary (citable) accession number: P40482
Secondary accession number(s): D6VVH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 156 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, Direct protein sequencing, 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: 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.