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Protein

Protein transport protein SEC31

Gene

SEC31

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.6 Publications

GO - Molecular functioni

  • structural molecule activity Source: SGD

GO - Biological processi

  • COPII-coated vesicle budding Source: SGD
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29580-MONOMER.
ReactomeiR-SCE-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein SEC31
Alternative name(s):
Protein WEB1
Gene namesi
Name:SEC31
Synonyms:WEB1
Ordered Locus Names:YDL195W
ORF Names:D1229
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL195W.
SGDiS000002354. SEC31.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000514361 – 1273Protein transport protein SEC31Add BLAST1273

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei349PhosphoserineCombined sources1
Modified residuei836PhosphoserineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei977PhosphoserineCombined sources1
Modified residuei980PhosphoserineCombined sources1
Modified residuei988PhosphoserineCombined sources1
Modified residuei992PhosphoserineCombined sources1
Modified residuei999PhosphoserineCombined sources1
Modified residuei1050PhosphothreonineCombined sources1
Modified residuei1053PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38968.
PRIDEiP38968.

PTM databases

iPTMnetiP38968.

Interactioni

Subunit structurei

The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13. Interacts with EMP24, ERV25, SEC16 and SHR3.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SEC13Q044918EBI-20524,EBI-16529
SEC16P484153EBI-20524,EBI-16551
SEC23P153034EBI-20524,EBI-16584
SEC24P404824EBI-20524,EBI-16592

Protein-protein interaction databases

BioGridi31850. 69 interactors.
DIPiDIP-4792N.
IntActiP38968. 51 interactors.
MINTiMINT-567140.

Structurei

Secondary structure

11273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi17 – 20Combined sources4
Beta strandi22 – 26Combined sources5
Beta strandi28 – 30Combined sources3
Beta strandi43 – 49Combined sources7
Helixi50 – 52Combined sources3
Beta strandi65 – 70Combined sources6
Beta strandi72 – 75Combined sources4
Beta strandi77 – 84Combined sources8
Beta strandi86 – 89Combined sources4
Beta strandi100 – 103Combined sources4
Beta strandi107 – 109Combined sources3
Beta strandi113 – 116Combined sources4
Beta strandi118 – 120Combined sources3
Beta strandi123 – 127Combined sources5
Beta strandi129 – 131Combined sources3
Beta strandi133 – 135Combined sources3
Turni138 – 141Combined sources4
Turni145 – 147Combined sources3
Beta strandi165 – 168Combined sources4
Beta strandi175 – 183Combined sources9
Beta strandi185 – 189Combined sources5
Turni190 – 193Combined sources4
Beta strandi194 – 199Combined sources6
Beta strandi212 – 217Combined sources6
Beta strandi224 – 229Combined sources6
Beta strandi232 – 234Combined sources3
Beta strandi239 – 241Combined sources3
Beta strandi260 – 265Combined sources6
Beta strandi273 – 285Combined sources13
Beta strandi287 – 289Combined sources3
Beta strandi292 – 297Combined sources6
Beta strandi299 – 301Combined sources3
Beta strandi306 – 308Combined sources3
Beta strandi315 – 318Combined sources4
Beta strandi321 – 330Combined sources10
Beta strandi385 – 387Combined sources3
Turni388 – 390Combined sources3
Beta strandi391 – 395Combined sources5
Beta strandi402 – 405Combined sources4
Helixi416 – 424Combined sources9
Helixi428 – 436Combined sources9
Helixi441 – 456Combined sources16
Helixi458 – 466Combined sources9
Helixi509 – 519Combined sources11
Helixi523 – 531Combined sources9
Turni532 – 534Combined sources3
Helixi536 – 543Combined sources8
Helixi549 – 563Combined sources15
Helixi568 – 577Combined sources10
Helixi582 – 587Combined sources6
Helixi590 – 592Combined sources3
Helixi593 – 603Combined sources11
Helixi608 – 623Combined sources16
Turni624 – 626Combined sources3
Helixi628 – 637Combined sources10
Helixi641 – 650Combined sources10
Helixi652 – 661Combined sources10
Helixi666 – 685Combined sources20
Helixi697 – 711Combined sources15
Turni712 – 714Combined sources3
Helixi716 – 725Combined sources10
Helixi731 – 744Combined sources14
Beta strandi909 – 911Combined sources3
Helixi916 – 919Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PM6X-ray2.45A/C370-763[»]
2PM7X-ray2.35A/C370-763[»]
2PM9X-ray3.30A1-411[»]
2QTVX-ray2.50D899-947[»]
3MZLX-ray2.80B/D/F/H370-746[»]
4BZJelectron microscopy40.00A/C1-1273[»]
4BZKelectron microscopy40.00A/C1-1273[»]
ProteinModelPortaliP38968.
SMRiP38968.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38968.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati6 – 46WD 1Add BLAST41
Repeati60 – 99WD 2Add BLAST40
Repeati106 – 146WD 3Add BLAST41
Repeati158 – 198WD 4Add BLAST41
Repeati207 – 250WD 5Add BLAST44
Repeati255 – 295WD 6Add BLAST41
Repeati298 – 338WD 7Add BLAST41
Repeati385 – 405WD 8; interaction with SEC13Add BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi773 – 1149Pro-richAdd BLAST377

Sequence similaritiesi

Belongs to the WD repeat SEC31 family.Curated
Contains 8 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00390000003175.
HOGENOMiHOG000048339.
InParanoidiP38968.
KOiK14005.
OMAiGAPNAYY.
OrthoDBiEOG092C0AD5.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024298. ACE1_Sec16_Sec31.
IPR021614. Sec31.
IPR009917. SRA1-protein/COPII_Sec31.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12931. Sec16_C. 1 hit.
PF11549. Sec31. 1 hit.
PF07304. SRA1. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38968-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLAEFSRT ATFAWSHDKI PLLVSGTVSG TVDANFSTDS SLELWSLLAA
60 70 80 90 100
DSEKPIASLQ VDSKFNDLDW SHNNKIIAGA LDNGSLELYS TNEANNAINS
110 120 130 140 150
MARFSNHSSS VKTVKFNAKQ DNVLASGGNN GEIFIWDMNK CTESPSNYTP
160 170 180 190 200
LTPGQSMSSV DEVISLAWNQ SLAHVFASAG SSNFASIWDL KAKKEVIHLS
210 220 230 240 250
YTSPNSGIKQ QLSVVEWHPK NSTRVATATG SDNDPSILIW DLRNANTPLQ
260 270 280 290 300
TLNQGHQKGI LSLDWCHQDE HLLLSSGRDN TVLLWNPESA EQLSQFPARG
310 320 330 340 350
NWCFKTKFAP EAPDLFACAS FDNKIEVQTL QNLTNTLDEQ ETETKQQESE
360 370 380 390 400
TDFWNNVSRE ESKEKPTVFH LQAPTWYGEP SPAAHWAFGG KLVQITPDGK
410 420 430 440 450
GVSITNPKIS GLESNTTLSE ALKTKDFKPL INQRLVKVID DVNEEDWNLL
460 470 480 490 500
EKLSMDGTEE FLKEALAFDN DESDAQDDAN NEKEDDGEEF FQQIETNFQP
510 520 530 540 550
EGDFSLSGNI EQTISKNLVS GNIKSAVKNS LENDLLMEAM VIALDSNNER
560 570 580 590 600
LKESVKNAYF AKYGSKSSLS RILYSISKRE VDDLVENLDV SQWKFISKAI
610 620 630 640 650
QNLYPNDIAQ RNEMLIKLGD RLKENGHRQD SLTLYLAAGS LDKVASIWLS
660 670 680 690 700
EFPDLEDKLK KDNKTIYEAH SECLTEFIER FTVFSNFING SSTINNEQLI
710 720 730 740 750
AKFLEFINLT TSTGNFELAT EFLNSLPSDN EEVKTEKARV LIASGKSLPA
760 770 780 790 800
QNPATATTSK AKYTNAKTNK NVPVLPTPGM PSTTSIPSMQ APFYGMTPGA
810 820 830 840 850
SANALPPKPY VPATTTSAPV HTEGKYAPPS QPSMASPFVN KTNSSTRLNS
860 870 880 890 900
FAPPPNPYAT ATVPATNVST TSIPQNTFAP IQPGMPIMGD YNAQSSSIPS
910 920 930 940 950
QPPINAVSGQ TPHLNRKAND GWNDLPLKVK EKPSRAKAVS VAPPNILSTP
960 970 980 990 1000
TPLNGIPANA ASTMPPPPLS RAPSSVSMVS PPPLHKNSRV PSLVATSESP
1010 1020 1030 1040 1050
RASISNPYAP PQSSQQFPIG TISTANQTSN TAQVASSNPY APPPQQRVAT
1060 1070 1080 1090 1100
PLSGGVPPAP LPKASNPYAP TATTQPNGSS YPPTGPYTNN HTMTSPPPVF
1110 1120 1130 1140 1150
NKPPTGPPPI SMKKRSNKLA SIEQNPSQGA TYPPTLSSSA SPLQPSQPPT
1160 1170 1180 1190 1200
LASQVNTSAE NVSHEIPADQ QPIVDFLKEE LARVTPLTPK EYSKQLKDCD
1210 1220 1230 1240 1250
KRLKILFYHL EKQDLLTQPT IDCLHDLVAL MKEKKYKEAM VIHANIATNH
1260 1270
AQEGGNWLTG VKRLIGIAEA TLN
Length:1,273
Mass (Da):138,717
Last modified:July 27, 2011 - v3
Checksum:i87F192E4B10E7571
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti317A → T in AAA50367 (PubMed:7760818).Curated1
Sequence conflicti367T → S in CAA58252 (PubMed:8896272).Curated1
Sequence conflicti367T → S in CAA98772 (PubMed:9169867).Curated1
Sequence conflicti691S → N in AAA50367 (PubMed:7760818).Curated1
Sequence conflicti754A → V in AAA50367 (PubMed:7760818).Curated1
Sequence conflicti877T → A in AAA50367 (PubMed:7760818).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15219 Genomic DNA. Translation: AAA50367.1.
X83276 Genomic DNA. Translation: CAA58252.1.
Z74243 Genomic DNA. Translation: CAA98772.1.
BK006938 Genomic DNA. Translation: DAA11668.2.
PIRiS58782.
RefSeqiNP_010086.2. NM_001180255.2.

Genome annotation databases

EnsemblFungiiYDL195W; YDL195W; YDL195W.
GeneIDi851332.
KEGGisce:YDL195W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15219 Genomic DNA. Translation: AAA50367.1.
X83276 Genomic DNA. Translation: CAA58252.1.
Z74243 Genomic DNA. Translation: CAA98772.1.
BK006938 Genomic DNA. Translation: DAA11668.2.
PIRiS58782.
RefSeqiNP_010086.2. NM_001180255.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PM6X-ray2.45A/C370-763[»]
2PM7X-ray2.35A/C370-763[»]
2PM9X-ray3.30A1-411[»]
2QTVX-ray2.50D899-947[»]
3MZLX-ray2.80B/D/F/H370-746[»]
4BZJelectron microscopy40.00A/C1-1273[»]
4BZKelectron microscopy40.00A/C1-1273[»]
ProteinModelPortaliP38968.
SMRiP38968.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31850. 69 interactors.
DIPiDIP-4792N.
IntActiP38968. 51 interactors.
MINTiMINT-567140.

PTM databases

iPTMnetiP38968.

Proteomic databases

MaxQBiP38968.
PRIDEiP38968.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL195W; YDL195W; YDL195W.
GeneIDi851332.
KEGGisce:YDL195W.

Organism-specific databases

EuPathDBiFungiDB:YDL195W.
SGDiS000002354. SEC31.

Phylogenomic databases

GeneTreeiENSGT00390000003175.
HOGENOMiHOG000048339.
InParanoidiP38968.
KOiK14005.
OMAiGAPNAYY.
OrthoDBiEOG092C0AD5.

Enzyme and pathway databases

BioCyciYEAST:G3O-29580-MONOMER.
ReactomeiR-SCE-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.

Miscellaneous databases

EvolutionaryTraceiP38968.
PROiP38968.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR024298. ACE1_Sec16_Sec31.
IPR021614. Sec31.
IPR009917. SRA1-protein/COPII_Sec31.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12931. Sec16_C. 1 hit.
PF11549. Sec31. 1 hit.
PF07304. SRA1. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSEC31_YEAST
AccessioniPrimary (citable) accession number: P38968
Secondary accession number(s): D6VRF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1840 molecules/cell in log phase SD medium.1 Publication

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.