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P38968 (SEC31_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein transport protein SEC31
Alternative name(s):
Protein WEB1
Gene names
Name:SEC31
Synonyms:WEB1
Ordered Locus Names:YDL195W
ORF Names:D1229
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1273 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.8 Ref.9 Ref.12 Ref.26

Subunit structure

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. Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.27

Subcellular location

Cytoplasmic vesicleCOPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Ref.5 Ref.10 Ref.12 Ref.22 Ref.24.

Miscellaneous

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

Sequence similarities

Belongs to the WD repeat SEC31 family.

Contains 8 WD repeats.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12731273Protein transport protein SEC31
PRO_0000051436

Regions

Repeat6 – 4641WD 1
Repeat60 – 9940WD 2
Repeat106 – 14641WD 3
Repeat158 – 19841WD 4
Repeat207 – 25044WD 5
Repeat255 – 29541WD 6
Repeat298 – 33841WD 7
Repeat385 – 40521WD 8; interaction with SEC13
Compositional bias773 – 1149377Pro-rich

Amino acid modifications

Modified residue3491Phosphoserine Ref.17 Ref.18
Modified residue8361Phosphoserine Ref.17
Modified residue9741Phosphoserine Ref.18
Modified residue9771Phosphoserine Ref.18
Modified residue9801Phosphoserine Ref.17 Ref.18
Modified residue9881Phosphoserine Ref.18
Modified residue9921Phosphoserine Ref.16 Ref.17 Ref.18
Modified residue9991Phosphoserine Ref.16 Ref.17 Ref.18
Modified residue10501Phosphothreonine Ref.15 Ref.16 Ref.17 Ref.18
Modified residue10531Phosphoserine Ref.16 Ref.17

Experimental info

Sequence conflict3171A → T in AAA50367. Ref.1
Sequence conflict3671T → S in CAA58252. Ref.2
Sequence conflict3671T → S in CAA98772. Ref.3
Sequence conflict6911S → N in AAA50367. Ref.1
Sequence conflict7541A → V in AAA50367. Ref.1
Sequence conflict8771T → A in AAA50367. Ref.1

Secondary structure

.......................................................................................................................... 1273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38968 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 87F192E4B10E7571

FASTA1,273138,717
        10         20         30         40         50         60 
MVKLAEFSRT ATFAWSHDKI PLLVSGTVSG TVDANFSTDS SLELWSLLAA DSEKPIASLQ 

        70         80         90        100        110        120 
VDSKFNDLDW SHNNKIIAGA LDNGSLELYS TNEANNAINS MARFSNHSSS VKTVKFNAKQ 

       130        140        150        160        170        180 
DNVLASGGNN GEIFIWDMNK CTESPSNYTP LTPGQSMSSV DEVISLAWNQ SLAHVFASAG 

       190        200        210        220        230        240 
SSNFASIWDL KAKKEVIHLS YTSPNSGIKQ QLSVVEWHPK NSTRVATATG SDNDPSILIW 

       250        260        270        280        290        300 
DLRNANTPLQ TLNQGHQKGI LSLDWCHQDE HLLLSSGRDN TVLLWNPESA EQLSQFPARG 

       310        320        330        340        350        360 
NWCFKTKFAP EAPDLFACAS FDNKIEVQTL QNLTNTLDEQ ETETKQQESE TDFWNNVSRE 

       370        380        390        400        410        420 
ESKEKPTVFH LQAPTWYGEP SPAAHWAFGG KLVQITPDGK GVSITNPKIS GLESNTTLSE 

       430        440        450        460        470        480 
ALKTKDFKPL INQRLVKVID DVNEEDWNLL EKLSMDGTEE FLKEALAFDN DESDAQDDAN 

       490        500        510        520        530        540 
NEKEDDGEEF FQQIETNFQP EGDFSLSGNI EQTISKNLVS GNIKSAVKNS LENDLLMEAM 

       550        560        570        580        590        600 
VIALDSNNER LKESVKNAYF AKYGSKSSLS RILYSISKRE VDDLVENLDV SQWKFISKAI 

       610        620        630        640        650        660 
QNLYPNDIAQ RNEMLIKLGD RLKENGHRQD SLTLYLAAGS LDKVASIWLS EFPDLEDKLK 

       670        680        690        700        710        720 
KDNKTIYEAH SECLTEFIER FTVFSNFING SSTINNEQLI AKFLEFINLT TSTGNFELAT 

       730        740        750        760        770        780 
EFLNSLPSDN EEVKTEKARV LIASGKSLPA QNPATATTSK AKYTNAKTNK NVPVLPTPGM 

       790        800        810        820        830        840 
PSTTSIPSMQ APFYGMTPGA SANALPPKPY VPATTTSAPV HTEGKYAPPS QPSMASPFVN 

       850        860        870        880        890        900 
KTNSSTRLNS FAPPPNPYAT ATVPATNVST TSIPQNTFAP IQPGMPIMGD YNAQSSSIPS 

       910        920        930        940        950        960 
QPPINAVSGQ TPHLNRKAND GWNDLPLKVK EKPSRAKAVS VAPPNILSTP TPLNGIPANA 

       970        980        990       1000       1010       1020 
ASTMPPPPLS RAPSSVSMVS PPPLHKNSRV PSLVATSESP RASISNPYAP PQSSQQFPIG 

      1030       1040       1050       1060       1070       1080 
TISTANQTSN TAQVASSNPY APPPQQRVAT PLSGGVPPAP LPKASNPYAP TATTQPNGSS 

      1090       1100       1110       1120       1130       1140 
YPPTGPYTNN HTMTSPPPVF NKPPTGPPPI SMKKRSNKLA SIEQNPSQGA TYPPTLSSSA 

      1150       1160       1170       1180       1190       1200 
SPLQPSQPPT LASQVNTSAE NVSHEIPADQ QPIVDFLKEE LARVTPLTPK EYSKQLKDCD 

      1210       1220       1230       1240       1250       1260 
KRLKILFYHL EKQDLLTQPT IDCLHDLVAL MKEKKYKEAM VIHANIATNH AQEGGNWLTG 

      1270 
VKRLIGIAEA TLN 

« Hide

References

« Hide 'large scale' references
[1]"Suppression of mutations in two Saccharomyces cerevisiae genes by the adenovirus E1A protein."
Zieler H.A., Walberg M., Berg P.
Mol. Cell. Biol. 15:3227-3237(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / SNY243.
[2]"The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast chromosome IV reveals the location of five known genes and characterizes at least six new open reading frames including putative genes for ribosomal protein L35 and a sugar transport protein."
Verhasselt P., Voet M., Mathys J., Volckaert G.
Yeast 12:1065-1070(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 367.
Strain: ATCC 204508 / S288c.
[5]"COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast."
Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A., Schekman R.W., Orci L.
Cell 83:1183-1196(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex."
Wuestehube L.J., Duden R., Eun A., Hamamoto S., Korn P., Ram R., Schekman R.W.
Genetics 142:393-406(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"COPII subunit interactions in the assembly of the vesicle coat."
Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.
J. Biol. Chem. 272:25413-25416(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE COPII COAT, INTERACTION WITH SEC16.
[8]"Sec31 encodes an essential component of the COPII coat required for transport vesicle budding from the endoplasmic reticulum."
Salama N.R., Chuang J.S., Schekman R.W.
Mol. Biol. Cell 8:205-217(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH SEC13.
[9]"Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles."
Campbell J.L., Schekman R.W.
Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes."
Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S., Schekman R.W., Yeung T.
Cell 93:263-275(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[11]"Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles."
Gilstring C.F., Melin-Larsson M., Ljungdahl P.O.
Mol. Biol. Cell 10:3549-3565(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHR3.
[12]"The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting."
Matsuoka K., Schekman R.W.
Methods 20:417-428(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex."
Belden W.J., Barlowe C.
J. Biol. Chem. 276:43040-43048(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EMP24 AND ERV25.
[14]"Dynamics of the COPII coat with GTP and stable analogues."
Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
Nat. Cell Biol. 3:531-537(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE COPII COAT.
[15]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1050, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[16]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-999; THR-1050 AND SER-1053, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[17]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-836; SER-980; SER-992; SER-999; THR-1050 AND SER-1053, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-974; SER-977; SER-980; SER-988; SER-992; SER-999 AND THR-1050, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Structure of the Sec23p/24p and Sec13p/31p complexes of COPII."
Lederkremer G.Z., Cheng Y., Petre B.M., Vogan E., Springer S., Schekman R.W., Walz T., Kirchhausen T.
Proc. Natl. Acad. Sci. U.S.A. 98:10704-10709(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
[21]"Surface structure of the COPII-coated vesicle."
Matsuoka K., Schekman R.W., Orci L., Heuser J.E.
Proc. Natl. Acad. Sci. U.S.A. 98:13705-13709(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
[22]"Sec16p potentiates the action of COPII proteins to bud transport vesicles."
Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
J. Cell Biol. 158:1029-1038(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[23]"Self-assembly of minimal COPII cages."
Antonny B., Gounon P., Schekman R.W., Orci L.
EMBO Rep. 4:419-424(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF THE COPII COMPLEX.
[24]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[25]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[26]"Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting."
Sato K., Nakano A.
J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: COPII COMPLEX ASSEMBLY, FUNCTION OF THE COPII COMPLEX.
[27]"Structure and organization of coat proteins in the COPII cage."
Fath S., Mancias J.D., Bi X., Goldberg J.
Cell 129:1325-1336(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-763 IN COMPLEX WITH SEC13, SUBUNIT.
[28]"Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31."
Bi X., Mancias J.D., Goldberg J.
Dev. Cell 13:635-645(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 899-947 IN COMPLEX WITH SEC23 AND SAR1.
[29]"Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat."
Whittle J.R., Schwartz T.U.
J. Cell Biol. 190:347-361(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 370-746 IN COMPLEX WITH SEC13.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15219 Genomic DNA. Translation: AAA50367.1.
X83276 Genomic DNA. Translation: CAA58252.1.
Z74243 Genomic DNA. Translation: CAA98772.1.
BK006938 Genomic DNA. Translation: DAA11668.2.
PIRS58782.
RefSeqNP_010086.2. NM_001180255.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP38968.
SMRP38968. Positions 5-745, 907-942.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31850. 65 interactions.
DIPDIP-4792N.
IntActP38968. 51 interactions.
MINTMINT-567140.
STRING4932.YDL195W.

Proteomic databases

PaxDbP38968.
PeptideAtlasP38968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL195W; YDL195W; YDL195W.
GeneID851332.
KEGGsce:YDL195W.

Organism-specific databases

CYGDYDL195w.
SGDS000002354. SEC31.

Phylogenomic databases

eggNOGNOG248389.
GeneTreeENSGT00390000003175.
HOGENOMHOG000048339.
KOK14005.
OMACSGNIEK.
OrthoDBEOG79GTFQ.

Enzyme and pathway databases

BioCycYEAST:G3O-29580-MONOMER.

Gene expression databases

GenevestigatorP38968.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR021614. 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]
PfamPF11549. Sec31. 1 hit.
PF07304. SRA1. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38968.
NextBio968393.
PROP38968.

Entry information

Entry nameSEC31_YEAST
AccessionPrimary (citable) accession number: P38968
Secondary accession number(s): D6VRF8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references