P38968 (SEC31_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein transport protein SEC31

Alternative name(s):
Protein WEB1

Gene names

Name:	SEC31
Synonyms:	WEB1
Ordered Locus Names:	YDL195W
ORF Names:	D1229

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1273 AA.
Sequence status	Complete.
Protein existence	Evidence 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.24
Subunit structure	The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Interacts with SEC13, EMP24, ERV25, SEC16 and SHR3. Ref.7 Ref.8 Ref.10 Ref.11 Ref.13
Subcellular location	Cytoplasmic vesicle › COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Ref.5 Ref.10 Ref.12 Ref.19 Ref.22.
Miscellaneous	Present with 1840 molecules/cell in log phase SD medium. Ref.23
Sequence similarities	Belongs to the WD repeat SEC31 family. Contains 8 WD repeats.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasmic vesicle Endoplasmic reticulum Membrane
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	COPII-coated vesicle budding Inferred from direct assay. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	COPII vesicle coat Inferred from direct assay. Source: SGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mating projection tip Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction Ref.7. Source: IntAct structural molecule activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEC13	Q04491	9	EBI-20524,EBI-16529
SEC16	P48415	3	EBI-20524,EBI-16551
SEC23	P15303	4	EBI-20524,EBI-16584
SEC24	P40482	4	EBI-20524,EBI-16592

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1273

1273

Protein transport protein SEC31

PRO_0000051436

Regions

Repeat

6 – 46

41

WD 1

Repeat

60 – 99

40

WD 2

Repeat

106 – 146

41

WD 3

Repeat

158 – 198

41

WD 4

Repeat

207 – 250

44

WD 5

Repeat

255 – 295

41

WD 6

Repeat

298 – 338

41

WD 7

Repeat

617 – 658

42

WD 8

Compositional bias

773 – 1149

377

Pro-rich

Amino acid modifications

Modified residue

349

1

Phosphoserine Ref.16

Modified residue

396

1

Phosphothreonine Ref.16 Ref.25

Modified residue

414

1

Phosphoserine Ref.16

Modified residue

728

1

Phosphoserine Ref.16

Modified residue

830

1

Phosphoserine Ref.16

Modified residue

836

1

Phosphoserine Ref.16 Ref.25

Modified residue

844

1

Phosphoserine Ref.15

Modified residue

974

1

Phosphoserine Ref.15 Ref.16 Ref.20

Modified residue

975

1

Phosphoserine Ref.15 Ref.16

Modified residue

977

1

Phosphoserine Ref.16 Ref.20

Modified residue

980

1

Phosphoserine Ref.16 Ref.20

Modified residue

992

1

Phosphoserine Ref.16 Ref.20 Ref.26

Modified residue

996

1

Phosphothreonine Ref.16

Modified residue

997

1

Phosphoserine Ref.16

Modified residue

999

1

Phosphoserine Ref.16 Ref.20 Ref.25 Ref.26

Modified residue

1050

1

Phosphothreonine Ref.16 Ref.25 Ref.26

Modified residue

1053

1

Phosphoserine Ref.16 Ref.26

Modified residue

1157

1

Phosphothreonine Ref.16

Modified residue

1158

1

Phosphoserine Ref.16

Experimental info

Sequence conflict

317

1

A → T in AAA50367. Ref.1

Sequence conflict

367

1

T → S in CAA58252. Ref.2

Sequence conflict

367

1

T → S in CAA98772. Ref.3

Sequence conflict

691

1

S → N in AAA50367. Ref.1

Sequence conflict

754

1

A → V in AAA50367. Ref.1

Sequence conflict

877

1

T → A in AAA50367. Ref.1

Secondary structure

1

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1273

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Beta strand

17 – 20

4

Beta strand

22 – 26

5

Beta strand

28 – 30

3

Beta strand

43 – 49

7

Helix

50 – 52

3

Beta strand

65 – 70

6

Beta strand

72 – 75

4

Beta strand

77 – 84

8

Beta strand

86 – 89

4

Beta strand

100 – 103

4

Beta strand

107 – 109

3

Beta strand

113 – 116

4

Beta strand

118 – 120

3

Beta strand

123 – 127

5

Beta strand

129 – 131

3

Beta strand

133 – 135

3

Turn

138 – 141

4

Turn

145 – 147

3

Beta strand

165 – 168

4

Beta strand

175 – 183

9

Beta strand

185 – 189

5

Turn

190 – 193

4

Beta strand

194 – 199

6

Beta strand

212 – 217

6

Beta strand

224 – 229

6

Beta strand

232 – 234

3

Beta strand

239 – 241

3

Beta strand

260 – 265

6

Beta strand

273 – 285

13

Beta strand

287 – 289

3

Beta strand

292 – 297

6

Beta strand

299 – 301

3

Beta strand

306 – 308

3

Beta strand

315 – 318

4

Beta strand

321 – 330

10

Beta strand

385 – 387

3

Helix

388 – 390

3

Beta strand

391 – 395

5

Beta strand

402 – 405

4

Helix

416 – 424

9

Helix

428 – 436

9

Helix

441 – 456

16

Helix

458 – 466

9

Helix

509 – 519

11

Helix

523 – 531

9

Turn

532 – 534

3

Helix

536 – 543

8

Helix

551 – 554

4

Helix

556 – 560

5

Turn

561 – 566

6

Helix

568 – 577

10

Helix

582 – 587

6

Helix

590 – 592

3

Helix

593 – 603

11

Helix

608 – 623

16

Turn

624 – 626

3

Helix

628 – 638

11

Helix

641 – 650

10

Helix

652 – 660

9

Turn

661 – 663

3

Helix

666 – 685

20

Helix

697 – 711

15

Turn

712 – 714

3

Helix

716 – 725

10

Helix

731 – 744

14

Beta strand

909 – 911

3

Helix

916 – 919

4

Sequences

	Sequence		Length	Mass (Da)
	P38968 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 87F192E4B10E7571	FASTA	1,273	138,717
	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

References

	« Hide 'large scale' referencesShow '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: 7760818] [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: 8896272] [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. , 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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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: 8548805] [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: 8852839] [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: 9325247] [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: 9190202] [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: 9023343] [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: 9568718] [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: 10564255] [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: 10720463] [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: 11560939] [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: 11389436] [Abstract] Cited for: IDENTIFICATION IN THE COPII COAT.
[15]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844; SER-974 AND SER-975, MASS SPECTROMETRY.
[16]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; THR-396; SER-414; SER-728; SER-830; SER-836; SER-974; SER-975; SER-977; SER-980; SER-992; THR-996; SER-997; SER-999; THR-1050; SER-1053; THR-1157 AND SER-1158, MASS SPECTROMETRY.
[17]	"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: 11535824] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
[18]	"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: 11717432] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE SEC13/31 COMPLEX.
[19]	"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: 12235121] [Abstract] Cited for: SUBCELLULAR LOCATION.
[20]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-977; SER-980; SER-992 AND SER-999, MASS SPECTROMETRY. Strain: 2124.
[21]	"Self-assembly of minimal COPII cages." Antonny B., Gounon P., Schekman R.W., Orci L. EMBO Rep. 4:419-424(2003) [PubMed: 12671686] [Abstract] Cited for: STRUCTURE OF THE COPII COMPLEX.
[22]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[23]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[24]	"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: 14627716] [Abstract] Cited for: COPII COMPLEX ASSEMBLY, FUNCTION OF THE COPII COMPLEX.
[25]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-396; SER-836; SER-999 AND THR-1050, MASS SPECTROMETRY. Strain: YAL6B.
[26]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-999; THR-1050 AND SER-1053, MASS SPECTROMETRY. Strain: ADR376.
+	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.

PIR

S58782.

RefSeq

NP_010086.2. NM_001180255.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PM6	X-ray	2.45	A/C	370-763	[»]
2PM7	X-ray	2.35	A/C	370-763	[»]
2PM9	X-ray	3.30	A	1-411	[»]
2QTV	X-ray	2.50	D	899-947	[»]
3MZL	X-ray	2.80	B/D/F/H	370-746	[»]

ProteinModelPortal

P38968.

SMR

P38968. Positions 5-745, 907-942.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4792N.

IntAct

P38968. 53 interactions.

MINT

MINT-567140.

STRING

P38968.

Proteomic databases

PeptideAtlas

P38968.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

851332.

KEGG

sce:YDL195W.

NMPDR

fig|4932.3.peg.819.

Organism-specific databases

CYGD

YDL195w.

SGD

S000002354. SEC31.

Phylogenomic databases

eggNOG

fuNOG04878.

GeneTree

EFGT00050000000088.

HOGENOM

HBG735654.

OMA

NGEDFFN.

OrthoDB

EOG4RR9RS.

Gene expression databases

ArrayExpress

P38968.

Genevestigator

P38968.

GermOnline

YDL195W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR021614. Sec31.
IPR009917. SRA1-protein/COPII_Sec31.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]

Gene3D

G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.

KO

K14005.

Pfam

PF11549. Sec31. 1 hit.
PF07304. SRA1. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]

SMART

SM00320. WD40. 6 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

968393.

Entry information

Entry name

SEC31_YEAST

Accession

Primary (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:	January 25, 2012
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program