P15303 (SEC23_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein transport protein SEC23

Gene names

Name:	SEC23
Ordered Locus Names:	YPR181C
ORF Names:	P9705.14

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	768 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. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.25 Ref.26 Ref.35 Ref.38 Ref.39 Ref.41
Subunit structure	The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Forms two other heterodimeric complexes with SFB3 and PDR17. Interacts with BET1, BET3, BOS1, EMP24, GRH1, SEC16, SEC22 and SYS1. Ref.9 Ref.13 Ref.15 Ref.16 Ref.20 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.35 Ref.37 Ref.39 Ref.40 Ref.41
Subcellular location	Cytoplasm. Cytoplasmic vesicle › COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Potential Ref.12 Ref.20 Ref.25 Ref.26 Ref.34.
Post-translational modification	Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex. Ref.37
Sequence similarities	Belongs to the SEC23/SEC24 family. SEC23 subfamily.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane
Ligand	Metal-binding Zinc
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER to Golgi vesicle-mediated transport Inferred from electronic annotation. Source: InterPro intracellular protein transport Inferred from electronic annotation. Source: InterPro regulation of COPII vesicle coating Inferred from direct assay Ref.11. Source: SGD
Cellular_component	COPII vesicle coat Inferred from direct assay PubMed 8004676. Source: SGD Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTPase activator activity Inferred from direct assay Ref.11. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEC16	P48415	5	EBI-16584,EBI-16551
SEC24	P40482	4	EBI-16584,EBI-16592
SEC31	P38968	4	EBI-16584,EBI-20524
SFB2	P53953	5	EBI-16584,EBI-17006

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 768

768

Protein transport protein SEC23

PRO_0000205145

Sites

Metal binding

56

1

Zinc

Metal binding

61

1

Zinc

Metal binding

80

1

Zinc

Metal binding

83

1

Zinc

Amino acid modifications

Modified residue

24

1

Phosphoserine Ref.31

Secondary structure

1

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768

Helix Strand Turn

Details...

Helix

3 – 10

8

Beta strand

11 – 22

12

Helix

23 – 28

6

Beta strand

33 – 37

5

Beta strand

48 – 51

4

Turn

59 – 61

3

Beta strand

69 – 72

4

Turn

73 – 76

4

Beta strand

77 – 79

3

Turn

81 – 83

3

Beta strand

86 – 88

3

Helix

91 – 93

3

Beta strand

98 – 100

3

Helix

103 – 105

3

Beta strand

108 – 113

6

Beta strand

123 – 129

7

Helix

134 – 149

16

Beta strand

156 – 168

13

Beta strand

172 – 183

12

Helix

190 – 198

9

Beta strand

221 – 223

3

Helix

224 – 227

4

Beta strand

228 – 230

3

Helix

231 – 243

13

Helix

262 – 276

15

Beta strand

283 – 290

8

Beta strand

294 – 297

4

Helix

311 – 315

5

Helix

322 – 339

18

Beta strand

342 – 348

7

Helix

355 – 365

11

Beta strand

369 – 373

5

Helix

378 – 386

9

Beta strand

394 – 397

4

Beta strand

399 – 408

10

Beta strand

412 – 420

9

Beta strand

437 – 439

3

Beta strand

443 – 450

8

Beta strand

456 – 462

7

Beta strand

484 – 495

12

Turn

496 – 498

3

Beta strand

499 – 512

14

Helix

517 – 521

5

Helix

525 – 539

15

Helix

545 – 563

19

Beta strand

564 – 567

4

Helix

571 – 573

3

Turn

578 – 581

4

Helix

582 – 592

11

Turn

594 – 596

3

Helix

603 – 613

11

Helix

618 – 625

8

Beta strand

628 – 632

5

Beta strand

634 – 636

3

Helix

645 – 647

3

Beta strand

653 – 657

5

Beta strand

659 – 666

8

Helix

668 – 676

9

Helix

678 – 680

3

Helix

682 – 684

3

Helix

685 – 703

19

Beta strand

710 – 715

6

Helix

719 – 721

3

Helix

722 – 725

4

Beta strand

740 – 742

3

Helix

752 – 763

12

Sequences

	Sequence		Length	Mass (Da)
	P15303 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 69811913848265FB	FASTA	768	85,385
	10 20 30 40 50 60 MDFETNEDIN GVRFTWNVFP STRSDANSNV VPVGCLYTPL KEYDELNVAP YNPVVCSGPH 70 80 90 100 110 120 CKSILNPYCV IDPRNSSWSC PICNSRNHLP PQYTNLSQEN MPLELQSTTI EYITNKPVTV 130 140 150 160 170 180 PPIFFFVVDL TSETENLDSL KESIITSLSL LPPNALIGLI TYGNVVQLHD LSSETIDRCN 190 200 210 220 230 240 VFRGDREYQL EALTEMLTGQ KPTGPGGAAS HLPNAMNKVT PFSLNRFFLP LEQVEFKLNQ 250 260 270 280 290 300 LLENLSPDQW SVPAGHRPLR ATGSALNIAS LLLQGCYKNI PARIILFASG PGTVAPGLIV 310 320 330 340 350 360 NSELKDPLRS HHDIDSDHAQ HYKKACKFYN QIAQRVAANG HTVDIFAGCY DQIGMSEMKQ 370 380 390 400 410 420 LTDSTGGVLL LTDAFSTAIF KQSYLRLFAK DEEGYLKMAF NGNMAVKTSK DLKVQGLIGH 430 440 450 460 470 480 ASAVKKTDAN NISESEIGIG ATSTWKMASL SPYHSYAIFF EIANTAANSN PMMSAPGSAD 490 500 510 520 530 540 RPHLAYTQFI TTYQHSSGTN RIRVTTVANQ LLPFGTPAIA ASFDQEAAAV LMARIAVHKA 550 560 570 580 590 600 ETDDGADVIR WLDRTLIKLC QKYADYNKDD PQSFRLAPNF SLYPQFTYYL RRSQFLSVFN 610 620 630 640 650 660 NSPDETAFYR HIFTREDTTN SLIMIQPTLT SFSMEDDPQP VLLDSISVKP NTILLLDTFF 670 680 690 700 710 720 FILIYHGEQI AQWRKAGYQD DPQYADFKAL LEEPKLEAAE LLVDRFPLPR FIDTEAGGSQ 730 740 750 760 ARFLLSKLNP SDNYQDMARG GSTIVLTDDV SLQNFMTHLQ QVAVSGQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast Sec23p acts in the cytoplasm to promote protein transport from the endoplasmic reticulum to the Golgi complex in vivo and in vitro." Hicke L., Schekman R.W. EMBO J. 8:1677-1684(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: MBY8-20C.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway." Novick P., Field C., Schekman R.W. Cell 21:205-215(1980) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Order of events in the yeast secretory pathway." Novick P., Ferro S., Schekman R.W. Cell 25:461-469(1981) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Reconstitution of SEC gene product-dependent intercompartmental protein transport." Baker D., Hicke L., Rexach M.F., Schleyer M., Schekman R.W. Cell 54:335-344(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex in yeast: the acceptor Golgi compartment is defective in the sec23 mutant." Ruohola H., Kabcenell A.K., Ferro-Novick S. J. Cell Biol. 107:1465-1476(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway." Kaiser C.A., Schekman R.W. Cell 61:723-733(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Sec23p and a novel 105-kDa protein function as a multimeric complex to promote vesicle budding and protein transport from the endoplasmic reticulum." Hicke L., Yoshihisa T., Schekman R.W. Mol. Biol. Cell 3:667-676(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[10]	"Multicopy STS1 restores both protein transport and ribosomal RNA stability in a new yeast sec23 mutant allele." Liang S., Lacroute F., Kepes F. Eur. J. Cell Biol. 62:270-281(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum." Yoshihisa T., Barlowe C., Schekman R.W. Science 259:1466-1468(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"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.
[13]	"Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p." Espenshade P.J., Gimeno R.E., Holzmacher E., Teung P., Kaiser C.A. J. Cell Biol. 131:311-324(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEC16.
[14]	"Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro." Kuehn M.J., Schekman R.W., Ljungdahl P.O. J. Cell Biol. 135:585-595(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p." Gimeno R.E., Espenshade P.J., Kaiser C.A. Mol. Biol. Cell 7:1815-1823(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEC16.
[16]	"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.
[17]	"Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast." Suetterlin C., Doering T.L., Schimmoeller F., Schroeder S., Riezman H. J. Cell Sci. 110:2703-2714(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"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.
[19]	"Role of endoplasmic reticulum-derived vesicles in the formation of Golgi elements in sec23 and sec18 Saccharomyces Cerevisiae mutants." Morin-Ganet M.N., Rambourg A., Clermont Y., Kepes F. Anat. Rec. 251:256-264(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"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.
[21]	"COPII-cargo interactions direct protein sorting into ER-derived transport vesicles." Kuehn M.J., Herrmann J.M., Schekman R.W. Nature 391:187-190(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
[22]	"Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs." Springer S., Schekman R.W. Science 281:698-700(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BET1; BOS1; SAR1 AND SEC24.
[23]	"Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter." Penalver E., Lucero P., Moreno E., Lagunas R. J. Bacteriol. 181:2555-2563(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE SEC23/24 COMPLEX.
[24]	"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.
[25]	"Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae." Shimoni Y., Kurihara T., Ravazzola M., Amherdt M., Orci L., Schekman R.W. J. Cell Biol. 151:973-984(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SFB3.
[26]	"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.
[27]	"Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae." Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W., Yoshihisa T. Mol. Biol. Cell 11:983-998(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDR17.
[28]	"An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export." Votsmeier C., Gallwitz D. EMBO J. 20:6742-6750(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYS1.
[29]	"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.
[30]	"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.
[31]	"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-24, MASS SPECTROMETRY.
[32]	"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 SEC23/24 COMPLEX.
[33]	"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 SEC23/24 COMPLEX.
[34]	"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.
[35]	"SNARE selectivity of the COPII coat." Mossessova E., Bickford L.C., Goldberg J. Cell 114:483-495(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE SEC23/24 COMPLEX, INTERACTION WITH BET1; SEC22 AND SED5.
[36]	"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.
[37]	"Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23." Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C. Nat. Cell Biol. 5:661-667(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH SEC24.
[38]	"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.
[39]	"Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile." Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A., Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S., Krogan N.J. Cell 123:507-519(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GRH1.
[40]	"The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic." Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S. J. Cell Biol. 176:255-261(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GHR1.
[41]	"TRAPPI tethers COPII vesicles by binding the coat subunit Sec23." Cai H., Yu S., Menon S., Cai Y., Lazarova D., Fu C., Reinisch K., Hay J.C., Ferro-Novick S. Nature 445:941-944(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH BET3.
[42]	"Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat." Bi X., Corpina R.A., Goldberg J. Nature 419:271-277(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAR1 AND ZINC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15474 Genomic DNA. Translation: CAA33501.1.
U25842 Genomic DNA. Translation: AAB68114.1.
BK006949 Genomic DNA. Translation: DAA11597.1.

PIR

BVBY23. S05742.

RefSeq

NP_015507.1. NM_001184278.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M2O	X-ray	2.50	A/C	1-768	[»]
1M2V	X-ray	2.75	A	1-768	[»]
2QTV	X-ray	2.50	A	2-768	[»]

ProteinModelPortal

P15303.

SMR

P15303. Positions 2-768.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2232N.

IntAct

P15303. 37 interactions.

MINT

MINT-540233.

STRING

4932.YPR181C.

Proteomic databases

PaxDb

P15303.

PeptideAtlas

P15303.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR181C; YPR181C; YPR181C.

GeneID

856311.

KEGG

sce:YPR181C.

Organism-specific databases

CYGD

YPR181c.

SGD

S000006385. SEC23.

Phylogenomic databases

eggNOG

COG5047.

GeneTree

ENSGT00390000006916.

HOGENOM

HOG000231690.

KO

K14006.

OMA

KDDPQSF.

OrthoDB

EOG4JWZNN.

Gene expression databases

Genevestigator

P15303.

GermOnline

YPR181C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007123. Gelsolin_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]

Pfam

PF00626. 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]

SMART

SM00327. VWA. 1 hit.
[Graphical view]

SUPFAM

SSF81811. Sec23_helical. 1 hit.
SSF82919. Znf_Sec23_Sec24. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P15303.

NextBio

981685.

Entry information

Entry name

SEC23_YEAST

Accession

Primary (citable) accession number: P15303
Secondary accession number(s): D6W4I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program