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STE23/YLR389C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrXII: 902660 to 899577 CDS: 902660 - 899577 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
STE23	YLR389C		ORF, Verified	S000004381
Description
Metalloprotease involved, with homolog Axl1p, in N-terminal processing of pro-a-factor to the mature form; member of the insulin-degrading enzyme family

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By catalytic activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR011237 , EBI:IPR011249 Assigned on 2008-02-13 UniProtKB hydrolase activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0378 Assigned on 2007-05-23 UniProtKB metal ion binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR011237 , EBI:IPR011249 Assigned on 2008-02-13 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0479 Assigned on 2007-05-23 UniProtKB metalloendopeptidase activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001431 , EBI:IPR007863 , EBI:IPR011765 Assigned on 2007-05-23 UniProtKB metallopeptidase activity Boyartchuk VL and Rine J (1998) Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor. Genetics 150(1):95-101        TAS : Traceable Author Statement Assigned on 2002-11-19 SGD Adames N, et al. (1995) Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science 270(5235):464-7      ISS : Inferred from Sequence or structural Similarity Assigned on 2005-01-03 SGD GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0482 Assigned on 2007-05-23 UniProtKB peptidase activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0645 Assigned on 2007-05-23 UniProtKB zinc ion binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR007863 Assigned on 2008-02-13 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0862 Assigned on 2007-05-23 UniProtKB
Biological Process Annotation(s) Reference(s) Evidence Assigned By peptide pheromone maturation Adames N, et al. (1995) Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science 270(5235):464-7      IMP : Inferred from Mutant Phenotype IGI : Inferred from Genetic Interaction with SGD:AXL1 Assigned on 2005-01-03 SGD proteolysis Boyartchuk VL and Rine J (1998) Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor. Genetics 150(1):95-101        TAS : Traceable Author Statement Assigned on 2002-11-19 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001431 , EBI:IPR007863 , EBI:IPR011765 Assigned on 2007-05-23 UniProtKB response to pheromone GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0589 Assigned on 2007-05-23 UniProtKB
Cellular Component Annotation(s) Reference(s) Evidence Assigned By integral to membrane Boyartchuk VL and Rine J (1998) Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor. Genetics 150(1):95-101        TAS : Traceable Author Statement Assigned on 2002-11-19 SGD

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]
No summary paragraph available

Basic References [TOP]
BASIC INFORMATION REFERENCES forSTE23/YLR389C for STE23 1) Boyartchuk VL and Rine J (1998) Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor. Genetics 150(1):95-101        2) Adames N, et al. (1995) Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science 270(5235):464-7

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for STE23/YLR389C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for STE23/YLR389C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MGVSLLA C-term NNSSESE Length(aa) 1,027 MW(Da) 117,578 pI 6.72 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.099   Codon Adaptation Index 0.164   Frequency of Optimal Codons 0.466   Hydropathicity of Protein -0.388   Aromaticity Score 0.107

10 20 30 40 50 | | | | | MGVSLLASSSAFVTKPLLTQLVHLSPISLNFTVRRFKPFTCLSRYYTTNP YNMTSNFKTFNLDFLKPDLDERSYRFIELPNKLKALLIQDPKADKAAASL DVNIGAFEDPKNLPGLAHFCEHLLFMGSEKFPDENEYSSYLSKHGGSSNA YTASQNTNYFFEVNHQHLFGALDRFSGFFSCPLFNKDSTDKEINAVNSEN KKNLQNDIWRIYQLDKSLTNTKHPYHKFSTGNIETLGTLPKENGLNVRDE LLKFHKNFYSANLMKLCILGREDLDTLSDWTYDLFKDVANNGREVPLYAE PIMQPEHLQKIIQVRPVKDLKKLEISFTVPDMEEHWESKPPRILSHLIGH EGSGSLLAHLKKLGWANELSAGGHTVSKGNAFFAVDIDLTDNGLTHYRDV IVLIFQYIEMLKNSLPQKWIFNELQDISNATFKFKQAGSPSSTVSSLAKC LEKDYIPVSRILAMGLLTKYEPDLLTQYTDALVPENSRVTLISRSLETDS AEKWYGTAYKVVDYPADLIKNMKSPGLNPALTLPRPNEFVSTNFKVDKID GIKPLDEPVLLLSDDVSKLWYKKDDRFWQPRGYIYLSFKLPHTHASIINS MLSTLYTQLANDALKDVQYDAACADLRISFNKTNQGLAITASGFNEKLII LLTRFLQGVNSFEPKKDRFEILKDKTIRHLKNLLYEVPYSQMSNYYNAII NERSWSTAEKLQVFEKLTFEQLINFIPTIYEGVYFETLIHGNIKHEEALE VDSLIKSLIPNNIHNLQVSNNRLRSYLLPKGKTFRYETALKDSQNVNSCI QHVTQLDVYSEDLSALSGLFAQLIHEPCFDTLRTKEQLGYVVFSSSLNNH GTANIRILIQSEHTTPYLEWRINNFYETFGQVLRDMPEEDFEKHKEALCN SLLQKFKNMAEESARYTAAIYLGDYNFTHRQKKAKLVANITKQQMIDFYE NYIMSENASKLILHLKSQVENKELNENELDTAKYPTGQLIEDVGAFKSTL FVAPVRQPMKDFEISAPPKLNNSSESE*

Protein Structures from PDB: proteins of known structure with sequence similarity to STE23/YLR389C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to STE23 Homolog Source (per PDB) Protein Alignment: STE23 vs. Homolog External Links P-Value %Identical %Similar Alignment 2g48 ( Chain: B, A) Crystal structure of human insulin-degrading enzyme in complex with amylin PDB_Info PDB_Structure Homo sapiens Chain B = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain A = 1.6e-151 38 32 View alignment 3e50 ( Chain: A, B) Insulin-degrading enzym PDB_Info PDB_Structure Unknown Chain A = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain B = 1.6e-151 38 32 View alignment 2g54 ( Chain: B, A) Crystal structure of zn-bound human insulin-degrading enzyme in complex with insulin b chain PDB_Info PDB_Structure Homo sapiens Chain B = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain A = 1.6e-151 38 32 View alignment 2g47 ( Chain: B, A) Crystal structure of human insulin-degrading enzyme in complex with amyloid-beta (1-40) PDB_Info PDB_Structure Homo sapiens Chain B = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain A = 1.6e-151 38 32 View alignment 2g49 ( Chain: B, A) Crystal structure of human insulin-degrading enzyme in complex with glucagon PDB_Info PDB_Structure Homo sapiens Chain B = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain A = 1.6e-151 38 32 View alignment 2g56 ( Chain: A, B) Crystal structure of human insulin-degrading enzyme in complex with insulin b chain PDB_Info PDB_Structure Homo sapiens Chain A = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain B = 1.6e-151 38 32 View alignment 2jbu ( Chain: A, B) Crystal structure of human insulin degrading enzyme complexed with co-purified peptides. PDB_Info PDB_Structure Homo sapiens | Escherichia coli Chain A = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain B = 1.6e-151 38 32 View alignment 2jg4 ( Chain: A, B) Substrate-free ide structure in its closed conformation PDB_Info PDB_Structure Homo sapiens Chain A = 1.6e-151 38 32 View alignment SCOP MMDB CATH Chain B = 1.6e-151 38 32 View alignment 2wby ( Chain: A, B) Crystal structure of human insulin-degrading enzyme in complex with insulin PDB_Info PDB_Structure Homo sapiens Chain A = 4.0e-150 38 32 View alignment SCOP MMDB CATH Chain B = 4.0e-150 38 32 View alignment 2wc0 ( Chain: B, A) Crystal structure of human insulin degrading enzyme in complex with iodinated insulin PDB_Info PDB_Structure Homo sapiens Chain B = 4.0e-150 38 32 View alignment SCOP MMDB CATH Chain A = 4.0e-150 38 32 View alignment 3e4a ( Chain: A, B) Insulin-degrading enzy PDB_Info PDB_Structure Unknown Chain A = 5.7e-150 39 32 View alignment SCOP MMDB CATH Chain B = 5.7e-150 39 32 View alignment 3e4z ( Chain: B, A) Insulin-degrading enzym PDB_Info PDB_Structure Unknown Chain B = 6.4e-150 38 32 View alignment SCOP MMDB CATH Chain A = 6.4e-150 38 32 View alignment 3cww ( Chain: A, B) Crystal structure of ide-bradykinin complex PDB_Info PDB_Structure Homo sapiens Chain A = 1.9e-149 38 33 View alignment SCOP MMDB CATH Chain B = 1.9e-149 38 33 View alignment 1q2l ( Chain: A) Crystal structure of pitrilysin PDB_Info PDB_Structure Escherichia coli str. k12 substr. w3110 8.6e-75 27 34 View alignment SCOP MMDB CATH 3eoq ( Chain: A, B) The crystal structure of putative zinc protease beta- subunit from thermus thermophilus hb8 PDB_Info PDB_Structure Thermus thermophilus Chain A = 3.4e-10 25 26 View alignment SCOP MMDB CATH Chain B = 3.4e-10 25 26 View alignment 1hr6 ( Chain: H, B, D, F) Yeast mitochondrial processing peptidase PDB_Info PDB_Structure Saccharomyces cerevisiae Chain H = 3.6e-05 22 33 View alignment SCOP MMDB CATH Chain B = 3.6e-05 22 33 View alignment Chain D = 3.6e-05 22 33 View alignment Chain F = 3.6e-05 22 33 View alignment 1hr8 ( Chain: B, F, H, D) Yeast mitochondrial processing peptidase beta-e73q mutant complexed with cytochrome c oxidase iv signal peptide PDB_Info PDB_Structure Saccharomyces cerevisiae Chain B = 6.9e-05 22 33 View alignment SCOP MMDB CATH Chain F = 6.9e-05 22 33 View alignment Chain H = 6.9e-05 22 33 View alignment Chain D = 6.9e-05 22 33 View alignment 1hr7 ( Chain: H, D, F, B) Yeast mitochondrial processing peptidase beta-e73q mutant PDB_Info PDB_Structure Saccharomyces cerevisiae Chain H = 6.9e-05 22 33 View alignment SCOP MMDB CATH Chain D = 6.9e-05 22 33 View alignment Chain F = 6.9e-05 22 33 View alignment Chain B = 6.9e-05 22 33 View alignment 1hr9 ( Chain: F, D, B, H) Yeast mitochondrial processing peptidase beta-e73q mutant complexed with malate dehydrogenase signal peptide PDB_Info PDB_Structure Saccharomyces cerevisiae Chain F = 6.9e-05 22 33 View alignment SCOP MMDB CATH Chain D = 6.9e-05 22 33 View alignment Chain B = 6.9e-05 22 33 View alignment Chain H = 6.9e-05 22 33 View alignment

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
STE23	SGD (2007) Information without a citation in SGD

Sequence Annotation Notes

Date

Note

2004-02-04

Brachat et al. 2003 predicted and confirmed the insertion of a single T nucleotide in YLR389C. As a consequence of this sequence change, YLR389C was extended at the 3' end, increasing the size of the predicted protein from 988 amino acids to 1027 amino acids. Query: GCTCTTTGTTTTCCACTTGAGATTTCAAATGTAGAATCAACTTCGATGCGTTCTCGCTCA ||||||||||| |||||||||||||||||||||||||||||||||||||||||||||||| Sbjct: 899741 GCTCTTTGTTT-CCACTTGAGATTTCAAATGTAGAATCAACTTCGATGCGTTCTCGCTCA 899799 Brachat S, et al. (2003) Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii. Genome Biol 4(7):R45

Mapping Notes

Date

Note

1996-09-21

Edition 13: The STE23 product shows homology to the AXL1 product and other members of the Insulin-degrading enzyme family of proteases (see Adames et al. Science 270:464-467) Cherry JM, et al. (1996) "Genetic and Physical Maps of Saccharomyces cerevisiae (Edition 13)". Pp. 361-364 in 1996 Yeast Genetics and Molecular Biology Meeting Program and Abstracts. Bethesda, MD: The Genetics Society of America

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YLR389C	SGD Systematic Sequence
851105	NCBI: Gene ID
NP_013493.2	NCBI: RefSeq protein version ID
NP_013493.2	NCBI: RefSeq protein version ID
42742289	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YGAC Triples YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
10 curated references; 0 references not yet curated
Fungal Related Genes/Proteins Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Physical Properties RNA Levels and Processing Substrates/Ligands/Cofactors Transcription	Alper BJ, et al. (2009) Yeast Ste23p shares functional similarities with mammalian insulin-degrading enzymes. Yeast 26(11):595-610	|AXL1
Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	Grunau S, et al. (2009) Peroxisomal targeting of PTS2 pre-import complexes in the yeast Saccharomyces cerevisiae. Traffic 10(4):451-60	|PEX13 |PEX14 |PEX18 |PEX21 |PEX5 |PEX7 |POT1 |SSA1 |SSA2
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Krishnankutty RK, et al. (2009) Proteolytic processing of certain CaaX motifs can occur in the absence of the Rce1p and Ste24p CaaX proteases. Yeast 26(8):451-63	|AXL1 |MFA1 |MOH1 |MRPS8 |NAP1 |PEX19 |POP8 |RCE1 |REC1 |SAM37 |STE14 |STE24 |VPS71 |VTI1 |MORE
Regulation of Transcription	Rintala E, et al. (2009) Low oxygen levels as a trigger for enhancement of respiratory metabolism in Saccharomyces cerevisiae. BMC Genomics 10():461	|AAT2 |ACO1 |ACS1 |ADH1 |ADH2 |AFR1 |AGA1 |AGA2 |ALD4 |ALD6 |ANT1 |ARE1 |ARN1 |ASH1 |MORE
Cross-species Expression Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Strains/Constructs	Alper BJ, et al. (2006) A common genetic system for functional studies of pitrilysin and related M16A proteases. Biochem J 398(1):145-52	|AXL1
Fungal Related Genes/Proteins	Fabre E, et al. (2005) Comparative genomics in hemiascomycete yeasts: evolution of sex, silencing, and subtelomeres. Mol Biol Evol 22(4):856-73	|ABF1 |ASH1 |AXL1 |CDC24 |DOT1 |ESA1 |ESC1 |FAR1 |FUS3 |GCN5 |HMLALPHA1 |HMLALPHA2 |HMRA1 |HMRA2 |MORE
Cellular Location Cross-species Expression Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Physical Properties Protein Sequence Features Strains/Constructs	Kim S, et al. (2005) Yeast as a tractable genetic system for functional studies of the insulin-degrading enzyme. J Biol Chem 280(30):27481-90	|AXL1 |MFA1 |MFA2
Function/Process Mutants/Phenotypes Strains/Constructs	Jonson L, et al. (2004) Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae. Eur J Biochem 271(23-24):4788-97	|AAP1 |AFG3 |APE2 |APE3 |AXL1 |CYM1 |ECM14 |KAE1 |LAP2 |LAP4 |OCT1 |PRD1 |QRI7 |STE24 |MORE
Cellular Location Function/Process	Boyartchuk VL and Rine J (1998) Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor. Genetics 150(1):95-101	|AXL1 |MFA1 |RCE1 |STE24
Function/Process Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Strains/Constructs	Adames N, et al. (1995) Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science 270(5235):464-7	|AXL1 |MFA1

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