CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011348
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 A-factor-processing enzyme 
Protein Synonyms/Alias
 Insulin-degrading enzyme homolog 
Gene Name
 STE23 
Gene Synonyms/Alias
 YLR389C; L8084.12 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
449STVSSLAKCLEKDYIubiquitination[1]
710RSWSTAEKLQVFEKLacetylation[2]
972LKSQVENKELNENELubiquitination[1]
983ENELDTAKYPTGQLIubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 Involved in the N-terminal endoproteolytic cleavage of the P2 precursor of the a-factor mating pheromone. Capable of proteolysing the established mammalian insulin-degrading enzymes (IDEs) substrates amyloid-beta peptide and insulin B-chain. 
Sequence Annotation
 ACT_SITE 121 121 Proton acceptor (By similarity).
 METAL 118 118 Zinc (By similarity).
 METAL 122 122 Zinc (By similarity).
 METAL 199 199 Zinc (By similarity).  
Keyword
 Complete proteome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Pheromone response; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1027 AA 
Protein Sequence
MGVSLLASSS AFVTKPLLTQ LVHLSPISLN FTVRRFKPFT CLSRYYTTNP YNMTSNFKTF 60
NLDFLKPDLD ERSYRFIELP NKLKALLIQD PKADKAAASL DVNIGAFEDP KNLPGLAHFC 120
EHLLFMGSEK FPDENEYSSY LSKHGGSSNA YTASQNTNYF FEVNHQHLFG ALDRFSGFFS 180
CPLFNKDSTD KEINAVNSEN KKNLQNDIWR IYQLDKSLTN TKHPYHKFST GNIETLGTLP 240
KENGLNVRDE LLKFHKNFYS ANLMKLCILG REDLDTLSDW TYDLFKDVAN NGREVPLYAE 300
PIMQPEHLQK IIQVRPVKDL KKLEISFTVP DMEEHWESKP PRILSHLIGH EGSGSLLAHL 360
KKLGWANELS AGGHTVSKGN AFFAVDIDLT DNGLTHYRDV IVLIFQYIEM LKNSLPQKWI 420
FNELQDISNA TFKFKQAGSP SSTVSSLAKC LEKDYIPVSR ILAMGLLTKY EPDLLTQYTD 480
ALVPENSRVT LISRSLETDS AEKWYGTAYK VVDYPADLIK NMKSPGLNPA LTLPRPNEFV 540
STNFKVDKID GIKPLDEPVL LLSDDVSKLW YKKDDRFWQP RGYIYLSFKL PHTHASIINS 600
MLSTLYTQLA NDALKDVQYD AACADLRISF NKTNQGLAIT ASGFNEKLII LLTRFLQGVN 660
SFEPKKDRFE ILKDKTIRHL KNLLYEVPYS QMSNYYNAII NERSWSTAEK LQVFEKLTFE 720
QLINFIPTIY EGVYFETLIH GNIKHEEALE VDSLIKSLIP NNIHNLQVSN NRLRSYLLPK 780
GKTFRYETAL KDSQNVNSCI QHVTQLDVYS EDLSALSGLF AQLIHEPCFD TLRTKEQLGY 840
VVFSSSLNNH GTANIRILIQ SEHTTPYLEW RINNFYETFG QVLRDMPEED FEKHKEALCN 900
SLLQKFKNMA EESARYTAAI YLGDYNFTHR QKKAKLVANI TKQQMIDFYE NYIMSENASK 960
LILHLKSQVE NKELNENELD TAKYPTGQLI EDVGAFKSTL FVAPVRQPMK DFEISAPPKL 1020
NNSSESE 1027 
Gene Ontology
 GO:0019898; C:extrinsic to membrane; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IDA:SGD.
 GO:0007323; P:peptide pheromone maturation; IGI:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0019236; P:response to pheromone; IEA:UniProtKB-KW. 
Interpro
 IPR011249; Metalloenz_LuxS/M16.
 IPR011237; Pept_M16_dom.
 IPR011765; Pept_M16_N.
 IPR001431; Pept_M16_Zn_BS.
 IPR007863; Peptidase_M16_C. 
Pfam
 PF00675; Peptidase_M16
 PF05193; Peptidase_M16_C 
SMART
  
PROSITE
 PS00143; INSULINASE 
PRINTS