STE13_YEAST
ID STE13_YEAST Reviewed; 931 AA.
AC P33894; D6W2S4; Q9URF1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Dipeptidyl aminopeptidase A;
DE Short=DPAP A;
DE EC=3.4.14.-;
DE AltName: Full=YSCIV;
GN Name=STE13; Synonyms=YCI1; OrderedLocusNames=YOR219C; ORFNames=YOR50-9;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7975897; DOI=10.1002/yea.320100610;
RA Anna-Arriola S.S., Herskowitz I.;
RT "Isolation and DNA sequence of the STE13 gene encoding dipeptidyl
RT aminopeptidase.";
RL Yeast 10:801-810(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 204510 / AB320;
RA Flanagan C.A., Thorner J.;
RT "STE13.";
RL (In) Gething M.-J., Novick P., Stevens T.H., Rothblatt J. (eds.);
RL Guidebook to the yeast secretory pathway, pp.1-1, Oxford University Press,
RL Oxford (1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-119.
RX PubMed=8509444; DOI=10.1083/jcb.121.6.1197;
RA Nothwehr S.F., Roberts C.J., Stevens T.H.;
RT "Membrane protein retention in the yeast Golgi apparatus: dipeptidyl
RT aminopeptidase A is retained by a cytoplasmic signal containing aromatic
RT residues.";
RL J. Cell Biol. 121:1197-1209(1993).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC -!- FUNCTION: Responsible for the proteolytic maturation of the alpha-
CC factor precursor.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Single-pass type II membrane
CC protein. Note=Lysosome-like vacuoles.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; L21944; AAA35119.1; -; Genomic_DNA.
DR EMBL; U08230; AAA17897.1; -; Unassigned_DNA.
DR EMBL; X92441; CAA63182.1; -; Genomic_DNA.
DR EMBL; Z75127; CAA99437.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10990.1; -; Genomic_DNA.
DR PIR; A49737; A49737.
DR RefSeq; NP_014862.3; NM_001183638.3.
DR AlphaFoldDB; P33894; -.
DR SMR; P33894; -.
DR BioGRID; 34613; 27.
DR DIP; DIP-2596N; -.
DR IntAct; P33894; 1.
DR MINT; P33894; -.
DR STRING; 4932.YOR219C; -.
DR ESTHER; yeast-dap1; DPP4N_Peptidase_S9.
DR MEROPS; S09.005; -.
DR iPTMnet; P33894; -.
DR MaxQB; P33894; -.
DR PaxDb; P33894; -.
DR PRIDE; P33894; -.
DR EnsemblFungi; YOR219C_mRNA; YOR219C; YOR219C.
DR GeneID; 854394; -.
DR KEGG; sce:YOR219C; -.
DR SGD; S000005745; STE13.
DR VEuPathDB; FungiDB:YOR219C; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; P33894; -.
DR OMA; DKMFYLV; -.
DR BioCyc; YEAST:YOR219C-MON; -.
DR PRO; PR:P33894; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P33894; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:SGD.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007323; P:peptide pheromone maturation; IDA:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Glycoprotein; Hydrolase; Membrane; Pheromone response;
KW Protease; Reference proteome; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..931
FT /note="Dipeptidyl aminopeptidase A"
FT /id="PRO_0000122420"
FT TOPO_DOM 1..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 141..931
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 785
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 863
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 896
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 931 AA; 107200 MW; 81AF70094093C023 CRC64;
MSASTHSHKR KNSHLFPQRK SSNSSMDKPF FPNNDSVANT DPQSNENGHT INEIRPTEAT
IDVTDVPQTP FLQEQYSMRP RRESFQFNDI ENQHHTHSFF SVNKFNRRWG EWSLPEKRSY
VLVFTLIALS VLVLLVILIP SKLLPTKITR PKTSAGDSSL GKRSFSIENV LNGDFAIPED
TFHFIDPPQR LLGQDSDPGL YFTTKEIDGH TNFIAKQLFD ETFEVNLGGN RFLYEGVEFT
VSTVQINYKL DKLIFGTNLE SEFRHSSKGF YWIKDLNTGN IEPILPPEKS DDNYELGLSK
LSYAHFSPAY NYIYFVYENN LFLQQVNSGV AKKVTEDGSK DIFNAKPDWI YEEEVLASDQ
AIWWAPDDSK AVFARFNDTS VDDIRLNRYT NMNEAYLSDT KIKYPKPGFQ NPQFDLFLVN
LQNGIIYSIN TGGQKDSILY NGKWISPDTF RFEITDRNSK ILDVKVYDIP SSQMLTVRNT
NSNLFNGWIE KTKDILSIPP KPELKRMDYG YIDIHADSRG FSHLFYYPTV FAKEPIQLTK
GNWEVTGNGI VGYEYETDTI FFTANEIGVM SQHLYSISLT DSTTQNTFQS LQNPSDKYDF
YDFELSSSAR YAISKKLGPD TPIKVAGPLT RVLNVAEIHD DSILQLTKDE KFKEKIKNYD
LPITSYKTMV LDDGVEINYI EIKPANLNPK KKYPILVNIY GGPGSQTFTT KSSLAFEQAV
VSGLDVIVLQ IEPRGTGGKG WSFRSWAREK LGYWEPRDIT EVTKKFIQRN SQHIDESKIA
IWGWSYGGFT SLKTVELDNG DTFKYAMAVA PVTNWTLYDS VYTERYMNQP SENHEGYFEV
STIQNFKSFE SLKRLFIVHG TFDDNVHIQN TFRLVDQLNL LGLTNYDMHI FPDSDHSIRY
HNAQRIVFQK LYYWLRDAFA ERFDNTEVLH L
