DAP2_YEAST
ID DAP2_YEAST Reviewed; 818 AA.
AC P18962; D3DKX5; E9P957;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Dipeptidyl aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.-;
DE AltName: Full=YSCV;
GN Name=DAP2; OrderedLocusNames=YHR028C;
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=2647766; DOI=10.1083/jcb.108.4.1363;
RA Roberts C.J., Pohlig G., Rothman J.H., Stevens T.H.;
RT "Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B,
RT an integral membrane glycoprotein of the yeast vacuole.";
RL J. Cell Biol. 108:1363-1373(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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; X15484; CAA33512.1; -; Genomic_DNA.
DR EMBL; U10399; AAB68879.1; -; Genomic_DNA.
DR EMBL; AY723822; AAU09739.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06719.1; -; Genomic_DNA.
DR PIR; S46780; A30107.
DR RefSeq; NP_011893.1; NM_001179158.1.
DR PDB; 3KL4; X-ray; 3.50 A; B=26-51.
DR PDB; 3ZN8; EM; 12.00 A; S=31-44.
DR PDB; 7OBR; EM; 2.80 A; s=24-90.
DR PDBsum; 3KL4; -.
DR PDBsum; 3ZN8; -.
DR PDBsum; 7OBR; -.
DR AlphaFoldDB; P18962; -.
DR SMR; P18962; -.
DR BioGRID; 36459; 84.
DR DIP; DIP-5759N; -.
DR STRING; 4932.YHR028C; -.
DR ESTHER; yeast-dap2; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR iPTMnet; P18962; -.
DR MaxQB; P18962; -.
DR PaxDb; P18962; -.
DR PRIDE; P18962; -.
DR EnsemblFungi; YHR028C_mRNA; YHR028C; YHR028C.
DR GeneID; 856423; -.
DR KEGG; sce:YHR028C; -.
DR SGD; S000001070; DAP2.
DR VEuPathDB; FungiDB:YHR028C; -.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000161291; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; P18962; -.
DR OMA; MRTPQEN; -.
DR BioCyc; YEAST:G3O-31088-MON; -.
DR EvolutionaryTrace; P18962; -.
DR PRO; PR:P18962; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P18962; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016485; P:protein processing; ISS:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..818
FT /note="Dipeptidyl aminopeptidase B"
FT /id="PRO_0000122421"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..818
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 679
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 756
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 789
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 83
FT /note="Q -> H (in Ref. 1; CAA33512)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="S -> N (in Ref. 1; CAA33512)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..188
FT /note="FEEIGNE -> LRRLET (in Ref. 1; CAA33512)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="D -> N (in Ref. 1; CAA33512)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="H -> R (in Ref. 4; AAU09739)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..375
FT /note="TSNVVRNESS -> DFKRGKERKF (in Ref. 1; CAA33512)"
FT /evidence="ECO:0000305"
FT CONFLICT 808..818
FT /note="AKRAFDGQFVK -> QSVLSMGNLTNELTIYSSSHRDIHKTFSYLHTMYI
FT (in Ref. 1; CAA33512)"
FT /evidence="ECO:0000305"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3KL4"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:3KL4"
SQ SEQUENCE 818 AA; 93404 MW; 318F450445375BD3 CRC64;
MEGGEEEVER IPDELFDTKK KHLLDKLIRV GIILVLLIWG TVLLLKSIPH HSNTPDYQEP
NSNYTNDGKL KVSFSVVRNN TFQPKYHELQ WISDNKIESN DLGLYVTFMN DSYVVKSVYD
DSYNSVLLEG KTFIHNGQNL TVESITASPD LKRLLIRTNS VQNWRHSTFG SYFVYDKSSS
SFEEIGNEVA LAIWSPNSND IAYVQDNNIY IYSAISKKTI RAVTNDGSSF LFNGKPDWVY
EEEVFEDDKA AWWSPTGDYL AFLKIDESEV GEFIIPYYVQ DEKDIYPEMR SIKYPKSGTP
NPHAELWVYS MKDGTSFHPR ISGNKKDGSL LITEVTWVGN GNVLVKTTDR SSDILTVFLI
DTIAKTSNVV RNESSNGGWW EITHNTLFIP ANETFDRPHN GYVDILPIGG YNHLAYFENS
NSSHYKTLTE GKWEVVNGPL AFDSMENRLY FISTRKSSTE RHVYYIDLRS PNEIIEVTDT
SEDGVYDVSF SSGRRFGLLT YKGPKVPYQK IVDFHSRKAE KCDKGNVLGK SLYHLEKNEV
LTKILEDYAV PRKSFRELNL GKDEFGKDIL VNSYEILPND FDETLSDHYP VFFFAYGGPN
SQQVVKTFSV GFNEVVASQL NAIVVVVDGR GTGFKGQDFR SLVRDRLGDY EARDQISAAS
LYGSLTFVDP QKISLFGWSY GGYLTLKTLE KDGGRHFKYG MSVAPVTDWR FYDSVYTERY
MHTPQENFDG YVESSVHNVT ALAQANRFLL MHGTGDDNVH FQNSLKFLDL LDLNGVENYD
VHVFPDSDHS IRYHNANVIV FDKLLDWAKR AFDGQFVK
