DPP3_YEAST
ID DPP3_YEAST Reviewed; 711 AA.
AC Q08225; O94146; Q05663;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Probable dipeptidyl peptidase 3;
DE EC=3.4.14.4;
DE AltName: Full=Dipeptidyl aminopeptidase III;
DE AltName: Full=Dipeptidyl arylamidase III;
DE AltName: Full=Dipeptidyl peptidase III;
DE Short=DPP III;
GN OrderedLocusNames=YOL057W; ORFNames=O1232;
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].
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8789261;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL Yeast 12:67-76(1996).
RN [2]
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 [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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide from a peptide comprising
CC four or more residues, with broad specificity. Also acts on
CC dipeptidyl 2-naphthylamides.; EC=3.4.14.4;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NY33};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NY33};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 3260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA62529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X91067; CAA62529.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74798; CAA99065.1; -; Genomic_DNA.
DR EMBL; Z74799; CAA99066.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10726.1; -; Genomic_DNA.
DR PIR; S66749; S66749.
DR RefSeq; NP_014584.1; NM_001183312.1.
DR PDB; 3CSK; X-ray; 1.95 A; A=1-711.
DR PDBsum; 3CSK; -.
DR AlphaFoldDB; Q08225; -.
DR SMR; Q08225; -.
DR BioGRID; 34344; 81.
DR MINT; Q08225; -.
DR STRING; 4932.YOL057W; -.
DR MEROPS; M49.004; -.
DR iPTMnet; Q08225; -.
DR MaxQB; Q08225; -.
DR PaxDb; Q08225; -.
DR PRIDE; Q08225; -.
DR EnsemblFungi; YOL057W_mRNA; YOL057W; YOL057W.
DR GeneID; 854097; -.
DR KEGG; sce:YOL057W; -.
DR SGD; S000005418; YOL057W.
DR VEuPathDB; FungiDB:YOL057W; -.
DR eggNOG; KOG3675; Eukaryota.
DR GeneTree; ENSGT00390000007335; -.
DR HOGENOM; CLU_011977_1_0_1; -.
DR InParanoid; Q08225; -.
DR OMA; HCQARFA; -.
DR BioCyc; YEAST:G3O-33468-MON; -.
DR BRENDA; 3.4.14.4; 984.
DR EvolutionaryTrace; Q08225; -.
DR PRO; PR:Q08225; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08225; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; ISS:SGD.
DR InterPro; IPR005317; Dipeptidyl-peptase3.
DR InterPro; IPR039461; Peptidase_M49.
DR PANTHER; PTHR23422; PTHR23422; 1.
DR Pfam; PF03571; Peptidase_M49; 1.
DR PIRSF; PIRSF007828; Dipeptidyl-peptidase_III; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..711
FT /note="Probable dipeptidyl peptidase 3"
FT /id="PRO_0000078243"
FT ACT_SITE 461
FT /evidence="ECO:0000250|UniProtKB:O55096"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 78..97
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 384..393
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 442..466
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 512..527
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 531..536
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 542..562
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 577..591
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:3CSK"
FT TURN 619..621
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 622..639
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 643..653
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 658..661
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 664..669
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 681..684
FT /evidence="ECO:0007829|PDB:3CSK"
FT STRAND 690..693
FT /evidence="ECO:0007829|PDB:3CSK"
FT HELIX 699..710
FT /evidence="ECO:0007829|PDB:3CSK"
SQ SEQUENCE 711 AA; 80510 MW; C8FEBD32834FA683 CRC64;
MSHFFADHDA PLSMLSVKTE YFPQLTDKEQ KYAHFMSKAS HAGSRVVMRQ VSHESEPIFD
LILAIHSKLN GKYPEDDITQ KQQTGLYLEY VSQFLSNLGN FKSFGDTKFI PRCEVKFFKQ
LLELAKINPC SSPLTLSPVD VNHEFTSHHL FSTINELIDI GIYHVEEKAA LLGFPSQGYT
SAYYLGLPVT PEDMALLKEQ LFAELAILPE NTRINKVGEN SFQIWVASEN VKNQITETYP
SGQITLSNAV TKVEFIFGDH SREMRLVASY LKEAQKFAAN DTQKAMLQEY INHFVTGSSQ
AHKEAQKLWV KDISPVIETN IGFIETYREP SGIIGEFESL VAIQNKERTA KFSSLVNNAE
EFISLLPWSK DYEKPIFNPP DFTSLEVLTF TGSGIPAGIN IPNYDDVRLK IGFKNVSLGN
ILSAAAKSSS KHPPSFISQE DRPIFEKYQS DSFEVQVGIH ELLGHGSGKL LTEFTDGFNF
DKENPPLGLD GKPVSTYYKV GETWGSKFGQ LAGPFEECRA EVIAMFLLTN KKILDIFGFH
DVESQDKVIY AGYLQMARAG LLALEYWNPK TGKWGQPHMQ ARFSIMKTFM KHSTDKNFLK
LEMNSTNDDF AIKLDKSLIK TAGHECVKDY LKHLHVYKCS GDVEQGSKYF IDRSTVTPDL
ASLRDIVLSK RLPRRQFIQS NSYIDDNNKV TLKEYDETPQ GMLQSFLDRE L
