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DPP3_DICDI
ID   DPP3_DICDI              Reviewed;         691 AA.
AC   Q557H1; Q8T1P0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=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   Name=dpp3-1; ORFNames=DDB_G0273471;
GN   and
GN   Name=dpp3-2; ORFNames=DDB_G0273563;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}.
CC   -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC       AX4. These strains contain a duplication of a segment of 750 kb of
CC       chromosome 2 compared to the corresponding sequence in strain AX2.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000010; EAL70690.1; -; Genomic_DNA.
DR   EMBL; AAFI02000010; EAL70736.1; -; Genomic_DNA.
DR   RefSeq; XP_644587.1; XM_639495.1.
DR   RefSeq; XP_644664.1; XM_639572.1.
DR   AlphaFoldDB; Q557H1; -.
DR   SMR; Q557H1; -.
DR   STRING; 44689.DDB0266801; -.
DR   MEROPS; M49.A02; -.
DR   PaxDb; Q557H1; -.
DR   PRIDE; Q557H1; -.
DR   EnsemblProtists; EAL70690; EAL70690; DDB_G0273563.
DR   EnsemblProtists; EAL70736; EAL70736; DDB_G0273471.
DR   GeneID; 8618951; -.
DR   GeneID; 8619026; -.
DR   KEGG; ddi:DDB_G0273471; -.
DR   KEGG; ddi:DDB_G0273563; -.
DR   dictyBase; DDB_G0273471; dpp3-1.
DR   dictyBase; DDB_G0273563; dpp3-2.
DR   eggNOG; KOG3675; Eukaryota.
DR   HOGENOM; CLU_011977_1_0_1; -.
DR   InParanoid; Q557H1; -.
DR   OMA; HCQARFA; -.
DR   PhylomeDB; Q557H1; -.
DR   PRO; PR:Q557H1; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; ISS:dictyBase.
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:dictyBase.
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   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Zinc.
FT   CHAIN           1..691
FT                   /note="Dipeptidyl peptidase 3"
FT                   /id="PRO_0000332967"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000250|UniProtKB:O55096"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY33"
FT   BINDING         492
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NY33"
SQ   SEQUENCE   691 AA;  78274 MW;  94C2097F73312E82 CRC64;
     MSVPSSVIEN HLVPKEIPVY RLNARESFNL LTEKEQLYAH HISVACWWGS KICLGQTSIE
     SGPIFNLFQN LFSIQNLKST VVPNIVSEEE YSDLLSYAAT FYGNMGNYLS FGDSKFIPRI
     SKEKLQLIIN KVNDNKVNEY WGKCSELMYS LDKQVRELGI DGNGISTYYS PNITKVEIEK
     VQKFMDSKSI SPYNTRLFKV SENNYNLLIA SASTSTPTVS HQFDGYTINI VYGDWNKNLT
     KVVDNLKLAL PYAANENQTN MLKKYIDSFY SGSIDDHKDS QRWWIKDISP AVETNIGFIE
     SYRDPYGVRG EWEGFVSMVN KEMSLKFGKL TDNATTFLSK LPWDKSFEKE KFNKPDFTSL
     EVLTFATTGI PAGINLSNYD DIRQTEGFKN VSLGNVIAAR KDEYVTFIQE SDQKLFNELS
     TEAFELQVGI HELYGHGSGK LFTTDANGNV NFKVGEVINP LTNKPIDPKT EVYKFGETYD
     SVFKSLGSPM EECRAECCGI YLSPDEKILE LFGFTDPKKA EDVYYVNWLI MARAGVCALE
     FYSPPSEGAP GKWRQAHMQA RYCILTTFLR SGIVTLDKTA DDVIVKLDKS KIRGIGVKAV
     GDFLNRLMVY KATANIDASI KLFDEYTHVN EEFLAIRDIV LAKKKPRKVF VQAHTYLNSN
     GKVCLQDFDD STQGMIDSMI TRFGKDDSDM L
 
 
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