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Database: UniProt
Entry: A0DFS0_PARTE
LinkDB: A0DFS0_PARTE
Original site: A0DFS0_PARTE 
ID   A0DFS0_PARTE            Unreviewed;       451 AA.
AC   A0DFS0;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE   AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN   ORFNames=GSPATT00016700001 {ECO:0000313|EMBL:CAK81887.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK81887.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK81887.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK81887.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- SUBUNIT: Homodimer. The monomeric form is inactive while the homodimer
CC       is active. {ECO:0000256|ARBA:ARBA00025833}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}. Lysosome
CC       {ECO:0000256|ARBA:ARBA00004371}.
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DR   EMBL; CT868418; CAK81887.1; -; Genomic_DNA.
DR   RefSeq; XP_001449284.1; XM_001449247.1.
DR   AlphaFoldDB; A0DFS0; -.
DR   STRING; 5888.A0DFS0; -.
DR   EnsemblProtists; CAK81887; CAK81887; GSPATT00016700001.
DR   GeneID; 5035069; -.
DR   KEGG; ptm:GSPATT00016700001; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_033697_1_1_1; -.
DR   InParanoid; A0DFS0; -.
DR   OMA; ENERYFW; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0070573; F:metallodipeptidase activity; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd03883; M28_Pgcp_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR039866; CPQ.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12053:SF3; CARBOXYPEPTIDASE Q; 1.
DR   PANTHER; PTHR12053; PROTEASE FAMILY M28 PLASMA GLUTAMATE CARBOXYPEPTIDASE-RELATED; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          245..435
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   451 AA;  50188 MW;  2EB4E7F3B66C1E7D CRC64;
     MTIAYCVNDA IKKNVDDIRQ AINSGSNKHK AYDKLAYIVD TFGPRMWAQP SMALAVDYLY
     NQIQNWDSTK NGLVEVKLEK LDEISTWVRG SEQLILKSPR KRPQKLGMIG LGLIVPGNIK
     DGEVVVVRNW SELDEKGKAN KLQGKIVCYN VPWTSYSNLK LYRQQGLDRA SAYGAIAVLL
     RSVASFSIYS PHTGNVRQSG TVPKIPGAAI TVEDAEMLQR MQDRGQKITV DLELNSEMKP
     SESHNIIAEI KGSKYPNQII LMGGHFDSWD TGSQTGAMDD GAGTLVTLEA LKVVADLGIR
     PLRTLRWIAW SGEEMGLPNN GNQHYAKYHG DEDHVVALEN DLGQKTAIGF GFSGKLQTSR
     MVRQLIMNYI PDLSVVNEND GSGVDTKPLG DKGVPLMRNI YKDPNDDYYF KYHHSAGDTM
     NILNPDEMDS NVFAISSMMY IIADNPERLP K
//
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