ID A0A091PZZ4_LEPDC Unreviewed; 189 AA.
AC A0A091PZZ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
DE Flags: Fragment;
GN ORFNames=N330_03674 {ECO:0000313|EMBL:KFQ12828.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ12828.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ12828.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ12828.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK681621; KFQ12828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PZZ4; -.
DR PhylomeDB; A0A091PZZ4; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
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 ECO:0000313|EMBL:KFQ12828.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:KFQ12828.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:KFQ12828.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001}.
FT DOMAIN 2..173
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ12828.1"
FT NON_TER 189
FT /evidence="ECO:0000313|EMBL:KFQ12828.1"
SQ SEQUENCE 189 AA; 21119 MW; 78784B70FC7526BE CRC64;
QIVLVSGHLD SWDVGQGAMD DGGGAFISWE ALSLIKDLGL RPKRTLRLVL WTAEEQGGIG
AKQYYQLHKE NISNFDIVME SDEGTFRPSG LGFTGNAKAR DIVKEIVTLL QPINVTEVYD
DADGTDIDYW MKDGVPGASL RDDLSKYFWF HHSQGDMMTV QDPNQMNLCA AVWTVVSYVI
ADMEEMLPR
//
