ID A0A2A3E762_APICC Unreviewed; 476 AA.
AC A0A2A3E762;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=APICC_04284 {ECO:0000313|EMBL:PBC27122.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC27122.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC27122.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC27122.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ288357; PBC27122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3E762; -.
DR STRING; 94128.A0A2A3E762; -.
DR Proteomes; UP000242457; 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 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 ECO:0000313|EMBL:PBC27122.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:PBC27122.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:PBC27122.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242457};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..476
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013217609"
FT DOMAIN 273..460
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 476 AA; 52843 MW; 47535C7F141F106E CRC64;
MLLSTKLLIV VWLLRLHSIF AAVTGEVDNV ISCKLPEPLL HEIDSYKIIV RAIINEALNG
SFKGTTWNEL AYFTDRFGPR PSGSEALEHS IDYVLNKSME YGLENVHGES VTVPHWVKGK
ESATLLKPRK MNIAILGLGT SVGTPPEGIT AEAIVVDSFQ ELYSKKDEIP GKIVVYNQKF
VSYDETVQYR KDGARQASKY GAVAVLIRSI TPYSLYTPHT GNQRYGKNVI KIPVASITIE
DATLLRRMAN RGEVLEINLK MEAKNLPSTV SRNVIADFRG STNPEKIVVV SGHIDSWDVG
QGAMDDGGGI FISWQALKLL KYLNYKPRRT VRLIMWTAEE VGSLGALDFI KAHQSEQNNL
QFVMESDAGT FAPLGIQYTG TDIVGCILER IMTLFSPMGN MKVRSPNQGP DIAIWINEGV
PGASLWNQDD KYFYYHHSNA DTMLVEDSEA LDKGTALFAA LSYILADLSI DLPRHK
//
