ID V9I887_APICE Unreviewed; 469 AA.
AC V9I887;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN ORFNames=ACCB00034.2 {ECO:0000313|EMBL:AEY56542.1}, ACCB00034.4
GN {ECO:0000313|EMBL:AEY56544.1}, ACCB00034.5
GN {ECO:0000313|EMBL:AEY56545.1}, ACCB00034.7
GN {ECO:0000313|EMBL:AEY56547.1};
OS Apis cerana (Indian honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7461 {ECO:0000313|EMBL:AEY56544.1};
RN [1] {ECO:0000313|EMBL:AEY56544.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AEY56544.1};
RA Sun L., Zheng H., Wang Y., Xie X., Zhu Y., Gu W., Wang S.;
RT "Decoding the brain transcriptome of the Eastern honeybee (Apis cerana)
RT based on pyrosequencing.";
RL Submitted (NOV-2011) 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; JR035614; AEY56542.1; -; mRNA.
DR EMBL; JR035616; AEY56544.1; -; mRNA.
DR EMBL; JR035617; AEY56545.1; -; mRNA.
DR EMBL; JR035619; AEY56547.1; -; mRNA.
DR AlphaFoldDB; V9I887; -.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:AEY56544.1};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:AEY56544.1};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:AEY56544.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..469
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007732525"
FT DOMAIN 266..453
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 469 AA; 52066 MW; F62B7A6977410FE1 CRC64;
MLLSTKLLIV VWLLRLHSIL ATVISCQLPQ SLLNEIDSYE PVVRAIINEA LNGSFKESTW
NELAYFTDRF GPRPSGSEAL ERSIDYVLNR SIEYGLENVH GEPVTVPHWV RGRESATLLK
PRQLNIAILG LGTSIGTPPE GITAEAIVVD SFEELNRRKD DVPGKIVIYN QKFVSYDETV
EYRTNGARQA SKYGAVAALV RSITPYSLYS PHTGHQTYGE NVTEIPVAAI TVEDATLLRR
MASRGEVLEI NLKMEAKNLP STISRNVIAD FRGSTNPEKI VVVSGHIDSW DVGQGAMDDG
GGIFISWQAV KLLKHLNYRP RRTVRLIMWT AEEVGSLGAL DFIKTHKSEQ NNLQFVMESD
AGTFAPLGIE YTGTDVVGCI LERIMTLCSP LGNMKVRSPS QGPDIDFWIN EGVPGGSLWN
QDDKYFYYHH SNADTMLVED PDALDRGTAL FAALSYVLAD LSIDLPRHK
//
