ID U3JT02_FICAL Unreviewed; 484 AA.
AC U3JT02;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Carboxypeptidase Q {ECO:0000256|ARBA:ARBA00014116};
DE AltName: Full=Plasma glutamate carboxypeptidase {ECO:0000256|ARBA:ARBA00033328};
GN Name=CPQ {ECO:0000313|Ensembl:ENSFALP00000005906.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000005906.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000005906.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000005906.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; U3JT02; -.
DR STRING; 59894.ENSFALP00000005906; -.
DR Ensembl; ENSFALT00000005933.2; ENSFALP00000005906.2; ENSFALG00000005663.2.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT00390000018110; -.
DR HOGENOM; CLU_033697_1_1_1; -.
DR Proteomes; UP000016665; Chromosome 2.
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 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:UP000016665};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..484
FT /note="Carboxypeptidase Q"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032316680"
FT DOMAIN 268..453
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 484 AA; 53269 MW; 3865EF790FC2D43C CRC64;
MKYLFLIFLM NLLHQYAGKS LRRDGSSLKS FEDIKNEIAG YTNIAKAIID LAVHGKAQNR
SYERLAVFAD TIGPRLSGSK NLEAGIKYMF NALQKDGLEN VHLEPVKVPH WERGEEFAVM
LEPRNHSIAI LGLGSSIATP PEGITAEVIV VASFDELHRR AQEAKGKIVV YNEPFISYGE
TVQYRLQGAV EAAKVGAVAS LIRSIASFSI HSPHTGEQSY QPDVPQIPTA CISVEDAEMM
SRMSLRGTKI VVHLRMGAKT YPDSLSFNTV AEIVGSKYPE QVVLVSGHLD SWDVGQGAMD
DGGGAFISWE ALSLIKDLGL RPKRTLRLVL WTGEEQGGVG AEQYYQLHKE NISNFDIVME
SDEGTFKPSG LGFTGSAEPR GIVREIMALL QPINATDVYD TADGTDIAHW MRDGVPGASL
HNDINKYFWF HHSQGDTMTV QDPSQMNLCA AVWTVVSYVI ADMEDMLPST SEKEQSRCLQ
AASL
//
