ID   A0A1S3WFS6_ERIEU        Unreviewed;       895 AA.
AC   A0A1S3WFS6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=LOW QUALITY PROTEIN: cytosolic carboxypeptidase 3 {ECO:0000313|RefSeq:XP_016045233.1};
GN   Name=AGBL3 {ECO:0000313|RefSeq:XP_016045233.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016045233.1};
RN   [1] {ECO:0000313|RefSeq:XP_016045233.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O
CC         = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-
CC         glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-
CC         COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623;
CC         Evidence={ECO:0000256|ARBA:ARBA00029302};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC         Evidence={ECO:0000256|ARBA:ARBA00029302};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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   RefSeq; XP_016045233.1; XM_016189747.1.
DR   CTD; 340351; -.
DR   eggNOG; KOG1814; Eukaryota.
DR   eggNOG; KOG3641; Eukaryota.
DR   InParanoid; A0A1S3WFS6; -.
DR   OrthoDB; 168164at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06907; M14_AGBL2-3_like; 1.
DR   Gene3D; 2.60.40.3120; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF23; CYTOSOLIC CARBOXYPEPTIDASE 3; 1.
DR   Pfam; PF18027; Pepdidase_M14_N; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|RefSeq:XP_016045233.1};
KW   Hydrolase {ECO:0000313|RefSeq:XP_016045233.1};
KW   Protease {ECO:0000313|RefSeq:XP_016045233.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT   DOMAIN          169..293
FT                   /note="Cytosolic carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18027"
FT   DOMAIN          320..461
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
SQ   SEQUENCE   895 AA;  104287 MW;  24C7CF1FF8C70335 CRC64;
     MSEDSEKEDY SDRTISDEDE SDEDTFMKFV SADIHPCTFF TADSISDPYF PRTTQILLEY
     QLGRWVPRLR EPRDLYGVSS SGPLSPTRWP YHCEVINEKV RHIVNFSNVS VCLHSHVWLL
     LSSNLTPNHS KFSNKNAYKE PCFVYSRVGG NRTPLKQPVD NCDDTLMFEA RFESGNLQKV
     VKVAEYEYQL TVRPDLFTNK HTQWYYFQVT NTQAGVVYRF TINNFTKPAS LYNRGMRPLF
     YSEKEAKCHN IGWLRIGDQI KYYRNNPGQE GRHYFSLTWT FQFPHNKDTC YFAHCYPYTY
     SNLQEYLSNI NNDPVRSKFC NIRVLCHTIA RNMVYILTIT TPLKNCDSRN RKAVILTARV
     HPGETNSSWI MKGFLDYILG DSSDAQLLRD TFVFKVVPML NPDGVIVGNY RCSLAGRDLN
     RNYTSLLKES FPSVWYTRNM IRRLMEKREV ILYCDLHGHS RKENIFMYGC DGSDRCKAMY
     LQQRIFPLML SKNCPDKFSF SACKFNIQKS KEGTGRVVMW KMGIRNSFTM EATFCGSTLG
     NKRGTHFNTK DLESMGYHFC DSLLDYCDPD RAKYYQCLKE LEEMEKHINL EKVYDDSDAS
     LKEITLDLES SSRESDSSES NDSPAYLLNL TSQNKYLKTK KERDSTITSC QNVRNDQEIC
     DKGLLVQKNK ELNSEMKGPH HDIKNKMKEC TSFQSKKTDI NWTDDEKRIY RENRIAQTQE
     ILQYLFPSME NPKHMQTTQI QQMLNPRNKF QNSPQLKPPT FMNVRKGSTS WIVHKDAPLI
     DTKTLMVSSS EWLQSESRRS FECLSPPKAL KKRKKYPLIR PLKSKDMQPL SSSWKTDHSS
     FGNDMGIIKD KSLSAEGAIQ HSVMHIIPYL TKNKDEQLXK NDGQYSFHIN LQLDK
//