ID A0A3Q0G1F5_ALLSI Unreviewed; 1221 AA.
AC A0A3Q0G1F5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cytosolic carboxypeptidase 1 {ECO:0000256|ARBA:ARBA00041044};
DE EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
DE AltName: Full=ATP/GTP-binding protein 1 {ECO:0000256|ARBA:ARBA00043070};
DE AltName: Full=Protein deglutamylase CCP1 {ECO:0000256|ARBA:ARBA00043068};
GN Name=AGTPBP1 {ECO:0000313|RefSeq:XP_025053479.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025053479.1};
RN [1] {ECO:0000313|RefSeq:XP_025053479.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-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 -!- CATALYTIC ACTIVITY:
CC Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] +
CC H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-
CC glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-
CC COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555,
CC ChEBI:CHEBI:149556; EC=3.4.17.24;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
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}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR RefSeq; XP_025053479.1; XM_025197694.1.
DR AlphaFoldDB; A0A3Q0G1F5; -.
DR Proteomes; UP000189705; 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; cd06906; M14_Nna1; 1.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033852; CBPC1/4.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF24; CYTOSOLIC CARBOXYPEPTIDASE 1; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|RefSeq:XP_025053479.1};
KW Hydrolase {ECO:0000313|RefSeq:XP_025053479.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000313|RefSeq:XP_025053479.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 718..807
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 886..990
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 371..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..393
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 137167 MW; 24D0E5AB60AC989D CRC64;
MNKVKTTSEK SLASNSRIVV LLTQLEKINS ESLLVEADTA RYVTSKILHL AQSQEKTRKE
MTAKGSTGVE VILSTLENTR DLQTTLNILS ILIELVSVGG GRRACILVSK GGTQILLQLL
LGASKDSPPN EELMVQLHSL LAKIGPKGNH SRDKKFGVKA RINGALNISL NLVKQNLQNH
RLILPCLQVL RVYSTNSVNA VSLGKNGVVE LMFKIIGPFS KKNTGLMKVA LDTLAALLKS
KTNARRAVDR GYVQVLLTIY VDWHRHDSRH RHMLIRKGIL QCIKSVTNIK LGRKAFIDAN
GMKILYNTSQ DCLAVRTLDP LVNTSSLIMR KCFPKNRLPL PTIKSAFHFQ LPVIPTSGPV
AQLYSLPPEV DDVVDESDDN DDIETETETE NENEDDKDQH FKNDDIETDI DKLKPKQELG
RPIEELKIYE QFFPELAENF QEYDLVSKEP KPFASATNLG GPIVVPTAGE EHPAEANQSV
KGIAVKDHSS LQMEEYNKRP SFLDLPKKDH NKDSLQLQND QKKLLSSCQC LSQEIVKGLD
RITLQNTSKS EQYYSTGCLI KKESKTSLTT PACNKPCQHV SSCGSGLFEG PSVQLGKLCC
TGVDPDEEED SSSHSSGEQV LLEVPDMLPL HNPDLYIEIV KNTKSVPEYS EVAYPDYFGH
IPPPFKEPIL ERPYGVQRTK IAQDIERLIH QNDIVDRVIY DLDNSSCSVP EEGDILKFNS
KFESGNLRKV IQIRKNEYDL ILNSDINSNH YHQWFYFEVS GMKTGIGYRF NIINCEKSNS
QFNYGMQPLM YSVQEALNAR PWWGRVGTDI CYYKNHFSRS SIAAGGQKGK SYYTITFTVS
FPHKDDVCYF AYHYPYTYST LKMHLQKLES MHNPQQIYFR EDVLCETLAG NSCPLVTITA
MPESNYYEHV CQFRNRPYVF LSARVHPGET NASWVMKGTL EYLMSSSPAA QSLRESYIFK
IVPMLNPDGV INGNHRCSLS GEDLNRQWQN PNLDLHPTIY HAKGLLQYMA TIKRLPLVFC
DYHGHSRKKN VFMYGCSIKE TMWHTDVSAA SCDVIEDLGY RALPKILSQT APAFCMSSCS
FVVEKSKEST ARVVVWREIG VQRSYTMEST LCGCDQGKYK GLQIGTRELE EMGAKFCVGL
LRLKRLTSPL EHNLPSSLLD IENELIESSC KVTSFSPHSS LMGKCPPTFG ICRQSSAVSG
GCKSDPCPST QADRLSVFNK C
//