ID A0A1U8D6U7_ALLSI Unreviewed; 1227 AA.
AC A0A1U8D6U7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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_014372840.1};
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_014372840.1};
RN [1] {ECO:0000313|RefSeq:XP_014372840.1}
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 -!- 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_006018523.1; XM_006018461.2.
DR RefSeq; XP_014372840.1; XM_014517354.2.
DR AlphaFoldDB; A0A1U8D6U7; -.
DR GeneID; 102385577; -.
DR KEGG; asn:102385577; -.
DR CTD; 23287; -.
DR eggNOG; KOG3641; Eukaryota.
DR OrthoDB; 168164at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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_014372840.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|RefSeq:XP_014372840.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000313|RefSeq:XP_014372840.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT DOMAIN 713..802
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 881..985
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 366..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 138227 MW; 08A5F923A226C6D8 CRC64;
MNKVKTTSEK SLASNSRIVV LLTQLEKINS ESLLVEADTA RYVTSKILHL AQSQEKTRKE
MTAKGSTGVE VILSTLENTR DLQTTLNILS ILIELVSVGG GRRACILVSK GGTQILLQLL
LGASKDSPPN EELMVQLHSL LAKIGPKDKK FGVKARINGA LNISLNLVKQ NLQNHRLILP
CLQVLRVYST NSVNAVSLGK NGVVELMFKI IGPFSKKNTG LMKVALDTLA ALLKSKTNAR
RAVDRGYVQV LLTIYVDWHR HDSRHRHMLI RKGILQCIKS VTNIKLGRKA FIDANGMKIL
YNTSQDCLAV RTLDPLVNTS SLIMRKCFPK NRLPLPTIKS AFHFQLPVIP TSGPVAQLYS
LPPEVDDVVD ESDDNDDIET ETETENENED DKDQHFKNDD IETDIDKLKP KQELGRPIEE
LKIYEQFFPE LAENFQEYDL VSKEPKPFAS ATNLGGPIVV PTAGEEHPAE ANQSVKGIAV
KDHSSLQMEE YNKRPSFLDL PKKDHNKDSL QLQNDQKKLL SSCQCLSQEI VKGLDRITLQ
NTSKSEQYYS TGCLIKKESK TSLTTPACNK PCQHVSSCGS GLFEGPSVQL GKLCCTGVDP
DEEEDSSSHS SGEQVLLEVP DMLPLHNPDL YIEIVKNTKS VPEYSEVAYP DYFGHIPPPF
KEPILERPYG VQRTKIAQDI ERLIHQNDIV DRVIYDLDNS SCSVPEEGDI LKFNSKFESG
NLRKVIQIRK NEYDLILNSD INSNHYHQWF YFEVSGMKTG IGYRFNIINC EKSNSQFNYG
MQPLMYSVQE ALNARPWWGR VGTDICYYKN HFSRSSIAAG GQKGKSYYTI TFTVSFPHKD
DVCYFAYHYP YTYSTLKMHL QKLESMHNPQ QIYFREDVLC ETLAGNSCPL VTITAMPESN
YYEHVCQFRN RPYVFLSARV HPGETNASWV MKGTLEYLMS SSPAAQSLRE SYIFKIVPML
NPDGVINGNH RCSLSGEDLN RQWQNPNLDL HPTIYHAKGL LQYMATIKRL PLVFCDYHGH
SRKKNVFMYG CSIKETMWHT DVSAASCDVI EDLGYRALPK ILSQTAPAFC MSSCSFVVEK
SKESTARVVV WREIGVQRSY TMESTLCGCD QGKYKGLQIG TRELEEMGAK FCVGLLRLKR
LTSPLEHNLP SSLLDIENEL IESSCKVTSP TTYVLDEDEP RFLEEVDYSA ESNDEQDVEL
ADNAGDYEPS IQEDALSDSE ATRTHLP
//
