ID A0A3Q7RCX4_VULVU Unreviewed; 1182 AA.
AC A0A3Q7RCX4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_025839966.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025839966.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025839966.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025839966.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025839966.1};
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_025839966.1; XM_025984181.1.
DR AlphaFoldDB; A0A3Q7RCX4; -.
DR Proteomes; UP000286640; 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_025839966.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|RefSeq:XP_025839966.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000313|RefSeq:XP_025839966.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT DOMAIN 712..802
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 878..984
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 500..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1182 AA; 133026 MW; 5B055CB53B4DF4E4 CRC64;
MSKLKVISEK SLTNNSRIVG LLAQLEKINT ESTESDTARY VTSKILHLAQ SQEKTRREMT
AKGSTGMEVL LSTLENTKDL QTTLNILSIL VELVSAGGGR RASFLVAKGG SQILLQLLMN
ASKESPLNEE LMVQIHSILA KIGPKDKKFG VKARINGALN ITLNLVKQNL QNPRLVLPCL
QLLRVYSANS VNSVSLGKNG VVELLFKIIG PFSKKNSGLM KVALDTLAAL LKSKTNARRA
VDRGYVQVLL TIYVDWHRHD NRHRNMLIRK GILQSLKSVT NIKLGRKAFI DANGMKILYN
TSQECLAVRT LDPLVNTSSL IMRKCFPKNR LPLPTIKSSF HFQLPVIPVT GPVAQLYSLP
PEVDDVVDES DDNDDIDLEA ENETENEDDV DQNFKNDDIE TDINKLKPQQ EPGRTIEELK
MYEHLFPELV DDFQDYDLIS KEPKPFVFEG KVRGPIVVPT AGEEASGNPG NLRKGIVRTN
VSPKADESDK KHTCVDLAKE DIKDNDRTSQ QQLGDQNRTI SSAQGLNNDI VKALDRITLQ
NIPPQTAPGF TAGAKKDYSL PLTVLTCTKA CPHMATCGNV LFEGRTVQLG KLCCTGVETE
DDEDTESTSS VEQASVEVSD GPTLHDSDLY IEIVKNTKSV PEYSEVAYPD YFGHIPPPFK
EPILERPYGV QRTKIAQDIE RLIHQSDIID RVVYDLDNPN YAIPEEGDIL KFNSKFESGN
LRKVIQIRKN EYDLILNSDI NSNHYHQWFY FEVSGMRPGV AYRFNIINCE KSNSQFNYGM
QPLMYSVQEA LNARPWWIRV GTDICYYKNH FSRSSVAAGG QKGKSYYTIT FTVNFPHKDD
VCYFAYHYPY TYSTLQMHLQ KLESAHNPQQ IYFRKDVLCE TLSGNTCPLV TITAMPESNY
YEHICQFRNR PYVFLSARVH PGETNASWVM KGTLEYLMSN NPTAQSLRES YIFKIVPMLN
PDGVINGNHR CSLSGEDLNR QWQSPNPDLH PTIYHAKGLL QYLAAVKHLP LVYCDYHGHS
RKKNVFMYGC SIKETVWHTN DNATSCDVVE DAGYRTLPKI LSHIAPAFCM SSCSFVVEKS
KESTARVVVW REIGVQRSYT MESTLCGCDQ GKYKGLQIGT RELEEMGAKF CVGLLRLKRL
TSPLEYNLPS GLLDFENDLI ESNCKVTRKL GSSELQILPP IL
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