ID A0A2K6FPT9_PROCO Unreviewed; 1275 AA.
AC A0A2K6FPT9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
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|Ensembl:ENSPCOP00000016005.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000016005.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000016005.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A2K6FPT9; -.
DR STRING; 379532.ENSPCOP00000016005; -.
DR Ensembl; ENSPCOT00000026627.1; ENSPCOP00000016005.1; ENSPCOG00000019757.1.
DR GeneTree; ENSGT00940000157707; -.
DR OMA; LEYNMPS; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0098957; P:anterograde axonal transport of mitochondrion; IEA:Ensembl.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0098958; P:retrograde axonal transport of mitochondrion; IEA:Ensembl.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT DOMAIN 761..835
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 927..1033
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 143533 MW; 11C41CA521BE18F3 CRC64;
MRAGSAASAA ASASPATGVC MKTPGSGRRG IRREPGVEPS AAAVRSPASA LLTNNSRVVG
LLAQLEKINT ESTESDTARY VTSKILHLAQ SQEKTRREMT AKGSTGMEVL LSTLENTKDL
QTTLNILSIL VELVSGGGGR RASFLVSKGG SQILLQLLVN ASKESPPHEE LMVQIHSILA
KIGPKDKKFG VKARINGTLN ITLNLVKQNL QNHRLVLPCL QLLRVYSANL KIKLEVSKDN
QLSNLVFKEI GHFILNNLIE KYLIYSTAFF CHLKNILSQF SFVKETNARR AVDRGYVQVL
LTIYVDWHRH DNRHRNMLIR KGILQSLKSV TNIKLGRKAF TDANGMKILY NTSQECLAVR
TLDPLVNTSS LIMRKCFPKN RLPLPTIKSC FHFQLPVIPV TGPVAQLYSL PPEVDDVVDE
SDDNDDIDLE AENETENEDD LDQNFKNDDI ETDINKLKPQ QEPGRKIEEL KMYEHLFPEL
IDDFQDYDLI SKEPKPFVFE GKVHGPIIVP TAGEEASGNS GNLRKGLAMK ENGSPKGDKK
ATLVDPAKED IKDNDRTLQQ QLGDQNRTTS SAHGLNNDIV KALDRITLQN IPSQTTPGFA
TGMKKDHGLP LTVFTCTKAC PHLATCGNVL FEGRTVQLGK LCCTGVETED DEDSESNSSV
EQASVEVPDG PTLHDPDLYI EVVKNTKSVP EYSEVAYPDY FGHIPPPFKE PILERPYGVQ
RTKIAQDIER LIHQSDIIDR VVYDLDNPNY IIPEEGDILK FNSKFESGNL RKVIQIRKNE
YDLILNSDIN SNHYHQWFYF EVSGMRPGVA YRFNIINCEK SNSQFNYGMQ PLMYSVQEAL
NARPWWIRMG TDICYYKNHF SRSSAAAGGQ KGKSYYTITF TVNFPHKDDV CYFAYHYPYT
YSTLQMHLQK LESAHNPQQI YFRKDVLCET LSGNSCPLVT ITAMPESNYY EHICQFRNRP
YVFLSARVHP GETNASWVMK GTLEYLMSNN PTAQSLRESY IFKIVPMLNP DGVINGNHRC
SLSGEDLNRQ WQSPNPDLHP TIYHAKGLLQ YLAAVKRLPL VYCDYHGHSR KKNVFMYGCS
IKETVWHTND NATSCDVVED MGYRTLPKIL SHIAPAFCMS SCSFVVEKSK ESTARVVVWR
EIGVQRSYTM ESTLCGCDQG KYKGLQIGTR ELEEMGAKFC VGLLRLKRLT SPLEYNMPSS
LLDFENDLIE SSCKVTSPTT YVLDEDEPRF LEEVDYSAES NDELDIELVE NAGDYEPSAQ
EEVLSDSELS RTYLP
//
