ID A0A2K5YNI2_MANLE Unreviewed; 1174 AA.
AC A0A2K5YNI2;
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:ENSMLEP00000017111.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000017111.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000017111.1}
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; A0A2K5YNI2; -.
DR STRING; 9568.ENSMLEP00000017111; -.
DR Ensembl; ENSMLET00000040585.1; ENSMLEP00000017111.1; ENSMLEG00000032749.1.
DR GeneTree; ENSGT00940000157707; -.
DR OMA; LEYNMPS; -.
DR Proteomes; UP000233140; Unplaced.
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: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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 660..733
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 825..932
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 132812 MW; 361E531EBAEB9CD3 CRC64;
KFKLKLIFLD ITLKLGNLTN NSRIVGLLAQ LEKINAEPSE SDTARYVTSK ILHLAQSQEK
TRREMTAKGS TGMEILLSTL ENTKDLQTTL NILSILVELV SAGGGRRVSF LVTKGGSQIL
LQLLMNASKE SPPHEDLMVQ IHSILAKIGP KDKKFGVKAR INGALNITLN LVKQNLQNHR
LVLPCLQLLR VYSANSVNSV SLGKNGVVEL MFKIIGPFSK KNSSLIKVAL DTLAALLKSK
TNARRAVDRG YVQVLLTIYV DWHRHDNRHR NMLIRKGILQ SLKSVTNIKL GRKAFIDANG
MKILYNTSQV MDDVVDESDD NDDIDVEAEN ETENEDDLDQ NFKNDDIETD INKLKPQQEP
GRTIEDLKMY EHLFPELVDD FQDYDLISKE PKPFVFEGKV RGPIVVPTAG EETSGNSGNL
RKVVMKENIS SKEDEGEKKS TFMDLAKEDT KDNDRTLQQQ PGDQNRTISS VHGLNNDIVK
ALDRITLQNI PSQTAPGFTT EVKKDCSLPL TVLTCAKACP HMATCGNVLF EGRTVQLGKL
CCTGVETEDD EDTESNSSVE QASVEVPDGP TLHDPDLYIE IVKNTKSVPE YSEVAYPDYF
GHVPPPFKEP ILERPYGVQR TKIAQDIERL IHQSDIIDRV VYDLDNPNYT IPEEGDILKF
NSKFESGNLR KVIQIRKNEY DLILNSDINS NHYHQWFYFE VSGMRPGVAY RFNIINCEKS
NSQFNYGMQP LMYSVQEALN ARPWWIRMGT DICYYKNHFS RSSVAAGGQK GKSYYTITFT
VSFPHKDDVC YFAYHYPYTY STLQMHLQKL ESAHNPQQIY FRKDVLCETL SGNSCPLVTI
TAMPESNYYE HICHFRNRPY VFLSARVHPG ETNASWVMKG TLEYLMSNNP TAQSLRESYI
FKIVPMLNPD GVINGNHRCS LSGEDLNRQW QSPNPDLHPT IYHAKGLLQY LAAVKRLPLV
YCDYHGHSRK KNVFMYGCSI KETVWHTNDN ATSCDVVEDT GYRTLPKILS HIAPAFCMSS
CSFVVEKSKE STARVVVWRE IGVQRSYTME STLCGCDQGK YKGLQIGTRE LEEMGAKFCV
GLLRLKRLTS PLEYNLPSSL LDFENDLIES SCKVTSPTTY VLDEDEPRFL EEVDYSAESN
DELDIELAEN VGDYEPSAQE EVLSDSELSR TYLP
//
