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Database: UniProt
Entry: H0VPR2_CAVPO
LinkDB: H0VPR2_CAVPO
Original site: H0VPR2_CAVPO 
ID   H0VPR2_CAVPO            Unreviewed;       540 AA.
AC   H0VPR2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=ATP/GTP binding protein like 4 {ECO:0000313|Ensembl:ENSCPOP00000012501.3};
GN   Name=AGBL4 {ECO:0000313|Ensembl:ENSCPOP00000012501.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000012501.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000012501.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000012501.3};
RG   Ensembl;
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   -!- 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}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; AAKN02052022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02052031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0VPR2; -.
DR   STRING; 10141.ENSCPOP00000012501; -.
DR   Ensembl; ENSCPOT00000014013.3; ENSCPOP00000012501.3; ENSCPOG00000013872.4.
DR   VEuPathDB; HostDB:ENSCPOG00000013872; -.
DR   eggNOG; KOG3641; Eukaryota.
DR   GeneTree; ENSGT00940000155042; -.
DR   HOGENOM; CLU_812693_0_0_1; -.
DR   InParanoid; H0VPR2; -.
DR   OMA; LRLWFNF; -.
DR   TreeFam; TF352938; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000013872; Expressed in testis and 4 other cell types or tissues.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005814; C:centriole; IEA:Ensembl.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; 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:0098957; P:anterograde axonal transport of mitochondrion; IEA:Ensembl.
DR   GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; 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:0120222; P:regulation of blastocyst development; IEA:Ensembl.
DR   GO; GO:0098958; P:retrograde axonal transport of mitochondrion; IEA:Ensembl.
DR   CDD; cd06908; M14_AGBL4_like; 1.
DR   Gene3D; 2.60.40.3120; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF9; CYTOSOLIC CARBOXYPEPTIDASE 6; 1.
DR   Pfam; PF18027; Pepdidase_M14_N; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   DOMAIN          169..458
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   REGION          451..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  61907 MW;  357332D847EE2149 CRC64;
     MAERSQTAPE AGNNTGNDDV IGGNVSKYMV LPTGYCGQPK KGHLIFDACF ESGNLGRVDQ
     VSEFEYDLFI RPDTCNPRFR VWFNFTVENV KESQRVIFNI VNFSKTKSLY RDGMAPMVKS
     TSRPKWQRLP PKNVYYYRCP DHRKNYVMSF AFCFDQEEDT YQFAYCYPYT YTRFQHYLDS
     LQKRNMNYFF REQLGQSVQQ RQLDLLTITS PENLREGAEK KVIFITGRVH PGETPSSFVC
     QGIIDFLVSN HPIACILREH LVFKIAPMLN PDGVYLGNYR CSLMGFDLNR HWLDPSPWAH
     PTLHGVKQLI IQMYNDPQTS LEFYIDIHAH STMMNGFMYG NIFEDEERFQ RQAIFPKLLC
     QNAEDFSYSS TSFNRDAVKA GTGRRFLGGL LDHTSYCYTL EVSFYSYITG GTTAAVPYTE
     EAYMKLGRNV ARTFLDYYRL NPLLEKVAVP MPKPRSSEER RLEGEHPSYL RAGQEPDVLS
     APMPAGSQPG EHLGSDIQRH LECAGPALSL DLITYSPSGP ASWKDMTMSN NLLLPDHSSH
//
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