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Database: UniProt
Entry: A0A2T7NRZ2_POMCA
LinkDB: A0A2T7NRZ2_POMCA
Original site: A0A2T7NRZ2_POMCA 
ID   A0A2T7NRZ2_POMCA        Unreviewed;      1133 AA.
AC   A0A2T7NRZ2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C0Q70_17221 {ECO:0000313|EMBL:PVD23945.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD23945.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD23945.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD23945.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD23945.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVD23945.1}.
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DR   EMBL; PZQS01000010; PVD23945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7NRZ2; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg10.
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   Gene3D; 2.60.40.3120; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR040626; Pepdidase_M14_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR12756:SF12; CYTOSOLIC CARBOXYPEPTIDASE-LIKE PROTEIN 5; 1.
DR   Pfam; PF18027; Pepdidase_M14_N; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          10..151
FT                   /note="Cytosolic carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18027"
FT   DOMAIN          239..314
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
FT   REGION          355..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..839
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  125784 MW;  50C17BB0AAA10007 CRC64;
     MEARFGNLTF TSKFDSGNLA RVEKVSKEDD EEVSNANVNY YLGDLRHDAE FNLWTKPDCA
     GSPAENSNRS WFYFGVRGWV PNRLIKFNIM NMNRQGKLYG QGYTPLTRLL PSRPKWERIR
     DKPTFEVIDN QFILTFTYRF PDLKGGTCYF AFSYPWSYTE SQEQLQILDK RFEHCLHMSP
     GSPPERLYYH RELLCYSLDK LRVDLLTITS CHGNTFCRET RFDKHLFPDQ DTPRCYKFKD
     KRVFLLSSRV HPGETPGSFV FNGFLDFILR ENDLRAAQLR QQYVFKLIPM LNPDGVMRGH
     YRTDQRGMNL NRMYLDPSPI LHPSIYAAKS LLVYHHVMNQ LPRLGGEPLK IHINFPCDEQ
     SSGKDGPGVP NSPQERSGGD QDVLQSGEHD ITLSSDSHKQ TTRRQNETKT KSYQHPLVSA
     SLKHVPAIQS NSEKWLEANI AGGTTSLELL SQQESAKVEP LNLTDLYMSD ESASDSCPPA
     GLENNQIFHV SSSSSSVVSL DKLHLPATGM VNGQAEMHHV DSELCLHLSE LNMSEDLCSN
     TLADDASFDS DTEATERLGN EGSEDEEASP VTLEGLSGNC SPHLSDAQLL EIHPHDSGVA
     FYMDLHGHAS KRGCFIYGNY FDNEDIQLES ILYAKLIALN SAHFDFGACN FSERNMYLKD
     KRDGFSKEGS GRVAIYKAIG IIHSYTLECN YNMGRLVNSV PPAFRDDGRA TPPPLAGFPP
     KFTQAHYEEV GRAVAVAVLD MRDTNPWSRV SLSEYNSIHG LRDWVRRYLR SLRGGPRIPR
     NPSLKSMNKN GNNGLPGKSD LTPVQNTTRV SAGRVIGLDS SSRASAIRQT SQNSATTGRR
     ELAPVKEATR NTTFSNMRTQ MRRHSSTSSS PPKLSSLSGP SLPVPPVQTQ GNSEHYSMMT
     TSSIAADTKV AIARRGGPTS RIPLPTSQSR LTLTAQANSL SDAGLTSADA SLSRTLPASL
     LQSTMQNQPL AQVHIVGSQM LQASAPPPSP THSQAQEAPQ PSRALMSLAG APSLSSTHSL
     LHKDQLQPPT GLKSLTGIGE SKSPRRRYWN VRRRTQVASP KPGVAKGQNK GAVSGGGDVE
     PAKSHRCKRR GPRKPIVVNE APVVVSSKMT AVQEEEMGQG ISSFLFYFHK NLF
//
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