ID I3MD70_ICTTR Unreviewed; 429 AA.
AC I3MD70;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Carboxypeptidase A5 {ECO:0000313|Ensembl:ENSSTOP00000008287.3};
GN Name=CPA5 {ECO:0000313|Ensembl:ENSSTOP00000008287.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000008287.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000008287.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AGTP01066048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MD70; -.
DR STRING; 43179.ENSSTOP00000008287; -.
DR Ensembl; ENSSTOT00000009238.3; ENSSTOP00000008287.3; ENSSTOG00000009234.3.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161666; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; I3MD70; -.
DR OrthoDB; 3540647at2759; -.
DR TreeFam; TF317197; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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:UniProtKB-KW.
DR CDD; cd03870; M14_CPA; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR034248; CPA_M14_CPD.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF16; CARBOXYPEPTIDASE A5; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012022812"
FT DOMAIN 180..202
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 316..326
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 429 AA; 48333 MW; B0B04C225AFB3F7E CRC64;
MLGVPRGGTG RQILLVFSIM LAAAWGQMNF TGDQVLRVLA KDEEQLSLLR DLEGLKPQKV
DFWRGPARPS LPVDMRIPFS ELNDIKAYLE SHGLAYSVMI KDIQVLLNEE REAMARSRRL
ERSTSSFSYS SYHTLEEIYS WIDNFVAENS NIVSKIHIGN SFENRSILVL KFSTGGSRRP
AIWIDTGIHS REWITHATGI WTAKKIVIEF GKNGLLTNIL KAMDIFIELV TNPDGFAFTH
SMNRLWRKNK SSRPGIFCIG VDLNRNWKSG FGGNGSNSNP CSETYHGPSP QSEPEVAAIV
NFITKHGNFK VLISIHSYSQ MLMYPYGHSM ESVSNEKELH SLAQDAVKAL YQVHGIQYIF
GSISATLYVA SGITVDWAYD NGIKYAFSFE LRDTGRYGFL LPATQIVPTA QETWMAILTI
MKHALHHPY
//
