ID   A0A212FCH2_DANPL        Unreviewed;       855 AA.
AC   A0A212FCH2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Carboxypeptidase A {ECO:0000313|EMBL:OWR51432.1};
GN   ORFNames=KGM_204790 {ECO:0000313|EMBL:OWR51432.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR51432.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR51432.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR51432.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
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:OWR51432.1}.
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DR   EMBL; AGBW02009192; OWR51432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212FCH2; -.
DR   STRING; 278856.A0A212FCH2; -.
DR   KEGG; dpl:KGM_204790; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   InParanoid; A0A212FCH2; -.
DR   Proteomes; UP000007151; 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   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 2.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 2.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 2.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:OWR51432.1};
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:UP000007151};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..855
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012781282"
FT   DOMAIN          124..407
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   DOMAIN          551..837
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   855 AA;  97641 MW;  79070EE6E16FDEDD CRC64;
     MFKPLLFFLA SIYVVYGKHE EYDGHSLYQV RVENAYQVDQ LMNVVERLLL DVWTYAQPEQ
     DGLILVSKEL KPLFEEELKS IGVEFAIDTE NIKDKLDLED QLLANASIAD AGRTHRGLSF
     DVIHRYAVVD RYLSDLARQY SNVRVASGGK SVEGRDIKYL RISSNNFQSG NKPVVVIQSL
     LHAREWVTLP VTLYAIHKLV IDVTEQDLIR DIDWVIIPIA NPDGYEFTHT RTRMWRKNRR
     TGFGRCIGVD LNRNFDFAWG IASSNQACAD TFHGPKAFSE PETQMTRDII NRYRSRIELF
     IDVHSFGSLI LYGYGNRQLP PHSNTLQQVA VEMARRIDAV KWPANRNYRV GNIAQVLYQA
     SGGCSDYAQA RIGNKLSYTY ELPAYRNLNN MNGFLVDPAF IRQAGYETWE GINGYSDCSP
     YPFSDWSYFS LSFVLTFCFV HAKHEMYDGH SLFKIKIQDE KQMKYLYSLA EVLDLDVWVL
     PFPGNDAAVL VSKESNEPFR SELSEYGFEF HIETDNIKRA LDLEDTLNEK ALRKNHFKSG
     YRGKIGFDRI YKLSEVDSYL ETLAESYPNT VTLVNAGKSF EGRDIKYLKI SSTNFQDVRK
     PIVFVESLLH AREWVTLPPT LWAIEKLVVN VTESDLIDTI DWIILPVANP DGYELTHNED
     RFWRKNRATG FVPGDFCVGV DLNRNFDIKW GSGSSSSVCS EIFHGSRPSS EPETVIISRI
     MEEYKNRIDL FIDLHSYGSM ILYGWGSGDL LPNAFSLQQI GLNMAKAIDD MKLIFNENYT
     VGNAGLVLYP ASGTAMDYAN RFNIPFSYVY ELPGSIFGTG LSGFLIEPEL VEHYAKETWE
     GIKTGARNVR DLLGR
//