ID   A0A087X6X0_POEFO        Unreviewed;       828 AA.
AC   A0A087X6X0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Si:ch1073-459j12.1 {ECO:0000313|Ensembl:ENSPFOP00000001523.2};
GN   Name=AEBP1 {ECO:0000313|Ensembl:ENSPFOP00000001523.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000001523.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000001523.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; AYCK01029412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A087X6X0; -.
DR   STRING; 48698.ENSPFOP00000001523; -.
DR   Ensembl; ENSPFOT00000001526.2; ENSPFOP00000001523.2; ENSPFOG00000001548.2.
DR   eggNOG; KOG2649; Eukaryota.
DR   GeneTree; ENSGT00940000158323; -.
DR   OMA; QENYGYH; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF48; ADIPOCYTE ENHANCER-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..828
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001832430"
FT   DOMAIN          23..180
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          485..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  94240 MW;  F440712B75060F9F CRC64;
     MVKIYFFFFL IVSSHSFVPP HVAECPPLGM ESHKIESDQL TASSMSQYAF SPQRARLNMQ
     GSEDEDNMRG GAWCANSEDR IHWFEVDARR ETEFTGVVTQ GRDALNESDF VTSYFLAFSN
     DSREWTTIHD GYADWLFFGN NDKDTPVMNR LAEPVLARYI RIIPQSWNGS LCMRLEVLGC
     PVPDPGGALY RQNEVTPVDY LEFKHHSYSE MVELMKSVHE ECPNITNIYS LGRSSKGREI
     MAMIISGNPT EHEIGEPEFR FTAGLHGNEA VGRELILLLM QYLCKEYKDR NPRAQRLVEG
     IRIHLVPSLN PDGHETAFEV GSEMSSWTMG HFTEDGFDIF QNFPDLNSIL WDAEDKGMVP
     KLTPNHHVPI PENFEFNTSI AMETRAIISW MKAYPFVLGA NFQGGEAIVA YPYDSLRLNK
     PAKSEQSRSR KKRQYEDEGF DVTEWGRGYQ EEPEEDWRSR GYAEPEEEWR GHGYDHGYDH
     GYDPGYEHGY SQGYGHREEE EDDGGRGAGF HYSEPEDEPR LTPDESLFRW LAVSYASTHL
     TMTHNYRGSC HGDIPAGAVG MVNRAKWKPV TGSMNDFSYL HTNCYELSIF LGCDKFPHQS
     ELAQEWEKNR EAMLTFMEQV HRGIRGIVKD QQGNPIANAT ISVEGINHDV TTAPTGDYWR
     LLNPGEYRVT AKAEGFSSET KLCVVGYESG ATSCSFNLAK SNWDRIKQIM ALHGNKPIRL
     SYSNSRTQTS SRSSGSQKRV ISGGNGFSSN SNASPQRMRM LRIARIRRLR QQRLMRLRLS
     LTTTMPTTTT TTTTAAPTTS WYDSWGLGEA ESVTPVLDYN YEYKIDDY
//