ID A0A1S3WCT9_ERIEU Unreviewed; 1131 AA.
AC A0A1S3WCT9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Adipocyte enhancer-binding protein 1 {ECO:0000313|RefSeq:XP_016044198.1};
GN Name=AEBP1 {ECO:0000313|RefSeq:XP_016044198.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016044198.1};
RN [1] {ECO:0000313|RefSeq:XP_016044198.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_016044198.1; XM_016188712.1.
DR AlphaFoldDB; A0A1S3WCT9; -.
DR STRING; 9365.ENSEEUP00000005648; -.
DR CTD; 165; -.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; A0A1S3WCT9; -.
DR OrthoDB; 5490979at2759; -.
DR Proteomes; UP000079721; Unplaced.
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 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; PS01285; FA58C_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:UP000079721};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1131
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010266589"
FT DOMAIN 372..529
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 37..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1049
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 127387 MW; 1AD0F3A3D211E98A CRC64;
MGAPLLGCLL ILLALWPGGR PQTVLTDDEI EEFLEGFLLE PREDNVEAPP EPTPGAGKAQ
ARDKPGAAKE ALPEKAKDKG KKGKKEKGPK ATKESLEGPP KPTKKPKEKP PKATKKPKEK
PPKATKKPKE KPPKATKKPK EKSPKATKKP KAGKRPPTLS PSEILLLPLP PPTHLGPQEP
PQEQGSILRS HPESPGFESE KAVSPPELEE ETEMPTLDYN DQIEREDYED FEYYRRQKRP
RPPPTRRKPP RPEPPEEKAK PPGPGVDIPE ERPEPPLKPL PPPLPLPDYG DGYVIPDYDD
MDYYFPPPGR PQKPDMGLET DEEKEKLKKP KKEGSSPKED REDKWSVDKG RDHKGPPKEK
ELEEEWAPAE KIKCPPIGME SHRIEDNQIR ASSMLRHGLG AQRGRLNMQA GATEDDYYDG
AWCAEDDART QWIEVDTRRT TRFTGVITQG RDSSIHDDFV TSFFVGFSND SQTWVMYTNG
YEEMTFHGNV DKDTPVLSEL PEPMVARFIR VYPLTWNGSL CMRLEVLGCP VSPIHSYYAQ
NEVVTTDNLD FRHHSYKDMR QVMKLVNEKC PTITRTYSLG KSSRGLKIYA MEISDNPGDH
EVGEPEFRYT AGIHGNEVLG RELLLLLMQY LCREYLDGNP RVRSLVHDTR IHLVPSLNPD
GYEVAAQMGS EFGNWALGLW SEEGFDIYED FPDLNSVLWG AEERKWVPYR VPNNNLPIPE
RYLSPEATVS TEVRAIIAWM EKNPFVLGAN LNGGERLVSY PFDMARTPTP EQLRAAALAA
AQGDEEEVSE AQETPDHAIF RWLGIAFASA HLTMTEPYRG GCQAQDYTGG MGIVNGAKWN
PRAGTINDFS YLHTNCLELS IYLGCDKFPH ESELPREWEN NKEALLTFME QVHRGIKGVV
TDEQGIPIAN ATISVSGINH GVKTASGGDY WRILNPGEYR VTAHAEGYTP SAKTCSVDYD
IGATQCNFVL ARSNWKRIRE ILAMNGNRPI PRVDPSRPMT PRQRLAQRRR LQQRLRMREQ
MRLRRLNATS TSAPPPTLPP PPSSPSLVPS MAPSPTAGPW HFPPETTANW EELETETYTE
VVTEFGTELG PEKEWEEEEG EDRGEEEEEE AFGLEFPDTT VETYTVNFGD F
//
