ID H0WW93_OTOGA Unreviewed; 943 AA.
AC H0WW93;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=AE binding protein 1 {ECO:0000313|Ensembl:ENSOGAP00000006638.2};
GN Name=AEBP1 {ECO:0000313|Ensembl:ENSOGAP00000006638.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000006638.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000006638.2}
RP IDENTIFICATION.
RG Ensembl;
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}.
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DR EMBL; AAQR03137142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WW93; -.
DR STRING; 30611.ENSOGAP00000006638; -.
DR Ensembl; ENSOGAT00000007424.2; ENSOGAP00000006638.2; ENSOGAG00000007419.2.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158323; -.
DR HOGENOM; CLU_006722_0_1_1; -.
DR InParanoid; H0WW93; -.
DR OMA; YIRRQKR; -.
DR TreeFam; TF315592; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1904026; P:regulation of collagen fibril organization; IEA:Ensembl.
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:UP000005225}.
FT DOMAIN 341..498
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 1..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 106754 MW; 28E39E083FB7CE42 CRC64;
EGFLSELEPE PREDDLEAPP PSEPTLRVQK AQAGDKSGTR SGEIGEASPG KAKDKGKKGK
KDKGPKVTKQ SQEGSPRPPK KGKEKPPKAT KKPKEKPPKA TKKPKEKPPK ATKKPKEKPP
KATKRPPTGK KPPTLASETL EWPLPPPHSL GPEEPPQEGG GPFPNNWQGP DKETHLETRE
PQPEPEEETE LPTLDYNDQI EREDYEDFEY IRRQKQPRPP LSRRRPERLW PQRPEEKAES
PEERTEPPLK PLLPLLPPDY GDGYVIPTYD DMDYYFRPPP PQKPDTERQT DEEKEELKKP
KKEGSPKEDE TDQWAVEKDK DHKGPRKGEE SEEEWTPKEK VKCPPIGMES HRIEDNQIRA
SSMLRHGLGA QRGRLNIQAG ANEDDYYDGA WCAEDDARTQ WIEVDTRRTT LFTGIITQGR
DSSIHDDFVT TFFVGFSNDS QTWVMYTNGY EEMTFHGNVD KDTPVLSELP EPMVARFIRI
YPLTWNGSLC MRLEVLGCPV SPIHSYYAQN EVVATDDLDF RHHSYKDMRQ LMKVVNEECP
TITRTYSLGK SSRGLKIYAM EISDNPGEHE LGEPEFRYTA GIHGNEVLGR ELLLLLMQYL
CREYRDGNPR VRSLVQDTRI HLVPSLNPDG YEVAAQMGSE FGNWALGLWT EEGFDIFEDF
PDLNSVLWGA EEKKWVPYRV PNNNLPIPER YLSPDATVST EVRAIIAWME KHPFVLGANL
NGGERLVSYP YDMARTPSQE QLLAAAMAAA RGEDEDEISE VQETPDHAIF RWLAISFAST
HLTMTEPYRG GCQAQDYTGG MGIVNGAKWN PRSGTINDFS YLHTNCLELS IYLGCDKFPH
ESELPREWEN NKEALLTFME QVHRGIKGVV TDEQSIPIAN ATISVSGIKH GVKTASGGDY
WRILNPGEYR VTAHAEGYTP SAKTCNVDYD IGATQCNFIL ARS
//
