ID A0A091DS18_FUKDA Unreviewed; 988 AA.
AC A0A091DS18;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Adipocyte enhancer-binding protein 1 {ECO:0000313|EMBL:KFO33065.1};
GN ORFNames=H920_05681 {ECO:0000313|EMBL:KFO33065.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO33065.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO33065.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO33065.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KN122106; KFO33065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DS18; -.
DR STRING; 885580.ENSFDAP00000008624; -.
DR MEROPS; M14.951; -.
DR eggNOG; KOG2649; Eukaryota.
DR Proteomes; UP000028990; 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 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:UP000028990}.
FT DOMAIN 313..470
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 112284 MW; 6F185D9C460A276C CRC64;
MEGGPEALLE KAKDKGKKGK KDKGPKATKQ PPSEGTPRPP KKGKEKPPQA TKKPKEKLPK
ATKKPKEKPP KATKKPKEKP PKATKKPKEK PPKATKRPPA VKKFSTPAPL ETEEWPLPPP
PHPGPEEPVQ EGEGTFPNGW QGPGEETHVA AREHQPELEE ETEILTLDYN DQIEREDYED
FEYIRRQKQP KVPPRRRFWP ERPEEKAEQP EERPEKKEET EPPLKPLLPD YGDGFVIPNY
DDMDYYFPLP PLPKPDAGQE TDEEKEELKK PKKEGSSPKE ETEDKWAVEK DKDHKGPQKG
EDLEEEWAPV EKIKCPPIGM ESHHIEDNQI RASSMLRHGL GAQRGRLNMQ AGTNEDDYYD
GAWCAEDDPH TQWIEVDTRR TTRFTGIITQ GRDSSIHDDF VTTFFVGFSN DSQTWVMYTN
GYEEMTFHGN VDKDTPVLSE LPEPVVARFI RIYPLTWNGS LCMRLEVLGC PVSPIYSYYT
LNEVVATDDL DFRHHSYKDM RQLMKLVNEE CPTITRTYSL GKSSRGLKIY AMEISDNPGE
HELGEPEFRY TAGIHGNEVL GRELLLLLMQ YLCREYRDGN PRVRSLVQDT RIHLVPSLNP
DGYEVAAQMG SEFGNWALGL WTEEGFDIFE DFPDLNSVLW GAEEKKWVPY RVPNNNLPIP
ERYLSPDATV STEVRAIITW MEKNPFVLGA NLNGGERLVS YPYDMAHTPS QEQLLAAAMA
AARGEDDEVS EAQETPDHAI FRWLAISFAS AHLTMTEPYR GGCQAQDYTN GMGIVNGAKW
NPRSGTINDF SYLHTNCLEL SIYLGCDKFP HESELPREWE NNKEALLTFM EQVHRGIKGV
VTDEQGIPIA NATISVSGIN HGVKTASGGD YWRILNPGEY RVTAHAEGYT PSAKTCNVDY
DIGATQCNFI LARSNWKRIR EIMAMNGNRP ILREYETETY TEVVTELGTE FGIELEPEEE
VEEEEEEITG LDLPFTTVET YTVNFGDF
//
