ID A0A091DWC3_FUKDA Unreviewed; 727 AA.
AC A0A091DWC3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 5 {ECO:0000313|EMBL:KFO36439.1};
GN ORFNames=H920_02188 {ECO:0000313|EMBL:KFO36439.1};
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:KFO36439.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO36439.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO36439.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KN121427; KFO36439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DWC3; -.
DR eggNOG; KOG3607; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF28; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Integrin {ECO:0000313|EMBL:KFO36439.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 191..388
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 400..489
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DISULFID 344..349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 727 AA; 81217 MW; 9C4F74A49BCC23A5 CRC64;
MREKEQGSRV VNTLASLQLQ LPPILSLTAT FLYRFQRSPL LPDPWTPQDE VWKSDLLLTL
GSYSLNAIVK SFLASASVVY SYDKNGAQHS QSLLPRMDCS YSGYVVGFPH SLVALTTCSG
LRGVMQFKNI SYGIEPLEAM SGFMHMIYEE SNNDTHVPLF GENDTYAWLN TAKSKVRSGL
HKTEFTKLFP RYIEMYIIVD KNLFVYMGSD VKTVTLKVIR LIGFVNTMLT QLKLTVVIST
IELWSNTNKF ATTGHPDDVL FRFLQWKHQH ADPKPHYISY LLAFEKHPTR IGATFPGYMC
GNKYDAGVAL YPVGLSLESY AVIIVQLLGL NVGLVYDNTD TCHCLGDICT MTPKAAYSGV
LTHFSTCSLD SFKSLASRSG LDCLKNNPHD KPVYKQSSRK RICGNSVREE GEECDCGTKL
NCTHTKCCDP TSCRKKGSVV CGSGECCTTD CQLKKANTLC RPSIDKECDF DEFCTGKQGD
CVPDTYARDG SHCDAGGAFC FGGICRTFDR QCQSLIGGDS RGAPFACFEE VNSRGDSYGN
CGHNFCQLQH VLCGKLVCTW PHKRLVSREN LSVVYTHVRN DICVAGEKTV RKTVRASLST
YLEHTDRDET FVEDGSMCGP DMVTTYFKLL LKIEVIFTLI LYQPIYLSQH YYSGKMHVTK
IPILTILKCV ISSIKDIHNV QLSPSCFLIT RLFCFVETGS HDVVETDLKL CSPGWSRTYR
DPPASAF
//