ID A0A3Q7TDA8_VULVU Unreviewed; 470 AA.
AC A0A3Q7TDA8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ADAM DEC1 {ECO:0000313|RefSeq:XP_025863571.1};
GN Name=ADAMDEC1 {ECO:0000313|RefSeq:XP_025863571.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025863571.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025863571.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025863571.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025863571.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_025863571.1; XM_026007786.1.
DR AlphaFoldDB; A0A3Q7TDA8; -.
DR STRING; 9627.ENSVVUP00000006261; -.
DR Ensembl; ENSVVUT00000008373; ENSVVUP00000006261; ENSVVUG00000004882.
DR KEGG; vvp:112926722; -.
DR OMA; ITKPVCG; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF125; ADAM DEC1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 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; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..470
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018645295"
FT DOMAIN 217..412
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 420..460
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 369..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 470 AA; 53432 MW; 53FC046AE16D5C65 CRC64;
MLCATSQLTA VGNMSLTLLS VLWLIIQTQA IAIKQTPELE LYEVVRPKKL HILYKREIQN
HQTENGKDER YEPELQYQIV LNGKEVVLHL QKSKHLLGPD YTETYYSPRG EEITTSPRNM
EHCYYKGHIL NEKDSVASIN TCNGLRGYFT HHNQRYVIKP LKSTDQEEHA ILTYNQEELD
LANHTCGIRN VGRKQGHIRT SRSLNSPEQE DFLQAEKYID LFLVLDNAFY NIYKGNLTSI
RSFVFDVMNL LNVIYNTLDI QVALVGMEIW SDGDKIKVVP NTGDTFNNFL NWHRSNLRKM
KIHDHAQLLS GLGFDNRRVG MAASNSLCSP SSVAVIEAKR KNNVALVGLM SHELGHVLGM
PDIPYYTKCP SGSCVMNQYL SSKFPKDFST SCRSHFERYI LSQKPKCLLQ APIPKNIITK
PVCGNQLLEV GEDCDCGSPK ECSNPCCEAK TCKLKSKADC RKETLNHIIE
//
