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Database: UniProt
Entry: A0A2Y9L010_ENHLU
LinkDB: A0A2Y9L010_ENHLU
Original site: A0A2Y9L010_ENHLU 
ID   A0A2Y9L010_ENHLU        Unreviewed;       470 AA.
AC   A0A2Y9L010;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=ADAM DEC1 {ECO:0000313|RefSeq:XP_022374760.1};
GN   Name=LOC111157544 {ECO:0000313|RefSeq:XP_022374760.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022374760.1};
RN   [1] {ECO:0000313|RefSeq:XP_022374760.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022374760.1};
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_022374760.1; XM_022519052.1.
DR   AlphaFoldDB; A0A2Y9L010; -.
DR   STRING; 391180.A0A2Y9L010; -.
DR   KEGG; elk:111157544; -.
DR   OrthoDB; 5406290at2759; -.
DR   Proteomes; UP000248482; 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   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:UP000248482};
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_5015868156"
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;  52795 MW;  12F39441F440C161 CRC64;
     MLCGTSQLSA VGNMSLALLS VLWLIIQTQA IAINQTSELE LYEVVHPKKL HILHKREIRN
     NQTENGKEER YEPELQYQIT LNGEEVVLHL QKSKHILRPD YSEIYYSPRG EEITTDPQNM
     EHCFYKGHIL NEKGSVASIS TCNGLRGYFT HHDQRYMIKP LKSTDQEEHA VLTYNQEEPD
     LANYTCGVRS VGRKQGHIRT SRSLNSPEEK NYLQAEKYID LLLVLDNAFY NMYKGNLTLI
     RSFVFDVMNL LNVIYNTIDV QVALVGMEIW SDGDKIKIVP NIGDTFNNFL NWHRSNLGKM
     KRHDHAQLLS GIGFSNRRVG MAASNSLCSS ASVAVIEASG KNNVALVGVM SHELGHVLGM
     PDVPYYTKCP SGSCVMNEYL SSKFPKDFSI SCRSHFKKYI LSQKPKCLLQ APTPKNIITN
     SVCGNKLLEA GEDCNCGSPK ECSNRCCEAV TCTLKPEAGC KGDTLNNITQ
//
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