ID A0A2Y9KCR5_ENHLU Unreviewed; 826 AA.
AC A0A2Y9KCR5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 17 isoform X1 {ECO:0000313|RefSeq:XP_022369339.1};
GN Name=LOC111154187 {ECO:0000313|RefSeq:XP_022369339.1};
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_022369339.1};
RN [1] {ECO:0000313|RefSeq:XP_022369339.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022369339.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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_022369339.1; XM_022513631.1.
DR AlphaFoldDB; A0A2Y9KCR5; -.
DR STRING; 391180.A0A2Y9KCR5; -.
DR KEGG; elk:111154187; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd14246; ADAM17_MPD; 1.
DR CDD; cd04270; ZnMc_TACE_like; 1.
DR Gene3D; 4.10.70.30; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR034025; ADAM10_ADAM17.
DR InterPro; IPR032029; ADAM17_MPD.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF6; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 17; 1.
DR Pfam; PF16698; ADAM17_MPD; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13688; Reprolysin_5; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..826
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016126865"
FT TRANSMEM 668..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..470
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 471..559
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 725..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..755
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 826 AA; 92873 MW; B64B40A994585CEF CRC64;
MRQCLLFLTS VVPFVLAPRP PDDSPERLEK LDSLLSDYDI LSLSNIQQHS VRKRDLQAST
HLETLLTFSA LKRHFKLYLT SSTEHFSQNF KVVVVDGKDE SEYTVKWQDF FRGHVVGEPD
SRVLAHIGDD DITIRINTDG AEYNIEPLWR LINDTKDKRI LVYKSEDIKN VSRLQSPKVC
GYIKADNEEL LPKGLVDREP PDELVHRVKR RADPNPMKNT CKLLVVADHR FYRYMGRGEE
STTTNYLIEL IDRVDDIYRN TSWDNAGFKG YGIQIEQIRI LKSPQEVKPG ERHYNMAKSY
PNEEKDAWDV KMLLEQFSFD IAEEASKVCL AHLFTYQDFD MGTLGLAYVG SPRANSHGGV
CPKAYYSPIG KKNIYLNSGL TSTKNYGKTI LTKEADLVTT HELGHNFGAE HDPDGLAECA
PNEDQGGKYV MYPIAVSGDH ENNKMFSNCS KQSVYKTIES KAQECFQERS NKVCGNSRVD
EGEECDPGIM YLNNDTCCSS DCMLRAGVQC SDRNSPCCKN CQFETAQKKC QEAINATCKG
VSYCTGDSSE CPPPGNAADD TVCLDLGKCK DGKCVPFCER EQQRESCACN ETDNSCKVCC
RDPSGRCVPY VDAEQKNLFL RKGKPCTVGF CDMNGKCEKR VQDVIERFWD FIDQLSINTF
GKFLADNIVG SVLVFSLIFW IPFSILVHCV DKKLDKQYES LSLFHPSNVE MLSSMDSASV
RIIKPFPAPQ TPGRPQPLQP LQVASAPPLP PAAPKLEPQR MDTIQEDPST DSHADEDGFE
KDPFPNSGTA AKSFEDLTGR PVPRSEKAAS FKLQRQNRVG SKETEC
//
