ID A0A3B5ASZ4_9TELE Unreviewed; 826 AA.
AC A0A3B5ASZ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 17-like {ECO:0000313|Ensembl:ENSSPAP00000024558.1};
GN Name=ADAM17 {ECO:0000313|Ensembl:ENSSPAP00000024558.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000024558.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000024558.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B5ASZ4; -.
DR Ensembl; ENSSPAT00000024965.1; ENSSPAP00000024558.1; ENSSPAG00000018484.1.
DR GeneTree; ENSGT00940000155443; -.
DR Proteomes; UP000261400; 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 InterPro; IPR002870; Peptidase_M12B_N.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF5; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 17; 1.
DR Pfam; PF16698; ADAM17_MPD; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF13574; Reprolysin_2; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
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_5017406496"
FT TRANSMEM 663..685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..465
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 466..554
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 726..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..757
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 406
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; 92777 MW; 0F7238F9940B8EF0 CRC64;
MRRQLTFMTV FIVLTEAAVS PPADTAGQDF SKSSLRSMLD DFDVLPLASL QTHSVRRRDV
QTQTHVEKLL SFNALQRQFR LYLRTNDELF TEDFRAVVVD EDGRERSYPV NRHNYFTGHV
IGEENSRVQA HIDDHEFSAR ILTDEAEYNV EPLWRFTSAP PDGRLLIYRS EDIRNISRLQ
QPSVCGYVTS DPNQLLPDKS VFREKRQVHD HKKNTCPLLL VADHRFFKHM GREEESTTLN
YLIELIDRVD DIYRNTSWDD EFSGYGVQIQ QIIIEKSPTP VAPGKSHFNM RGSPLKDRDV
WDVKKLLEQF SVDIAEKASN VCLAHLFTYQ DFDEGTLGLA YVAPSKPDIP GGLCSKVALL
VFINPTSSIY LNTGLTSTKN YGKTILTKEA DLVTTHELGH NFGAEHDPDN IPYCAPREDQ
GGKYVMYPIA VSGDHVNNKL FSNCSKRSIV KRLRTKAPSC FKERNINVCG NSRVEQGEEC
DPGLLHINSD RCCTDHCRLR VGAQCSDRNS ACCKNCRFES EGEVCQEPID ATCKGHSYCT
GNSSECPPPE NAPDKTVCLD NGECLNGECI PFCQAILNLQ PCACNETNSS CKVCCRSSSG
VCAPYQDQTG SFLYLRKGKP CTVGFCDGAG KCMKQVQDVV ERLWDFIDKL DINTFGKFLA
DNIVGSVVAF SLLFWVPFSI LVHCVDKKLD KQYEQTTKSL FFPSNAELLS SLDSAPVRIF
KPPTFPTAPM RFQPSGPQQT STPPVPSAGP TPPPLDSPRM ATIHEDPSLD SHLDEEALEE
AFVRPVGAAR RSFEDLTEKS VSSRSEKAKM FRLQRQHQID SKETQC
//
