ID A0A3B4F4X9_9CICH Unreviewed; 827 AA.
AC A0A3B4F4X9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 17-like {ECO:0000313|Ensembl:ENSPNYP00000005650.1, ECO:0000313|RefSeq:XP_005732837.1};
GN Name=ADAM17 {ECO:0000313|Ensembl:ENSPNYP00000005650.1};
GN Synonyms=LOC102205708 {ECO:0000313|RefSeq:XP_005732837.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000005650.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000005650.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005732837.1}
RP IDENTIFICATION.
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_005732837.1; XM_005732780.1.
DR AlphaFoldDB; A0A3B4F4X9; -.
DR Ensembl; ENSPNYT00000005794.1; ENSPNYP00000005650.1; ENSPNYG00000004303.1.
DR GeneID; 102205708; -.
DR CTD; 560657; -.
DR GeneTree; ENSGT00940000155443; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; 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 Reference proteome {ECO:0000313|Proteomes:UP000695023};
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..827
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041167046"
FT TRANSMEM 670..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 223..472
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 473..561
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 735..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 827 AA; 92305 MW; D8BE581577AC5BF0 CRC64;
MWLLFAFLAA FTALTKAAVP PDTTEQDFMS LRAMLDDFDV LPLSSLQTHS VRRRDVQTQT
HVEKLISFSA LQRHFRLYLR TNDELFTSDF RAVVISEDGQ ESTYPVNRHN YFTGHVIGEE
NSRVQAHIED DEFSAHILTD EAEYNVEPLW RFTSAPSGGR LLIYRSEDIR NISRLQQPSV
CGYVTSDPSD LLPDSVKAAV MEEKEEEESA FRVKRHVHDH KKNSCPLLLV ADHRFFKHMG
RDEESTTLNY LIELIDRVDD IYRNTSWDEG FSGYGVQIDQ IIIKKYPTPV DPGKTHFNMK
GSPVEGRDVW DVKKLLEQFS VDIAGKASNV CLAHLFTYQD FDEGTLGLAY VAPSKADIAG
GLCSKASPST LNEQGVIYLN TGLTSTKNYG KTILTKEADL VTTHELGHNF GAEHDPDKPE
CAPREDQGGK YVMYPIAVSG DHVNNKMFSD CSKRSIVKRL RLKAPSCFKE RKINVCGNSR
VEQGEECDPG LLHINSDLCC TPNCRLKADA QCSDRNSACC RECRFEAKGA VCQEPIDATC
KGHSYCTGNS SECPPPENAP DKTACLDSGE CLNGECIPFC QAVLKLQPCA CNETNASCKV
CCRSSGGVCT PYQDISGSFL FLRKGKPCTV GFCDGAGKCM KQVQDVVERL WDFIDKLDIN
TFWKFLADNI VGSVVAFSLL FWVPFSILVH CVDRKLDRQY EQTTKSLLFP SNAELLSSLD
SASVRIFKSP TFSSGPLRFH PSGPEQTGAD PAQSPPPLDS PRMATIQEDP SSDSHLEEAS
LEEAFGRPAG ATRRSFEDLT EKMSRSEKAK VFRLQRQHQI DSKETQC
//
