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Database: UniProt
Entry: A0A3Q2CU81_CYPVA
LinkDB: A0A3Q2CU81_CYPVA
Original site: A0A3Q2CU81_CYPVA 
ID   A0A3Q2CU81_CYPVA        Unreviewed;       808 AA.
AC   A0A3Q2CU81;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 17-like {ECO:0000313|Ensembl:ENSCVAP00000009229.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000009229.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000009229.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q2CU81; -.
DR   Ensembl; ENSCVAT00000000292.1; ENSCVAP00000009229.1; ENSCVAG00000011267.1.
DR   GeneTree; ENSGT00940000155443; -.
DR   OMA; NTTWNSE; -.
DR   Proteomes; UP000265020; 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:SF7; ADAM METALLOPEPTIDASE DOMAIN 17A ISOFORM X1; 1.
DR   PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR   Pfam; PF16698; ADAM17_MPD; 1.
DR   Pfam; PF00200; Disintegrin; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        633..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          196..436
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          437..525
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REGION          717..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        368
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   808 AA;  89991 MW;  3BDF916B836E9853 CRC64;
     MEAGFCSLFP ETLSSILSEY EVLPVSGFQL HSVRKRDVHS ESHLERLVSF RALQRDFKLY
     LTTNTELFTD NFKAVFVDKN GKEEKYDVSL QNYFTGHVVG EAHSRVQAHI DGDEFSAHIL
     TDETEYNIEP LWRFTDSPID GRLLVYRSQD IRNLSRIASP EVCGYIHAEA EDLFPEAARS
     ESLHRVKRQA HDHRKNTCPL LLVADYRFFK QMGRSQESIT LNYLIELIDR VDDIYRNTTW
     NNEFKDYGVQ IQQRPPGMSG AGWAHYNMEN SPVAGEEVWE VKKLLEQFSS DIAENASTVC
     LAHLFTYQDF DKGTLGLAYV APPRNTPLAY YPSHSAKKPS YLNTGLTSTK NYGKTILTKE
     ADLVTTHELG HNFGAEHDPD NLLNCAPSDD EGGKFVMYPI AVSGDHVNNK RFSDCSKASV
     GKSLQLKAPM CFKERNSKVC GNSRVEEGED CDPGLLHLND DLCCSPECKF RENVKCSDRN
     SPCCKNCQYQ QAGTKCQEPI SATCKGMSFC TGNSSQCPPP ENAMDDTICV DNGRCLKGEC
     KPFCEAIEKL QSCACNETSD SCKVCCRKHG ICSPFTYPDG TFLYLRKGKP CTVGFCDGNG
     KCMKQVQDVI ERLWDFIDKL DINTFGKFLA DNIVGSVVVF SLIFWIPLSI LVYCVVRSFK
     FFSSPAVFAP QTQDILSNPE SAPVRIVKHS QPPFAARAAP SSQPLLLQSQ ARSLTPAAAC
     SSTTTQDPGP SYAANQDSAG DLRMATIPED TSSDSHLVEE GLSGDFTTAG ASSSATKSSF
     EDLTGQNPSR ERRRLKRQEC LDSKETEC
//
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