ID A0A3Q3MQA7_9TELE Unreviewed; 973 AA.
AC A0A3Q3MQA7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12-like {ECO:0000313|Ensembl:ENSMAMP00000029818.2};
GN Name=ADAM12 {ECO:0000313|Ensembl:ENSMAMP00000029818.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000029818.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000029818.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3Q3MQA7; -.
DR Ensembl; ENSMAMT00000030591.2; ENSMAMP00000029818.2; ENSMAMG00000020105.2.
DR GeneTree; ENSGT00940000155495; -.
DR InParanoid; A0A3Q3MQA7; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
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:SF112; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 12; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 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; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..973
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030081561"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..432
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 440..526
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 672..704
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 843..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..867
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 498..518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 676..686
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 694..703
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 973 AA; 104923 MW; 4186A44925A29F32 CRC64;
MNPGSRSLKF VILTALQVLS VSLSVCDRVV FRSAEGNLLS TTVQHRPTAE QKHYGTTVPL
QLVGQDWKPI SQLKSQSHPA SLKLLIEVEG EQLLLALEKN EGLFASTYTE THYLEDGSAV
TASHDFTANC YYHGEVEGHV NSDVSLSICA GIKGFISLEG KSYVLEPSAD HSDGTHWIYT
AEHLNFAPGT CGHDFNISYP TGHADSSLFR AFSTRHKRHA QTTTKYVELI IVADNREFQK
QGKDIEKVKQ RLAEIANYVD KFYRALNIRV ALVGLEVWSD VDKCPITQDP FTTLHEFLDW
RKVKLLPQKP HDNAQLISGV YFQGTTIGMA PIMSMCTAEQ SGGIVMSLLC KDHSDNPLGA
AVTLAHELGH NFGMNHDTPE RGCGCRVTVD RGGCIMTPST GYPFPTVFSS CSKKDLTASF
EKGIGMCLFN MPEVKVLYGG QKCGNGYVEE GEECDCGELE ECMNPCCNAT TCTLKGDAVC
AHGQCCQDCQ LKPAGTPCRE SSNSCDLPEF CTGSSPHCPS NVYLHDGHTC HNVDGYCYNG
ICQTHEQQCI TLWGQGAKPA PGICFERVNS AGDPYGNCGK DSKGSFAKCE AQDAKCGKIQ
CQGGANRPVI GTNAVSIETN IPLQEGGRIL CRGTHVYLGD DMPDPGLVLT GTKCGDGMMC
LNRHCQNVSV FGVHECSAKC SGRGVCNNNK NCHCEAHWAP PFCDKVGFGG SVDSGPIRLA
GSGNVTVGIL VALLTVLGVG VIIYIKRKAL RGLLFTSKKN PIEKLRPVSA AVSGLPPPNQ
PPSISISPPR LAPTLPHSAN IFKSPHRGPE ALLPPAPYPS HSLHRLPQCP PVHLSHPVPL
SLTLSLSTGP RQPRPPIPPP HRAPPPHIHL APRGASFRSV SHLNSCRMVM ELEKPSPPQK
PLPADPRSSR LVRSLSVVQG KTTGQGPSVV CGPVLKPGGV RPVRPIPHPS RPSPKHPPTL
PKPCIIANVK YSS
//
