ID A0A3Q1J666_ANATE Unreviewed; 877 AA.
AC A0A3Q1J666;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=ADAM metallopeptidase domain 15 {ECO:0000313|Ensembl:ENSATEP00000026774.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000026774.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000026774.2}
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; A0A3Q1J666; -.
DR STRING; 64144.ENSATEP00000026774; -.
DR Ensembl; ENSATET00000027199.2; ENSATEP00000026774.2; ENSATEG00000018524.2.
DR GeneTree; ENSGT00940000159822; -.
DR Proteomes; UP000265040; 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; 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:SF130; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 15; 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; PR01217; PRICHEXTENSN.
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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_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:UP000265040};
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 TRANSMEM 682..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..386
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 394..481
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 626..658
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 107..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 453..473
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 630..640
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 648..657
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 877 AA; 94638 MW; 99B4268872731C67 CRC64;
MDGQRQSLAE ALQDGHPDRL QCGLEVGGRL FLLDLEKNHD LLPKPPNVFY YLPNGTGVSV
RADPVTHCFY HGSVRGFPQS RVAVSTCSGL RGVVAINSTL SFELQPQEKT HLHHEEGENA
EGGGGSGGSG GGEAVDEGLH LVFSTSPLEG DAAGGCGVSH TAVPPIHSST HTHRRKRDIL
SETKYIELVL VADHQEFLNY QKNNKTIIYR MLDVANQVDW FYRPLNVRVA LTGLEIWSDR
DKIHVEKSPT DTLNNFLEWR TRELLPRLRH DNAQLVMGGS FDGTTVGMAS QSSMCSRDRS
GGVNVDHLVS VLGVASTVAH ELGHNLGMSH DTAERHCSCQ SEPRLGGCIM EPSTGFMPGQ
QFSSCSAADL SVSLLHGGGM CLFNVPQPDR LLGGPRCGNL YVEKGEECDC GLLEECEDPC
CNASTCQLVP GAQCSSDGIC CQDCKLRAAG SVCRLPLGEC DLPEFCTGSS PYCPPNVFLQ
NGEPCKDGAS YCYEGVCAST HAQCQILWGP NATSAPAVCF SSVNKKGNKF GNCGQLSNGS
YIPCENVDVH CGRIQCQGGR DRPLLGTNGE IITTTVRFNH SDLVCRGTFF HLGDDVSDPA
TVAQGVACGP GKACLNQKCQ DVSVFGVDDC RRKCNGHGVC NSNKNCHCDV GWAPPDCRYS
GHGGSVDSGP ARAARGSDPV RVALLVIFLF ILPVLLLFLA LRFPRFRRIL FCLGPNSPFH
KARQHNRTPV MERVDGRNGE QVRPLRYHLK PPMDIPLTLP HKEVHDRPAP PTKPLPPDPA
LKPLPQPVKQ RPAPPTKPLP PDPYSPTNQV AVPLKPVGPS KPRPPSPPSH LPPHPGYTSN
TKPPQLRAVA PAGGPHRRPP LPPVRPTVPQ KIDSSPV
//
