ID A0A3B4XYA8_SERLL Unreviewed; 891 AA.
AC A0A3B4XYA8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12-like {ECO:0000313|Ensembl:ENSSLDP00000021902.1};
GN Name=ADAM12 {ECO:0000313|Ensembl:ENSSLDP00000021902.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000021902.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000021902.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B4XYA8; -.
DR Ensembl; ENSSLDT00000022618.1; ENSSLDP00000021902.1; ENSSLDG00000017074.1.
DR GeneTree; ENSGT00940000155495; -.
DR Proteomes; UP000261360; 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; 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; 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 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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..891
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017456473"
FT TRANSMEM 643..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..335
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 343..429
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 575..607
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 685..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 401..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 579..589
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 597..606
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 891 AA; 97009 MW; AD7EC38DDD3196F3 CRC64;
MMCLFPLFCS LLRGLFASHY TETHYQEDGR AVTGNNCYYH GEVQAHPNSD VTLSVCSGLR
GFIALENKTF IIEPVSGQDT GSHLIYRVEE LTLTPGACGH GFNMSSVAPE NHIKSPFQSF
HTRHKRHAQK TTKYVELIIV ADNREFQKQG KDIDKVKQRL AEIANYVDKF YRALNIRVAL
VGLEVWSDSD KCPVTQDPFT TLHEFLDWRK VKLLPQKPHD NAQLISGVYF QGTTIGMAPI
MSMCTVEQSG GIVMDHSENP LGAAVTLAHE LGHNFGMNHD TPERGCGCRM TVDRGGCIMT
PSTGYPFPTV FSTCSKKDLA ASLEKGVGMC LYNMPEVKVL YGGQKCGNGY VEEGEECDCG
EAEECMNPCC NATTCTLKGD AVCAHGQCCE DCRLKPAGTL CRETSNSCDL PEFCTGANPH
CPANVYLHDG HACHNVEGYC YNGICQTHEQ QCITLWGPGA KPAPGICFER VNSAGDPYGN
CGKDSKGSFA KCDARDAKCG KIQCQGGANR PVIGTNAVSI ETNIPLQEGG RILCRGTHVY
LGDDMPDPGL VLAGTKCGDG MVCMNRQCQN VSVFGVHECS GKCNGRGVCN NKKNCHCEAH
WAPPFCEKGG FGGSIDSGPM RLADVRVCVL MCVLSYVASA DSVVITVAIL VTLVSLLVAT
VIIFVKRKTL LRLLFTNKKS TLEKLRSVQA SRPTSPIRTQ SMYRPTPQRK PPPKPSGASI
YKPSLLSAEP LLPPHNFHSH SLRRLPLYQP LHISQPMPVS LSVGQPTLPP LPAHHRVLPA
HTSLSPPRVP PFLSLPRQQS SYRPIFLQDF EKPSPPQKPL PADPLGRSSR LGHSATAAGV
HIPGAGPLPI PIPTVPRPPP TIPLPSRSVQ RDRNHMSQTG NMQHGFKCLL K
//
