ID A0A3P8YE24_ESOLU Unreviewed; 612 AA.
AC A0A3P8YE24;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|Ensembl:ENSELUP00000014827.2};
GN Name=ADAM12 {ECO:0000313|Ensembl:ENSELUP00000014827.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000014827.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000014827.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000014827.2}
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; A0A3P8YE24; -.
DR STRING; 8010.ENSELUP00000014827; -.
DR Ensembl; ENSELUT00000023752.2; ENSELUP00000014827.2; ENSELUG00000014859.2.
DR GeneTree; ENSGT00940000155495; -.
DR Proteomes; UP000265140; LG06.
DR Bgee; ENSELUG00000014859; Expressed in heart and 12 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000265140};
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 569..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..279
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 287..373
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 517..549
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 345..365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 521..531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 539..548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 612 AA; 65872 MW; 5230FF6FF4CE54E8 CRC64;
TEKEKPSWTL LYYLLSKMGF ISLENESFIL EPPADPSAGS LHRIYRAEQI KLTSGTCGHD
FNISWPPGDN HSQSDSPFRV FNTRVSSVPF QKQGKDVGKV KQRLAEIANY VDKFYRALNI
RVALVGLEVW SDQDKCPVTQ DPFTTLHEFL DWRKLKLLPT RPHDNAQLVS GVYFQGTTIG
MAPIMSMCTA EQSGGIVMDH SDNPLGAAVT LAHELGHNFG MNHDTPERGC GCRVTSDRGG
CIMTPSTGYP FPTVFSSCSK KDLVASLEKG VGMCLFNMPE VKVLYGGQKC GNGYVEEGEE
CDCGELEECL NPCCNATTCS LKAEAVCAHG QCCHECQLKP AGTPCRDSSN SCDLPEFCTG
ASPHCPGNVY LHDGHACHNV DGHCYNGICQ THEQQCITLW GQGAKPAPGI CFERVNSAGD
PYGNCGKDSK GSFAKCEAPD AKCGKIQCQG GANRPVIGTN AVSIETNIPL QEGGRILCRG
THVYLGDDMP DPGLVMAGTK CGNMCLNRQC QNVSVFGVNE CSGKCSGRGV CNNNKNCHCE
PHWAPPFCDK AGFGGSVDSG PMRLADHGGV AVGVLVAVLP FLGAGLIVCV KRKTLGGLLF
TNRKNAMEKL RC
//
