ID A0A452SCQ7_URSAM Unreviewed; 572 AA.
AC A0A452SCQ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ADAM metallopeptidase domain 9 {ECO:0000313|Ensembl:ENSUAMP00000030118.1};
GN Name=ADAM9 {ECO:0000313|Ensembl:ENSUAMP00000030118.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000030118.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000030118.1}
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:PRU00276}.
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DR AlphaFoldDB; A0A452SCQ7; -.
DR STRING; 9643.ENSUAMP00000030118; -.
DR Ensembl; ENSUAMT00000033602.1; ENSUAMP00000030118.1; ENSUAMG00000022936.1.
DR GeneTree; ENSGT00940000156239; -.
DR OMA; DFTVFTY; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IEA:Ensembl.
DR GO; GO:0042117; P:monocyte activation; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:0034241; P:positive regulation of macrophage fusion; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; 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:SF136; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 9; 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 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..572
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019379776"
FT DOMAIN 212..406
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 414..501
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 365..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 473..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 572 AA; 63991 MW; 5DC139DA7948C812 CRC64;
MGSGAGSPFG VLRLQWLLLF GLVGPVLGGA RPGFQQTSHL SSYEIITPWR LTRERREAPR
LHSKQVSYII QAEGKEHIIH LERNNDLLPR DFVVYTYDKE GALISDHPDL QNHCHYRGYV
EGVYNSSIAL SDCFGLRGLL HIENVSYGIE PLQNSSHFEH IFYRMDDVHK EPLKCGVFNK
DIEKETINYE EEEPPSITQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI
RLANYLDSMY IMLNIRIVLV GLEIWTNGNL INIIGGAGDV LGNFVQWREK FLITRRRHDS
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG
RDCFCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN CLLNIPKPDE AYSAPFCGNK
LVDPGEECDC GTPKECESDP CCEGSTCKLK SSAECAYGDC CKDCWFLPGG TLCRGKTNEC
DVPEYCNGSS QFCQPDVFIQ NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS RISSSCNVVV
LVKNHGECAL RHGSTFRHLD FDYTLILAVF LQ
//
