ID A0A0A0A2L3_CHAVO Unreviewed; 815 AA.
AC A0A0A0A2L3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 44.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KGL88291.1};
DE Flags: Fragment;
GN ORFNames=N301_14140 {ECO:0000313|EMBL:KGL88291.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL88291.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL88291.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL88291.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KL870407; KGL88291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0A2L3; -.
DR STRING; 50402.A0A0A0A2L3; -.
DR MEROPS; M12.209; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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: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.
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 Integrin {ECO:0000313|EMBL:KGL88291.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
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 665..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..372
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 380..467
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 606..640
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 701..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 331..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 439..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 630..639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL88291.1"
FT NON_TER 815
FT /evidence="ECO:0000313|EMBL:KGL88291.1"
SQ SEQUENCE 815 AA; 90778 MW; 275843B7319D81F8 CRC64;
QQVSQLSSYE VVIPQRLGRE RREASNVSSV QDKVSYAIEI EGKEYTIHLE KNKELLPKDF
TVYTYNKEGK LQSEYPDIQD HCHYQGYVEG TLDSVVAVST CSGLRGLVTI ENITYGIEPM
DSSSGSKHIL YRLDNVKREP AMCGVTAEDH EREHAEENHH PSMTQLLRSK RAVLHQTRYV
ELFIVVDKEK FEDFGKSETE VREHMVQLAN FLDSMYIMLN IRIVLVGLEI WKYENIISTD
GGAGDVLANF VQWREKNLVL RRRHDSAQFV LKKGFGGTAG MAYVGTVCSK SHAGGINVFG
RISIQMFASI MAHELGHNLG MNHDDERVCH CGASSCIMSS GASGSRNFSS CSAEDFEKLT
LNKGGSCLLN VPRPDETYSV PYCGNRLVDA GEECDCGSPK ECESDPCCEP GTCRLRSGAE
CAYGDCCKNC RLLPGGTECR ASNNECDLPE YCNGTSQFCQ PDFTVQNGHP CHNEEAYCYN
GVCQYYDAQC QDIFGSKAKA APKICFTEVN SKGDRFGNCG FHGHDYKKCS SWNAMCGKLQ
CENVKTMPVF GIKPAIIQTP IGDTTCWGVD FQLGSDVPDP GMVNEGTKCD TGKICRHFQC
VSASVLNYDC DVERQCHGHG VCNNNRNCHC EAGWAPPYCD TKGYGGSLDS GPPYNDKDTS
LRNGLLVFFF LVLPLLIAAA LAFAKRDRLK RCYRRLMSRC HSSLQSPPPR TEAEPRDYHH
RGFSHGMPYA PRGVPMDMER NTFPVPSYPV NQHPQQAYHQ SYYPSPQYQA AQPQKMPTRP
PPPQQKCAPQ GPPPSQQKCL PQGQYFPSRP APLPP
//
