ID A0A2D0R0H8_ICTPU Unreviewed; 817 AA.
AC A0A2D0R0H8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 isoform X1 {ECO:0000313|RefSeq:XP_017324146.1};
GN Name=adam9 {ECO:0000313|RefSeq:XP_017324146.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017324146.1};
RN [1] {ECO:0000313|RefSeq:XP_017324146.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017324146.1};
RG RefSeq;
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 RefSeq; XP_017324146.1; XM_017468657.3.
DR RefSeq; XP_017324147.1; XM_017468658.1.
DR AlphaFoldDB; A0A2D0R0H8; -.
DR STRING; 7998.ENSIPUP00000007929; -.
DR GeneID; 108265866; -.
DR KEGG; ipu:108265866; -.
DR CTD; 8754; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000221080; Chromosome 5.
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: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 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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT ACT_SITE 346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 320..400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 364..369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 472..492
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 663..672
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 817 AA; 89958 MW; D763019B4B8375A9 CRC64;
MAVVLSSHLQ IICVVFVLFD STGGSASQTS QFSSYEVSIP KRIGRHRREQ DGSVSDKVSY
VIPAQGKEHV IILEKNEFLL PEDFTVYSYA KDGSLITERP NMKDHCHYRG YVEDVDGSSA
ALSLCSGLRG VIHMQNTSLG IEPLEGSSDN EHLIYHLEDV KTEPFTCGTP HSRHHGNQVS
PGHAQAHNAT FGRPESHLIR KKRAVLHQTH YVELLLVVDN ERFNFTNRNQ TAVREEMVQL
ANYIDSMYVA LNIRVVLVGL EIWSVMNFIS TDGGAGEVLG RFTQWREKEL VPRRRHDSAQ
LILNRGFGIT AGMAFVGTAC SRSHGGGINA FTHKNVASFA SIVAHELGHN LGMNHDDDGR
NCKCDVAHCI MNSGATGSRN FSSCSADDFE KLILTAGGSC LMNVPRPDEA YSAPFCGNKL
VDVGEECDCG SEEECEKDPC CEPKTCKLRA GAQCAYGVCC KHCRFLPGGT VCRSSTDECD
LPEYCNGSSA LCRVDVFKQN GHPCREGVAY CYNGLCQHYD TQCQALFGPK AKAAPEVCFK
DVNSKGDRFG NCGYQNNHMK KCESRNAMCG KLQCENVQNT IVFSIKPSII QTPIGGTTCW
GVDFRLGTDV PDPGMVNEGT KCGENKVCLN YECKSADELK YDCDVQNKCH AHGVCNSNRN
CHCDYGWAPP FCEFAGYGGS TDSGPTWNDK DTSTRDGLLI FFFLVLPLLA LGLYVFFRRN
ELQRRFCRKK RSQGYEADSR PQTNNSRTPA NRHGNPSSIV KDGHQAQLLP AEEVVHTSKT
SASAPAYVSR PPRPAFTRPP PPASQLLPQR PAPPPPV
//
