ID A0A091S7N9_NESNO Unreviewed; 665 AA.
AC A0A091S7N9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9 {ECO:0000313|EMBL:KFQ53645.1};
DE Flags: Fragment;
GN ORFNames=N333_12313 {ECO:0000313|EMBL:KFQ53645.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ53645.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ53645.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ53645.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KK945003; KFQ53645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091S7N9; -.
DR MEROPS; M12.209; -.
DR Proteomes; UP000053840; 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; IPR006149; EB_dom.
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:SF122; ADAM METALLOPEPTIDASE DOMAIN 9; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01683; EB; 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; 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:KFQ53645.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000053840};
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 629..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..343
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 351..437
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 573..607
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 409..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 597..606
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ53645.1"
FT NON_TER 665
FT /evidence="ECO:0000313|EMBL:KFQ53645.1"
SQ SEQUENCE 665 AA; 73293 MW; 629F5550FDBC5FFA CRC64;
FCFQELPDDN LSYSVKTRNG TYLLKLKRNK KLVSEDFMLY TYGENGKVEA TQSKNETHCY
YHGTVEGIAD SVLALSTCDG LRGILFIDGK WYGMEPLNAS STFEHVFYQL EDMQDIPFQC
GVLNSSLHHE MFVKQPVKYT FKRRAVLPQK SYVELFVVVD NNRFLMKKSD PAAVQKETVE
LINYVDGMYG ALNIQIVLVG LEIWTDTNHI SVMEGSAGDV LSRFVSWRQK DLLKRSRNDV
GHLIIGRSSY SGSIGMAFVG TVCSQVQGGS ISTLNHDNVL RHATVVAHEL GHNLGMKHDD
TRCPASYIMH STDNGSRNFS TCSADDFENL ILSGGGNCLR NPPITSNVYK EPVCGNNVVD
SNEECDCGKP EECTNPCCDA ATCKLTPGSQ CAQGLCCKNC KFKVAGAECR SKMDFCDLPE
YCNGSNAYCP EDVYIMNGYP CSNMKAYCYY GVCQSFDSQC ESIYGKGARK APDACFERAN
IKGDRFGNCG MEGGVYKKCP VQHSLCGKLQ CTSVSLQNLP AWSVVNNASG VLCWSSDFDL
GSDVPDPAQV HDGTACGENK ACVDFECVDA SNLGYSCDVK QQCHDNGVCN NNGNCHCNSG
WAPPFCNRSG YGGSVDSGPA HIDTSLRDGL LIFFLLVVPV VIMTVVAVIK RDAIRRKFCR
KRRRQ
//
