ID A0A093DX46_9AVES Unreviewed; 640 AA.
AC A0A093DX46;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 19 {ECO:0000313|EMBL:KFV06746.1};
DE Flags: Fragment;
GN ORFNames=N339_00905 {ECO:0000313|EMBL:KFV06746.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV06746.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV06746.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV06746.1};
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; KL232620; KFV06746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093DX46; -.
DR MEROPS; M12.214; -.
DR Proteomes; UP000053149; 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:SF19; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 19; 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; 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:KFV06746.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000053149};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 155..353
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 361..447
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 596..628
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 419..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 600..610
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 618..627
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV06746.1"
FT NON_TER 640
FT /evidence="ECO:0000313|EMBL:KFV06746.1"
SQ SEQUENCE 640 AA; 70512 MW; 218D975D279DDE6F CRC64;
LFYPQHPFRA EVRIKAEGQE LILELEKNGN LFAPSYTETH YSWTGEPRTT SLTHTDHCFY
HGVVRGWERS SVTLSTCRGL RGLIVLSSNS SYILEPVPES PNQHLIYRLH NLRLQRGACG
YQGTGDVAED WLRDFTTGMK PPHQRVKRET LQATKYVELL LVADYAEFQK NHFNIEATRL
KLVEAANYVD KFYRSLNIRI ALVGLEIWSN WNKCDVTENP YSTLKSFLAW SSKERVHRKH
DNAQLITGVP FQGTTVGLAP VMAMCSDFQS GGVNMDHSDN AIGVAATIAH EMGHNFGMNH
DSVGCCTTPA EEGGCIMASA TGHPFPKVFN QCNRKELEKY LQSGGGMCLS NMPDTKKMYG
GKKCGNGYLE EGEECDCGEV EECKNPCCNA STCSLKLGAE CAHGSCCHQC KLMSPGTLCR
EQSGLCDLPE YCTGESPFCP ANSYQIDGAS CDGGKAYCYS GMCLTYTDQC LQLWGPGARP
APDACFEKVN AAGDIYGNCG KDIYGNYKKC EMRDAKCGKI QCQSSASKPL QSNAVAIDTT
IHMQRTQLRC RGTHVYRSES EEKEMLDPGL VLTGTKCGSH HVCFEGRCQN TSVIFESESC
SKKCHGHGVC NNNKNCHCNQ GWAPPFCNKQ GTGGSLDSGP
//
