ID A0A3Q1NKZ8_BOVIN Unreviewed; 822 AA.
AC A0A3Q1NKZ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=ADAM metallopeptidase domain 8 {ECO:0000313|Ensembl:ENSBTAP00000073056.1};
GN Name=ADAM8 {ECO:0000313|Ensembl:ENSBTAP00000073056.1,
GN ECO:0000313|VGNC:VGNC:25612};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000073056.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000073056.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000073056.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000073056.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000073056.1};
RG Ensembl;
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 AlphaFoldDB; A0A3Q1NKZ8; -.
DR PaxDb; 9913-ENSBTAP00000032645; -.
DR Ensembl; ENSBTAT00000070157.1; ENSBTAP00000073056.1; ENSBTAG00000023832.5.
DR VEuPathDB; HostDB:ENSBTAG00000023832; -.
DR VGNC; VGNC:25612; ADAM8.
DR GeneTree; ENSGT00940000158585; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000023832; Expressed in neutrophil and 101 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1NKZ8; baseline and differential.
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: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:SF20; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 8; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..822
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018581359"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..397
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 405..491
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 614..646
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 701..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..798
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 463..483
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 618..628
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 636..645
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 822 AA; 88048 MW; 149C250CB34FF849 CRC64;
MRGLGLLLFA ALGLQEVAPR AALPHVEQYE VVRPRRLPAP RARRALPSHL GLYPESVSYV
LGARGHTFTL HLRKNRDLVG SGYVETYTAA NGSQVTEQLQ RQDHCFYQGH VEGHPHSAAS
LSTCAGLRGF FQAGPAVRLI EPLAEAGEEG PHALYLAQHL QQEAGTCGVN DSSLESILGP
RVSAAFRPRW SEPRETRYVE LFVVTDSKEF QRFGSREAVR QRVLEVVNHV DKLYQELNFR
VVLVGLEMWN GGDKIQISSQ PDATLDNFLA WRTRELVGRQ AHDNVQLITG VDFTGTTVGL
AKVSTMCSSS SGAVNQDHSQ NPIGVASTMA HEMGHNLGMD HDENVAGCYC PVPREGGGCV
MAASIGSQYP RKFSQCSQAD LETFVEKPRT ACLLDAPDLD RLVGGPVCGN GFLERGEQCD
CGRPEDCQNR CCNASTCLLA EGAECAHGTC CHECRVKPAG ELCRPVKDQC DLGEHCDGQQ
PTCPEDAFRE NGTPCPGGYC YNGACPTLAR RCQDLWGPGS RVAVETCFLY SISKGCGAGV
PLPFGRVNKC GTLFCEGGQK TPERGYCTLT ISSGVCRVIV QDGSTEYEPV PKGTKCGEQQ
VCWDGFCQGL HVYRSRNCSA QCNSHGECNH KGQCHCRPGW APPHCAEPLA DARAAPGSLR
THVLVGVGAL VVLALILAGV LIYRKARSPV RRRNVAPKTA MGLSNPLFHE GLSKPAKGGA
QAPPGGSPEL ALYSQPHKPT ASSVTPKRPP PAPPGSLQPP AAKASPPSPL PVYPPQAPGQ
VIKPTCAPPM PPIKPGARGA QPGPTQGAAD PKVALKPPVQ RR
//
