ID A0A3Q1MKZ0_BOVIN Unreviewed; 822 AA.
AC A0A3Q1MKZ0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 1a-like {ECO:0008006|Google:ProtNLM};
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:ENSBTAP00000069928.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000069928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069928.1};
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:ENSBTAP00000069928.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069928.1};
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:PRU00276}.
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DR AlphaFoldDB; A0A3Q1MKZ0; -.
DR SMR; A0A3Q1MKZ0; -.
DR Ensembl; ENSBTAT00000069853.1; ENSBTAP00000069928.1; ENSBTAG00000050484.1.
DR VEuPathDB; HostDB:ENSBTAG00000050484; -.
DR GeneTree; ENSGT00940000161891; -.
DR InParanoid; A0A3Q1MKZ0; -.
DR OMA; NEGHAPP; -.
DR Proteomes; UP000009136; Unplaced.
DR Bgee; ENSBTAG00000050484; Expressed in semen and 10 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990913; C:sperm head plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF120; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 1A-RELATED; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068};
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 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 43..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..435
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 444..528
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 704..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 500..520
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 822 AA; 91362 MW; BAA6782730C0EAF5 CRC64;
MSVAASVRDS ASVLPSLWKR QLAMSEAIRM LQTWAPHMKG LRLALVPGLS CARLGILLFL
VLISLPSLYC DLGSPYHSSY EVVIPKSLTV EGREDQVEKL SYVLFMQGQR QLIHLTLKTD
YFVDNFPVFS YHDGILGQEM PLISRDCHYE GYIEGVPGSF VSVNTCSGLR GLLIKEGKSY
GLEPVHSSKR FEHLLYAMAH EARVSCGVTS KDSQVASTSR RPESGKPHSW QVPSDLWSHT
KYVEMFVVVN NQRFQMWGSD VNQTVQRVMD IIALANSFTR GINTEVVLAG MEIWTEGDLT
EVPVDLQVAL RNFNSWRQEK LFHRVKHDVA HMIVGQHPRE DTGQAFLSGA CSSDFAAAVE
SFHHEDVLLF AALMVHELGH NLGIRHDHPA CMCKDRPFCL MRENITKESG FSNCSSDFFH
RFLWEHKGAC LFNKPGHKGR LQRASRCGDG IVEGPEQCDC GSNCERHPCC DTRCQLREHA
ECSDGLCCDK CRLRYQGFMC RAALGECDLP EYCNGSSGEC PRDSYKLDGT MCDRIHYCAG
GRCKNPDNQC MDIYGSPARS APEMCYVSMN TRGDRFGNCG TTSSPRLTYL KCADDNIFCG
KLICTNVREI PQLKPNHTLI QVAHKDDWCW SMDAYGTADV PDDGDAHTGT LCAPHKVCMN
HLCTDYTSLG YNCETTELCN GKGVCNNFRH CHCEDGYAPP DCKDPGEGGS VDSGPPRISI
QLSSGGESET PKRRRNEFQG IGNVVFIVPS LLLVLLITAI LFISLRTGIE SDGLAASPCS
PRDSQESSPA PQFKSIDSSA LSFLHSPTLT STHDYWKNHS LD
//
