GenomeNet

Database: UniProt
Entry: H0WI57_OTOGA
LinkDB: H0WI57_OTOGA
Original site: H0WI57_OTOGA 
ID   H0WI57_OTOGA            Unreviewed;       787 AA.
AC   H0WI57;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=ADAM metallopeptidase domain 33 {ECO:0000313|Ensembl:ENSOGAP00000001095.2};
GN   Name=ADAM33 {ECO:0000313|Ensembl:ENSOGAP00000001095.2};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000001095.2, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000001095.2}
RP   IDENTIFICATION.
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   EMBL; AAQR03053905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0WI57; -.
DR   STRING; 30611.ENSOGAP00000001095; -.
DR   Ensembl; ENSOGAT00000001224.2; ENSOGAP00000001095.2; ENSOGAG00000001222.2.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000158971; -.
DR   HOGENOM; CLU_012714_7_2_1; -.
DR   InParanoid; H0WI57; -.
DR   OMA; MGAQCAH; -.
DR   TreeFam; TF314733; -.
DR   Proteomes; UP000005225; 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: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:SF38; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 33; 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   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|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:UP000005225};
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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..787
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003543899"
FT   TRANSMEM        700..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..407
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          415..501
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          647..679
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          182..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         347
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        473..493
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        651..661
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        669..678
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   787 AA;  84461 MW;  CB5A62500C082870 CRC64;
     MVRGSRRARG SPVLLLLLLL WPALGVGLLQ GNSSGKSVTL HWVLDGQPRR TVTIEELVSN
     PDSGLVALEA EGQELLLELE KNHRLLAPGY TETHYGPDGQ PVVLVPSHTD HCHYCGNVRG
     FPSSWVVLST CSGMSGLIVL SSNASYYLHP RVPVDSKDFS THMIFLTEQL LTWKGGCGHR
     DPGDKGGMAS LPRALQSRGR REPRRSQRYL ELYLVADHTL FLTQHQDLNR TKHRLLEVAS
     YVDQILRTLD IQVVLSGLEV WTERDLCSIT PDANATLWAF LQWRRGLWAR RPHDSAQLLT
     GCAFGGATVG LAPVEGMCRA ESSGGVSTDH SELAIGAAAT VAHEIGHSLG LSHDPDGCCV
     EAKAEQGGCV MAAATGHPFP RVFSACSRRQ LRAFFRKGGG ACLSDAPEPG VLAPPARCGN
     GFVEAGEECD CAPGQDCQDL CCFTHNCSLR VGAQCAHGDC CAHCLLKPAG ELCRQAAGEC
     DLPEFCTGSS PTCPPDLYLL DGSPCAKGRG YCWDGACPTL EQQCQQLWGP GSRPAPEACF
     QMVNSVGDAH GSCGQDSEGN FLPCAQRDAQ CGKLQCQGGE LSPLAPHTVP VDSTIHLDGS
     EVTCQGVFAL PGAQLDLLNL GLVEPGTQCG PSMVCQDRRC QNTTSQELQH CLAACHNHGV
     CNSNHNCHCA PGWAPPFCDK PGFGGSVDSS PTQSESHDTF LLAMLLSSLL PLLLGVGLAW
     CYYRLPGVHL WRCPWGWRRH PTCTGPALGC SRDHSLGSVH STRLGPTATR EPWPLVPSHL
     ESPLPHP
//
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