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Database: UniProt
Entry: A0A2C9KQP3_BIOGL
LinkDB: A0A2C9KQP3_BIOGL
Original site: A0A2C9KQP3_BIOGL 
ID   A0A2C9KQP3_BIOGL        Unreviewed;       743 AA.
AC   A0A2C9KQP3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=106068788 {ECO:0000313|EnsemblMetazoa:BGLB022413-PC};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB022413-PC, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB022413-PC}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB022413-PC};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   RefSeq; XP_013083718.1; XM_013228264.1.
DR   AlphaFoldDB; A0A2C9KQP3; -.
DR   STRING; 6526.A0A2C9KQP3; -.
DR   EnsemblMetazoa; BGLB022413-RC; BGLB022413-PC; BGLB022413.
DR   GeneID; 106068788; -.
DR   KEGG; bgt:106068788; -.
DR   VEuPathDB; VectorBase:BGLB022413; -.
DR   OrthoDB; 5395001at2759; -.
DR   Proteomes; UP000076420; 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:0032502; P:developmental process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd14246; ADAM17_MPD; 1.
DR   Gene3D; 4.10.70.30; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR032029; ADAM17_MPD.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR45702:SF6; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 17; 1.
DR   Pfam; PF16698; ADAM17_MPD; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF13574; Reprolysin_2; 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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   TRANSMEM        14..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        662..682
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          228..465
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          469..558
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   ACT_SITE        396
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   743 AA;  83705 MW;  2404573379241B8F CRC64;
     MTFILDLVFV RDTFYFPIAI DVIVLYAYTL AIVEGAIHDK LTYHEVINIH NSHVRHKRST
     NNDMSEFIKE FHFQAFNRSF TCNLTPRLNF FSPNFILAVY GENGKPVEHS FRRDQIYVGK
     CDGDPDSEIR GTFKEGIFSG TVHYDGELYG VENAKFHIQA SSMNDDSHML VYRANDIIWQ
     EGQKTQFSPS FCGNIHLNIS KDDSHTIVDH ATQAKLSRRK RSTATTLNTC KIIAVADYKF
     FQGVGRNNIY DTALYMANVI DRVDNIYRKT FFNLETSMDG FGFEIAKMVI YRYATNGFNA
     ETDSWDPLNL LQAFSRNTEY KNYCAAHLFT HQSFFGNVLG LAYIAPPREG QVGGICSPLA
     RLNEHMSSLN TAWSSTKNQN GDTVLLQQAN LVTAHELGHN WGAEHDPETS DCSPSTSRSG
     KGKYLMYPYS VSGYDANNLL FSPCSRELMS RVLKLKRDSC FSEKSYDTNQ VCGNGIIDEG
     EECDAGLLGR FNLDSCCNNN CQLIGDATCS PANHECCMNC TKAPSGYMCT QDSDVDCFES
     AFCNGFDLTC PKPSFKKDNS SCLDKGQCRN GKCIPFCAAR NLTACACEEL SNSCQRCCRK
     DSSSPCIPFD GNSPLPNGRP CIGGYCQDNV CKSSKVSTIQ RLFQIFENLS VDKIVQIFRT
     NVVGCVIVFS LILWIPATTA IWCQDRKARK QTERWEDTEI RTDRNLLHDE DGRLVAKPIK
     KSKADMETLR RRNVYSLFST SEV
//
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