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
//