ID A0A2T7PTH1_POMCA Unreviewed; 1129 AA.
AC A0A2T7PTH1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=C0Q70_03708 {ECO:0000313|EMBL:PVD36722.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD36722.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD36722.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD36722.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD36722.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD36722.1}.
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DR EMBL; PZQS01000002; PVD36722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PTH1; -.
DR EnsemblMetazoa; XM_025227788.1; XP_025083573.1; LOC112557762.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg2.
DR GO; GO:0005576; C:extracellular region; 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 Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF13688; Reprolysin_5; 1.
DR Pfam; PF00090; TSP_1; 2.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 2.
DR PROSITE; PS50092; TSP1; 2.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 15..203
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 630..804
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 1073..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT ACT_SITE 769
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 768
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 772
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 778
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 1129 AA; 124707 MW; 2A81D637DD534FCB CRC64;
MWTIEMMRSV EDKSLMIEVG VYLDRFFLNR VKNNLGLSTL QQLTDLVALK WSGIYALLSN
PLVVGWNITI KVVHLELWRE SPSWYNESNI HIGGRQNMIC KSTTDKPFDH IFLETANTTD
GRTVGISWLN NICNPRWRCS AGKGANLNSW IEAHETGHSL GLNHDKTFTS CNPNVTSGFM
TMKETVFQRL LRPGPQQDFK VCSKLTCIRK SPFIELKQMT TFLGTPCGKE QMCFNGACVP
WVKTVNPNYV RHLVKEGGWG PWSPFSSCNN TCGDAVSVST RQCNRPTPSV APFCKGDVIK
AHMCPSEKVC SGESSVESEL IKQRVSAVCS KVKASAASPH NLTGAGKVYG TSGEVDKCTV
TCNLVTGTSP ERFLLQDGTP CWGHDNNRDH DSNAFGCNGK SLGDGGGVEK DRCGLDDLLT
DGELKGHVTR IARAVDADDY NIATLYGTSL ISGAEKVLTK RDVEDHAAHP STESRNFELR
LTSGEQLRMS VQKRSAMSPD VTVVERVFGK EKVSRPQVRD CFFSGGLEGE EGHASLSLCD
GQVVSGRYTD RSEPYRPRER DFELHALPQA AATKRRSATE PLRVLVTWSD SKQKMDVTND
VIVPDIPDKS DTEGDNSKEM RMRSVQDKIV VMEIGVYLDR LFLEKINESL GLSTTQQLTD
LVTLKWSGVY ALLSNPLVVG WNITIKVVHL EIWRESPSWY NETVNNLGGR MDMICRSTTD
KPFDHIFLET ANTPGSTVGL SWLGTMCNPR WRCSIGKGVN LNSWIEAHET GHSMGLNHDN
TFTTCDPNVT SGFMSMKETI FRDCYGPVLD SSLRLTCIQK SPVGKIALMS TFTGTPCGKE
QMCLNGACVP WVKTVNPDYV RPLVREGDWG PWSPSSPCDN TCGDGVSVST RQCNRPTPNV
APFCNGDVLK AQMCPSRQVC SGESSVESEL VQQRVKAVCS RVKASGASVY NLTGEGKVHG
TSGEVDKCTV TCNLVTGTSS ERFLLQDGTP CWGEDNDRDH DSNVRGISWR CVQGRCLAFG
CNGKSLGEGG GVEKDRRVPT VLTLTRYNFI KRDVEDHRES VVKVQKLRAS SHFRRETTHV
TSEAASSMPK PESGGALGER NDNQSPTDQR LLLQWPSEGQ VWFRFTVAV
//
