ID A0A2T7PTM1_POMCA Unreviewed; 648 AA.
AC A0A2T7PTM1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=C0Q70_03714 {ECO:0000313|EMBL:PVD36727.1};
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:PVD36727.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD36727.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD36727.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD36727.1};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
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:PVD36727.1}.
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DR EMBL; PZQS01000002; PVD36727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PTM1; -.
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:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
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; PF13582; Reprolysin_3; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 202..377
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 342
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 320..391
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 358..377
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 423..442
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 477..513
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..519
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..503
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 648 AA; 71644 MW; 93959B93B89CB56C CRC64;
MTDVELTDHA RRIARAVNAE GYDIATLHGT SLFSGDKTRL TKRDVEEHAA HPSTESRNFE
LRLTSGERLR MSVQKRSGMS PDVTVVERVS GKEKVSRPQV RDCFFSGGLE GEEGHASLSL
CDGQVMGGIR AGNRDYEVHP LPETSAIRRR SADEPLHAVV TWSDQGNDLM AFDSISPDLS
DEDETEASDI IEETKPDSYK SATIEVGVYM DRFFLARVEE RFGLTTTEQL MELAALKWSG
INAVLSNPKV VGWNITIKVV HLEIWRESPS WYNESNFYLG GRQNMLCAST TDMPFDHIML
ETADTRPNRI KGISWMDRMC NPRWRCSAAR GAGFSNWIEA HETGHSMGLN HDWTFKSCDP
NVPKGFMSMQ ETVFRDCYSQ VLDRSLSSKG CLFKQNVDIS KYNSVNNIVP LYRGQKATLD
DQCRLNKGDG FEYLHIPSAD MCFKGTCVPW LKTVNPNYVR PLVREGGWGP WSPSSPCDNT
CGDAVSVSTR QCNRPTPRIS TFCNGSAIKA KMCPFQQVCP GESSVESELV KQRVKAVCGK
VKVSGASVYN LTGEGNLYST SGDMKKCSVT CNHVDGSSTT RFALQDGTPC WGEDNDRDHD
SNVRGISWRC VQGRCLAFGC NGKSLGEGGG VEKDRCGVCG GDGSSCPK
//
