ID A0A3Q3XMC2_MOLML Unreviewed; 890 AA.
AC A0A3Q3XMC2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000025346.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000025346.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR AlphaFoldDB; A0A3Q3XMC2; -.
DR Ensembl; ENSMMOT00000025772.1; ENSMMOP00000025346.1; ENSMMOG00000019155.1.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013277; Pept_M12B_ADAM-TS8.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF41; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 8; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01861; ADAMTS8.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..890
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018584256"
FT DOMAIN 171..380
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 314
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 318
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 324
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 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 246..298
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 275..280
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 292..375
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 330..359
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 401..426
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 412..434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 421..455
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 449..460
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 486..523
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..528
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..513
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 890 AA; 98681 MW; 7D4744954F435668 CRC64;
MRSGACLIVL LLCVMTAARP APFESEDVVP VRINKRSSGR FWKRSEEQPR FVLSAFGRDM
TLNLIPDTSF IAPSFSVQLA ELQNFINRTE ESEEQLSGCF YSGSVDEDQH SVVSVSLCSG
IFGCFITTES HRVPLLFDQA AAERNDGERF THGDGDARRE RRRRRFVSAP RFIETLVVAD
KSMAHFYGDD IKHYILTIMS MAAQLYKHPS IKNSVNVVLV NMLVVEDEEV GPEVSSNGDV
VLRNFCSWQQ FFNPPSQRDP RHYDTAMLFT REDICGQKSC DTLGVADVGT MCDPKRSCSV
IEDNGLQAAF TAAHELGHVL SMPHDDSKTC ERLFGDLGGH YLMAPLFVSL NKTAAWSPCS
ALYVTEFFDN GHGDCLLDVP ESPIPLPREL PGTKYSLDQQ CQQIFGKEFV HCPSMSEGEV
CSQLWCQEEG TMQCSTRNGS LPWADGTPCS LNGSCLHGAC MPTQEVMQPL VVVDGGWSSW
GPWQQCSRTC GGGVEFSYRE CANPVPQNGG KYCEGQRVQY QSCNTQPCDN EGKSFREEQC
EKYNSFNYLD YNGNMKQWIP KYAGVSPRDR CKLFCRARGS SEFKVFESKV IDGTTCGPDT
TSVCVQGQCV KAGCDQVIGS SKRPDKCGVC GGSGLTCRKI TGSYNKATYG YSDIITIPVG
ATNIDIKQRS LRGIKHDGNY LAVKRVSGGY ILNGNFSVST VEQDIPVLGA VLKYSGSSTT
LERIQSFRQL KEDITIQLLA TAGDANPPKV KYTFFIPRDV TFNKSKEKKQ LSLHVIHPFS
VPDWDLGEWS ECSKSCGSGW SRRNVECKDS AGFLSSLCDT DLKPMDIRPC GDLPCPIWQT
GPWSSCSRTC GQGERRRSVF CIDYTGKTVE PDKCDANKIP EVVSTEYFCV
//
