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Database: UniProt
Entry: A0A3Q4BUK2_MOLML
LinkDB: A0A3Q4BUK2_MOLML
Original site: A0A3Q4BUK2_MOLML 
ID   A0A3Q4BUK2_MOLML        Unreviewed;       809 AA.
AC   A0A3Q4BUK2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:ENSMMOP00000025392.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000025392.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3Q4BUK2; -.
DR   Ensembl; ENSMMOT00000025818.1; ENSMMOP00000025392.1; 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; 1.
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; PF00090; TSP_1; 1.
DR   PRINTS; PR01861; ADAMTS8.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR01705; TSP1REPEAT.
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   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..809
FT                   /note="Peptidase M12B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018584624"
FT   DOMAIN          188..397
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         191
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         191
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         331
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         335
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         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         392
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         395
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         395
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   DISULFID        263..315
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        292..297
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        309..392
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        347..376
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        418..443
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        429..451
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        438..472
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        466..477
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        503..540
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        518..530
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   809 AA;  89989 MW;  E5A704EAFEDE38C1 CRC64;
     MRSGACLIVL LLCVMTAARP APFESEDVVP VRINKRSSGR FWKRSEEQPR FVLSAFGRDM
     TLNLIPDTSF IAPSFSVQRI RARDGGALRG SPGAHPVAEL QNFINRTEES EEQLSGCFYS
     GSVDEDQHSV VSVSLCSGIF GCFITTEQLH VIRRRTFARS HRVPLLFTHG DGDARRERRR
     RRFVSAPRFI ETLVVADKSM AHFYGDDIKH YILTIMSMAA QLYKHPSIKN SVNVVLVNML
     VVEDEEVGPE VSSNGDVVLR NFCSWQQFFN PPSQRDPRHY DTAMLFTRED ICGQKSCDTL
     GVADVGTMCD PKRSCSVIED NGLQAAFTAA HELGHVLSMP HDDSKTCERL FGDLGGHYLM
     APLFVSLNKT AAWSPCSALY VTEFFDNGHG DCLLDVPESP IPLPRELPGT KYSLDQQCQQ
     IFGKEFVHCP SMSEGEVCSQ LWCQEEGTMQ CSTRNGSLPW ADGTPCSLNG SCLHGACMPT
     QEVMQPLVVV DGGWSSWGPW QQCSRTCGGG VEFSYRECAN PVPQNGGKYC EGQRVQYQSC
     NTQPWKSFRE EQCEKYNSFN YLDYNGNMKQ WIPKYAGVSP RDRCKLFCRA RGSSEFKVFE
     SKVIDGTTCG PDTTSVCVQG QCVKAGCDQV IGSSKRPDKC GVCGGSGLTC RKITGSYNKA
     TYGYSDIITI PVGATNIDIK QRSLRGIKHD GNYLAVKRVS GGYILNGNFS VSTVEQDIPV
     LGAVLKYSGS STTLERIQSF RQLKEDITIQ LLATAGDANP PKVKYTFFIP RDVTFNKSKE
     KKQLSLHVIH PILFCHLLLT LDNHYWELI
//
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