ID A0A3B3WWM7_9TELE Unreviewed; 1121 AA.
AC A0A3B3WWM7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=ADAM metallopeptidase with thrombospondin type 1 motif, 6 {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000007054.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000007054.1}
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 RefSeq; XP_014857603.1; XM_015002117.1.
DR RefSeq; XP_014857604.1; XM_015002118.1.
DR AlphaFoldDB; A0A3B3WWM7; -.
DR STRING; 48701.ENSPMEP00000007054; -.
DR Ensembl; ENSPMET00000004768.1; ENSPMEP00000007054.1; ENSPMEG00000008723.1.
DR GeneID; 106926923; -.
DR KEGG; pmei:106926923; -.
DR CTD; 11174; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000261480; Unplaced.
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: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; 4.
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; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF27; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 6; 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; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..1121
FT /note="ADAM metallopeptidase with thrombospondin type 1
FT motif, 6"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017274499"
FT DOMAIN 254..472
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1083..1121
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 223..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 407
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 411
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 417
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 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 330..391
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 366..373
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 385..467
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 424..451
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 494..516
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 505..523
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 511..546
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 536..551
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 574..611
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 578..616
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 589..601
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1121 AA; 124760 MW; 972770E168883CF6 CRC64;
MEILWKTLTW TLSLVVMAAS EFQRLSHSSQ EEFLSYLQHY QLTVPVRVDE NGNFLSYTVK
HQRPGRRRRA LADPAADPPG SRIYYRLSAY GKHFHLNLTL NNNLVSKHFT VEYWGKEGPE
WRHDVLDRCH YVGSLRSQHS TTRVALSNCK GLHGVITTEE DQYLIEPLKN ASSAASSEWN
LDGAQQHVIY KTSAIPSPQE QSQEFSCGIS DVTKSNAPCQ FSTSSPAHLS PVPQNASQQP
AGAHRRRRSV SSERFVETLV VADKMMVGYH GRKDIEHYIL SVMNIVAKLY RDFSLGNVVN
IIVTRLIVLT EDQPNLEINH HADKSLDSFC KWQRSILSHH SSGNSIPENG MAHHDNAVLI
TRYDICTYKN KPCGTLGLAS VAGMCEPERS CSINEDIGLG SAFTIAHEIG HNFGMNHDGI
GNSCGTKGHE TAKLMAAHIT ANTNPFSWSA CSKDYITSFL DSGRGTCLDN EPPKRDFLYP
TVAPGQVYDA DEQCRFQYGA SSRQCKYGEV CRELWCLSKS NRCVTNSIPA AEGTLCQTGS
IEKGWCYQGE CVAFGSQPES VDGGWGPWSL WGECSRTCGG GVSSSMRHCD SPAPSGGGKY
CLGERKRYRS CNIDACPAGS QDFREKQCGD FDNMPFRGKY YNWKPYTGGG VKPCALNCLA
EGYNFYTERS PAVVDGTRCQ ADSLDICING ECKHVGCDNI LDSVAREDRC RVCGGDGSTC
EATEGLFNDS LPRGGYMEVV QIPKGSVHIE IREVAVSKNY IALKSEEDDY YINGAWTIDW
PRKFDIAGTA FHYRRPTDEP ESLEALGPTT ENLSVMVLLQ EENLGIHYRF NIPIQRTGSG
DNEVGFSWHH PPWSECSATC AGGSQKQEVV CKRLDDNSVV QNSYCEPDSK PPENLRDCNP
EPCPPEWFIG EWSECGKTCD GGTRTRTVLC IRRIGPTEEE TLEDTFCLTH RPIERESCNN
QSCPPKWVTL EWSECTPKCG PGFKHRIALC KSSDLTKTFP PTTCLSHNKP PVRMRCSSGR
CPPPRWIPGD WGQCSAQCGL GQQMRTVTCL SYTGQMSNEC PDSLRPATMQ QCESKCDAIP
NSNSDECKDV NKVAYCPLVL KFKFCSRGYF RQMCCKTCQG H
//
