ID A0A3B1J6K5_ASTMX Unreviewed; 889 AA.
AC A0A3B1J6K5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 15 {ECO:0000313|Ensembl:ENSAMXP00000036964.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000036964.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000036964.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B1J6K5; -.
DR Ensembl; ENSAMXT00000030614.1; ENSAMXP00000036964.1; ENSAMXG00000029685.1.
DR GeneTree; ENSGT00940000155801; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000029685; Expressed in bone element and 12 other cell types or tissues.
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; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR006586; ADAM_Cys-rich.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF39; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 15; 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; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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:UP000018467};
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};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..889
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017279381"
FT DOMAIN 203..352
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 172..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 347
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 278..330
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 307..312
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 324..351
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..400
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 388..410
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 395..429
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 423..434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 458..495
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 462..500
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 473..485
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 889 AA; 97321 MW; B76118F20E1EC1A5 CRC64;
MRVPVRTAIH LLVQCVFLVH CAPETQLCVP VRLDTEHTDF SLFGTASAHP RFRVSAFDQD
LVLELHPDSS FIAPALVETR AANVNANAQL SRCFYAGSVN ADELSYAAVS LCGGMRGAFG
YGGWEYFIEP TQGAEGAHLI RRRRADGERR CAVDGDAGGS SAAVARALGK LQKRAQEENQ
EDEDQENATA QKSRAKRFAS VPRYVETLVV ADESMADFHG EDLKHYVLTL MSVAARLYKH
PSILNPINIA VVKFLVIGDE DKGPKVTGNA AMTLRNFCTW QKKMNKNSDK HPDYWDTAIL
FTKQDLCGAS TCDTLGMADV GTMCDPKRSC SVIEDDGLPS AFTTAHELGE CLLDQPQKPL
ALPDGLPGVF YGLEKQCELA FGTGSKPCPL MQAPCQRLWC TGKTRGQPVC QTRHFPWADG
TSCGEGMLCM RGVCLEQGEV TKAKVDGRWG KWGPFGSCSR TCGGGVQLAK RECNNPVPEN
GGKYCQGMRV KHRSCNLIPC PDTGKSYREE QCEAFNGFSL NTNRLALTVV WVPKYSGVSP
KDQCKLICRA NGTGYFYVLA PKVVDGTPCS PDSSAVCVQG KCTKAGCDGK LGSSKKFDRC
GVCGGDNKNC KKISGLFTKP THGYNFVVLL PVGAANVDIR QRGYKGIVSD DNYLAVKNSQ
SKYLLNGNYV VSAMERDILV RGSLLRYSGT GGQSETLQSV KPLGEALTVE VLSVGQMTPP
RIRYSFYLKR DNKEEKSLKK EGKERAENSV LPEDGRIIKK EDNLKEKVPK SVYPKEPPSY
GKWAAGGWDE CSVTCGNGLQ RRLVQCLRND DKPGTDCDPA KRPNAMRACG DPCPMWDVGE
WSPCSKNCGK GFKRRLLRCT SQTGMLLPRE HCVGLKKPQE LDFCSLNLC
//
