ID A0A3B1JGL4_ASTMX Unreviewed; 913 AA.
AC A0A3B1JGL4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 8 {ECO:0000313|Ensembl:ENSAMXP00000040846.1};
GN Name=ADAMTS8 {ECO:0000313|Ensembl:ENSAMXP00000040846.1};
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:ENSAMXP00000040846.1, 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:ENSAMXP00000040846.1}
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; A0A3B1JGL4; -.
DR STRING; 7994.ENSAMXP00000040846; -.
DR Ensembl; ENSAMXT00000048762.1; ENSAMXP00000040846.1; ENSAMXG00000033321.1.
DR GeneTree; ENSGT00940000159642; -.
DR InParanoid; A0A3B1JGL4; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000033321; Expressed in bone element and 5 other cell types or tissues.
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: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}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..913
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017347078"
FT DOMAIN 189..398
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 156..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 332
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 336
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 342
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 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 264..316
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 293..298
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 310..393
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 348..377
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 419..444
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 430..452
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 439..473
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 467..478
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 506..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 510..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..533
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 913 AA; 100346 MW; 7F6A3EBCCAAE61E4 CRC64;
MAPQVHSVLA VLLVVLLVKS VRCDLVESEE TVPVRLSPGR LGGVGGRQVF RLSAYGQVFT
LDLKPDSSFV SPALRIQRIS AKQLSEPQAR AGEELKRCFY SGTVNRDPDS VVSLSLCSGI
RGTFISRGDE YFIQPAETGN RGSSSQPHLL RRRVLPSTSK SELHQRPGDE QQARDDRKQR
DKRFVSSPRY IETLVVADYS MTQFYGEEIK HYLLTLMGMA AQLYAHPSLK NAVSVVVVKM
LVVEDEDLGP ELSSNGGVAL RNFCAWQQLF NPSSQRHPEH YDTAILFTRE DICGHQHCDT
LGVADVGTMC DPKRSCSVIE DNGLQAAFTV SHELGHVLSM PHDDSRNCEK FFGHIDGHHM
MAPFFVHLNK TLPWSPCSAL YVTEFFDNGH GDCLLDAPDQ AIPLQAEPPG HKYSLDRQCQ
QAFGEEYARC PNAPDDQACV QLWCREGGKL QCTTRNGSLP WADGTPCGED KTCHGGTCMF
TALDEAGQDE VPVDGGWGSW GPWGPCSRSC GGGVEFSRRE CTDPVPQNGG SYCVGQRVKY
QSCNIQTCPG DHGKSFREEQ CEKYNSDRYL DMNGNIKQWI PKYAGVSPRD RCKLFCRAKH
SNEFKVFEAK VVDGTTCGPD TTSICVQGQC IKAGCDQVIG SNMRLDKCGV CGGDGTSCRK
ISGSLNKATF GYNDVVTIPA GATNIDIKQR SHRGIKHDGN YLAVKAEDGN YILNGNFSVS
TAEQDIPVRG AVLRYSGSST TMERLLSFQE LKQTITIQVL STAGDAAPPR IKYTFFLSRE
VPFSKPGADG NTSPQVITPF GGADWVLGEW SECSKSCGAG WSRRSVECQD RAGSPSYFCD
ADLRPADIRP CGDLPCPVWQ MGPWSACSRT CGQGERRRSV LCMDYTGKAV EPEKCNPEKR
PEAVSGECFY QDC
//
