ID A0A3B1IK77_ASTMX Unreviewed; 1330 AA.
AC A0A3B1IK77;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 2 {ECO:0000313|Ensembl:ENSAMXP00000030116.1};
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:ENSAMXP00000030116.1, 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:ENSAMXP00000030116.1}
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 Ensembl; ENSAMXT00000036076.1; ENSAMXP00000030116.1; ENSAMXG00000007476.2.
DR GeneTree; ENSGT00940000156647; -.
DR InParanoid; A0A3B1IK77; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000007476; 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; -; 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:SF141; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 2; 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; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000018467};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017307086"
FT DOMAIN 254..458
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1051..1089
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 397
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 349
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="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 400
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 406
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 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 331..380
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 374..453
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 413..439
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 480..515
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 491..524
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 510..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 537..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 571..608
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 575..613
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 586..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1330 AA; 149627 MW; C8910C348B8EA728 CRC64;
MAVQPGYAFC SLLLLVQLAR ALYIAHSADS LQHVLKEYGL VKPVSVDVNG HFLTHAVSAS
RLNEQLPHQR RRRNAQYNGE QEHGSTRETL FYNVTVFGQE FHLHLRPNSR LVAPGATVEW
HEDDNRTHSE PLLPSDCLYV GHVTNVPDTS VAISNCDGLA GMIRAGQEEF FIEPLEKGGG
GDMTGEEEGG AGRHHILYRS SAIKKPTASH VDDFAPRASA LGGLASVRDF ARGFEAKVNS
SRRSKRQSYH EEIFNIEVLL GVDCSVVQFH GREHIQKYLL TLMNIVNEIY QDGSLGAHIN
VVLVRIMMLC SAKSMGLIEL GNPSQSLENV CRWAFLQQKE DENDAEYHDH AIFLTRQEFG
PTGMQGYAPV TGMCHPVRSC TLNHEDGFSS AFVVAHETGH VLGMEHDGQG NECGDEVPMG
SIMAPLVQAA FHRFHWSRCS QQELRRYLNT YDCLRDDPFD HEWPSLPQLP GLHYSMNEQC
RFDFGMGYMM CTALQKASRS AKQYSTYDPC KQLWCSHPEN PFFCKTKKGP PIDGTKCATG
KNCFKGHCIK LTSDILRQDG HWGQWTKFGS CSRTCGAGVR FRTRQCDNPI PANGGRTCYG
NNYEFQLCNT EECAKALADF REEQCKMWDP HFEHQGVKHQ WLPYEHPEHE ERCQLHCQSK
ETGDVVSMKR MVHDGTRCSY KDHYSVCVRG ECEKVGCDNV IASELEEDKC GVCGGDNSTC
KIVKGNFTRS TKKPGFLKIL EIPRGARHVM IREFKGTPHI LAVKNQATDH LFLNDEGEFP
ESRAVIEKGV LWEYSNDDDM ETVQTTGPLR YGVLIMVQSH STSKVTLSYK YILPKDPPSS
MENSLPVDET AYFEWALKKW SHCSKPCGGG KQYTRFGCRR KSDGKMVHRT LCSNISKPRA
ISRACNQKQC SEPVWVTGDW EECSKSCGKT GTQTRPVRCV RPQADGTQKT INSKYCSDDR
PEGRRTCNRN LCPAQWRTGP WSQCSVTCGN GTQERQVMCS TPDNTIGACL EPKPEIIRKC
QLMPCSGDRG NFLIQWLSRA DPEFPAPKIS SRSRCKGDKS VFCRMEVLNQ YCANSGYRQM
CCKSCSQSNF TSSLNTTSKP WSFTTVAPGT AVGNVRQRTP PSPPTPWKYT TILDPLTLRR
GTTFPSTISA FLEETDGPST TSDEEEYVSE PWTVVIPKEL SESTSWFEDL LSTSVQSTTE
SNDDVTEELA TTPTVTTAMA TTPALTTPRF TMPTVTTTRP THTTPVQTRV LLTSPPAIVS
LDRSEDRKEN NSIDVPYRVV DVNEVSQNHF IPRKRVLFRE KTHNKRIQEL LAEKRRQDFL
LRRLKRKPGD
//
