ID M4A2W1_XIPMA Unreviewed; 1653 AA.
AC M4A2W1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 9 {ECO:0000313|Ensembl:ENSXMAP00000008805.2};
GN Name=ADAMTS9 {ECO:0000313|Ensembl:ENSXMAP00000008805.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000008805.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000008805.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000008805.2};
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; ENSXMAT00000008819.2; ENSXMAP00000008805.2; ENSXMAG00000008746.2.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156409; -.
DR HOGENOM; CLU_000660_0_1_1; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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; 9.
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:SF278; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF A, ISOFORM B; 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; 9.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 11.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 10.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 10.
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:UP000002852};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1653
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017340791"
FT DOMAIN 306..515
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 121..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 450
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 454
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 460
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 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 513
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 513
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 381..434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 410..416
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 428..510
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 466..494
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 537..559
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 548..569
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 554..588
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 582..593
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 616..653
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 620..658
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 631..643
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1653 AA; 182575 MW; BD5D8B07DB58A754 CRC64;
MHVLLWGLGF LLFPDLLNVV ASTGRLLRSS SAAPEELAAY EIVTPVRVNE AGDRLPAGVH
FKRKRRSLDE GTGSAADHWA AANIHYRISA FGKNYHLNLT LDSGFIAPVY TVTVLGAPQG
DNGTAFATDA EREEEEEEEE EEEDTELRHC FYRGHVNAHA QHAAVISLCA GLFGTFRSPE
GEYFVEPLHS YQGEQYEEEH TKPHIVYRKL SSGNRTSEET SACDTSGHKH RHKRQRARRR
PAPVAGSASP LVGAGMLDDL GSLSASLTGS AWLTSERGVA GNRPSNDSGG DSGPHRRSKR
FLSYPRFVEV MLVADSKMVE HHGSNLQHYI LTLMSIVSSI YKDPSIGNLI NIVIVKLVII
NNELDGPAIS FNAQTTLKNF CIWQQNQNVP DDNHPSHHDT AILITRQDIC RARDKCDTLG
LAELGTVCDP YRSCSISEDN GLSTAFTIAH ELGHVFNMPH DDSNKCKEDG VKSQQHVMAP
TLNYNTNPWM WSKCSRKYIT EFLDTGYGEC LLDEPVSGPY SLSKQLPGRI YSVNRQCELI
FGAGTQVCPY MTQCRRLWCT SPEGAQRGCR TQHMPWADGT DCEPGRHCKH GRCIPNEHDA
SPVDGAWGVW SPFGTCSRTC GGGIKIAMRE CNRPVPQGGG MYCVGRRMKF RSCNSEPCSK
QKKDFREEQC AVFDGKHFNI NGLPPNVRWV PKYSGILMKD RCKLFCRVAG STAYYQLRDR
VIDGTPCGPD TNDICVQGLC RQAGCDHVLN SKARRDKCGV CGGDNSSCKT VAGPFNTVRY
GYNEVVRIPS GATNIDVRQH SYSGKPEDDN YLAISNSRGE FVLNGDFVVS MFKREIKVGD
AVIEYSGSDH VIERINCTDR IDEEIIVQVL SVGNLYNPDV SYSFNIPIED KPQQFFWDAY
GPWQECSRLC QGERKRKILC SRESDRVVVS DQRCHSSARP AAITEPCNTE CEVRWHVARK
SECTAQCGVG YRTLELYCAK ISQSDGKTQK VDDRYCSGQR KPDDREGCHG DCNPGGGWDY
SPWSECSKSC GGGTRRRGAV CRKSSDDGDD DESNCSQRDK LTVQTCNEFL CPQWKTGDWS
ECLVTCGKGY RHRQTWCQFG EDRLDDRFCG AAKPESVQAC QQQECASWQV GPWGQCTTSC
GPGYQMRAVK CVVGSYGAVM NDAECNAAAR PTDTQDCEVA QCSGSHPVPP VTKVPSHQGH
RTQWRFGSWT QCSASCGKGT RMRYVSCRDN QGGVAEESAC AHLTKPPARE VCSVVACGQW
KVLEWTACSV TCGQGKTTRE VVCVSFSDQE VNANECDPDD RPATEQDCAL SQCPSRPSES
LPLPSSPNTI TRSNVARGHS HQWRTGPWGA CSSTCAGGFQ RRVVVCQDEN GYPANSCEDR
NRPTEQRSCE SGPCPQWVYG NWGECTKPCG GGIKTRLVVC QRPNGERFND LSCEIHDKPP
DREQCNTQPC PSSPHWSTDP WSSCSASCGR GVKSRKVSCV TGSGRSIQDE NCRHSSPKPS
KQRRCRGGRC PKWKTGGWGE AVTQVLCTRQ ERMCFSSKQL WSSTHARSKW EQSKRWKANA
VSCKNVQPHA VTEFSGGRFS VRLETGVAPR RPAVPSALVR RPARAAVSQT VPLATAGEKG
TGRRAVSPAD RAIEGEHCSA LITTITRSMK CTA
//
