ID A0A1S2ZK98_ERIEU Unreviewed; 1933 AA.
AC A0A1S2ZK98;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 9 {ECO:0000313|RefSeq:XP_007520681.1};
GN Name=ADAMTS9 {ECO:0000313|RefSeq:XP_007520681.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007520681.1};
RN [1] {ECO:0000313|RefSeq:XP_007520681.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007520681.1; XM_007520619.1.
DR STRING; 9365.ENSEEUP00000000271; -.
DR GeneID; 103111340; -.
DR CTD; 56999; -.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; A0A1S2ZK98; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; 13.
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; IPR012314; Pept_M12B_GON-ADAMTSs.
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; PF08685; GON; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 13.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 14.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 13.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 14.
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:UP000079721};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1933
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010277110"
FT DOMAIN 290..496
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1733..1933
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 214..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 432
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 431
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 435
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 441
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 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 365..415
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 391..397
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 409..491
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 447..475
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 518..540
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 529..550
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 535..569
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 563..574
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 597..634
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 601..639
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 612..624
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1933 AA; 216450 MW; 2297817B3D5A8011 CRC64;
MQFVSWATLL TLLVRDLAEM RSPDAATAVR KDRLHPRQVK LLENLSEYEV ASPIRVNALG
EPFPANLHFK RRRRSIQPAS DPWPDFASSS SSTSSQAHYR LSAFGQQFLF NLTAHAGFIA
PQFTVTLLGE PGRNQTQFYS EEESELKHCF YRGHVNTKYE HTAVISLCSG MLGTFRSHDG
DYFIEPLLYV DEQEDEEVQH KPHIIYRHGI SDRQPSMERH TCDTPEHSSN PSKDKRKTRK
WGGRSSLADD VSVLKSSLTT KALSDYTNET DSMRGKRAHR RAKRFLSYPR FVEVMVVADN
KMFLYHGANL EHYILTLMSI VASIYKEPSI GNLINIVIVN LVVIHNEQEG PSISFNAQTT
LRNFCQWQHS KNYPGGIQHD TAVLVTRQDI CRAHDKCDTL GLAELGTICD PYRSCSISED
SGLSTAFTIA HELGHVFNMP HDDSNKCKEE GVKSTQHVMA PTLNFYTNPW MWSKCSRKYI
TDFLDTGYGE CLLNEPEHRP YYFPSQLPGV LYSVNKQCEL IFGPGSQVCP YMMQCRRLWC
NNMDGTHKGC RTQHTPWADG TECEPGKHCK FGFCVPKEME PPVTDGSWGS WSPFGACSRT
CGGGIRTTVR ECNRPEPKNG GKYCIGRRMK FKSCNTEPCP KQKRDFREEQ CAHFDGKHFN
INGLHSNVRW VPKYSGILMK DRCKLFCRVA GNTAYYQLRD RVIDGTPCSQ DTNDICVQGL
CRQAGCDHVL NSKARRDKCG ICGGDNSSCK TVAGTFNTVH YGYNTVVRIP AGATNIDVRQ
HSFSGKSEDD NYLALASSDG EFLLNGDFVV TMSKKEIRFG NALVEYSGSD NAVERINCTD
RIEKDLLLQV LSVGKLYNPD VRYSFNVPID GDKPQQFYWN SHGPWQACSK PCQGERKRRP
VCVRESDQLT VSDQRCDRLP QPGPVTEPCS TDCDLRWHVA GRSECSAQCG LGYRTLDIYC
AKYSRLDGSI ERVDDSFCSS HPKPNNQEKC SGECSTGGWH YSAWTECSKS CGGGTQRRRA
MCVNTQNELL DESKCSHQEK VTTHSCNEFP CPHWKTGDWS ECLVTCGKGH KHRQVWCQFG
EDRLNDRMCD PETKPASMQA CQQPECASWQ AGPWGQCSVT CGQGYQLRAV KCVIGTYMSV
VDDSDCNAAT KPTDTQDCEL PPCHSPPVAP DTRRSMHAVP RTQWRFGSWT PCSATCGKGT
RMRYVSCRDE NGSVADESAC ATLSRPVANE ECSVTPCGRW KALDWSPCSV TCGQGRATRQ
VLCVNYSDRV IDQSECDPEY IPETKQDCSM QPCPQRIPAD VLGQRPFQNE DYRPRSTSPG
THVLGGNQWR TGPWGACSST CAGGSQRRVV VCQDENGYTA TDCEERIKPD EQRVCESGPC
PQWVYGRWGE CSKLCGGGLR TRLVVCQRPN GERFPDLSCE ILDKPPDREQ CNTHTCPQDA
GWNTGPWSSC SVSCGRGHKQ RNVYCMAKDG SHLESDYCKH LAKPSGHRKC RGGRCPKWKA
GAWSQCSVSC GHGVRRRNVD CQMGTHKISR ESACNPYTRP ESERACQALP CPLYVWRADE
WQECTKTCGT GSRYRKVVCM DEDKGSEVHG VHCDVSQRPS DRESCSVQPC EYIWITGEWS
ECSVTCGKGY KQRLVSCSEI YTGKENYEYS YQTTINCPGM QPPSVQPCYL RECPVSAAWR
VGNWGSCSVS CGVGVMHRSV QCLTNEDQPS HLCPTDSKPE ERKTCHNTHN CGLAQSCKEV
KRLNAVSEDG EYFLVIKGKP LKVFCAGMQS DHPKEYMTLV DGDSENFSEV YGHRLHNPTE
CPYNGSRRDD CQCRKDYTAA GFSTFQKIRI DLATMQIITT DLQFARTREG HPVPFATAGD
CYSAAKCPQG RFSINLYGTG LSLTDSARWT SQGNYAVSDI KKSPDGTRVI GKCGGYCGKC
TPSSGTGLEV RVL
//
