ID A0A452S7D6_URSAM Unreviewed; 1569 AA.
AC A0A452S7D6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 9 {ECO:0000313|Ensembl:ENSUAMP00000028090.1};
GN Name=ADAMTS9 {ECO:0000313|Ensembl:ENSUAMP00000028090.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000028090.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000028090.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR STRING; 9643.ENSUAMP00000028090; -.
DR Ensembl; ENSUAMT00000031376.1; ENSUAMP00000028090.1; ENSUAMG00000021657.1.
DR GeneTree; ENSGT00940000156409; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
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 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; 13.
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; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 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; PF19030; TSP1_ADAMTS; 13.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 15.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 14.
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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
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:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 76..135
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1369..1569
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 787..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 86..114
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 157..179
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 168..186
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 174..205
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 199..210
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 233..270
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 237..275
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 248..260
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1569 AA; 175197 MW; 08D6A425D31408C1 CRC64;
TKPKRNEWNG LHRLFPQLLD ACETSLHTSV CRGDSPLNAK LATCANFVSG ESSRENSPSE
FVTRAENGMW VIELMFNMPH DDNNKCKEEG VKNPQHVMAP TLNFYTNPWM WSKCSRKYIT
EFLDTGYGEC LLNEPESRPY PLPHQLPGLL YNVNKQCELI FGPGSQVCPY MMQCRRLWCN
NVDGVCRTQH TPWADGTECE PGKHCKYGFC VPKEMEGPVT DGSWGSWSHF GTCSRTCGGG
IKTAVRECNR PEPKNGGKYC VGRRMKFKSC NTEPCLKQKR DFREEQCAQF DGKHFNINGL
LPTVRWVPKY SGILMKDRCK LFCRVAGNTA YYQLRDRVID GTPCGQDTSD ICVQGLCRQA
GCDHVLNSKA RRDKCGVCGG DNSSCKTVAG TFNTVHYGYN TVVRIPAGAT NIDVRQHSFS
GKSEDDNYLA LSSSKGEFLL NGDFVVTMSK REIRFGNAVI EYSGSDNVVE RINSTDRIEQ
ELLLQVLSVG KLYNPDVRYS FNIPIEDKPQ QFYWNSHGPW QACSKPCQGE RKRKPVCTRE
SDQLTVSDQR CDRLPQPAPI TEPCGIDCDL RWHVASRSEC SAQCGLGYRT LDIYCAKYSR
LDGKTEKVDD SFCSGHPKPS NREKCSGECN TGGWRYSAWT ECSKSCDGGS QRRRAICVNT
RNDVLDDSKC THQEKVTVQR CNEFPCPQWK TADWSECLVT CGKGHKHRQV WCQFGEDRLN
DRICDPETKP ASMQTCQQPE CASWQAGPWG QCSVTCGQGY QLRAVKCIIG TYMSVVDDND
CNAATRPTDT QDCELPSCHP PPAVPEPRRS THNTPRTQWR FGSWTPCSAT CGKGTRMRYV
SCRDEDGSVA DESACRTLPR PVAKEECSVT PCGQWKALDW SPCSVTCGQG RATRQVVCVN
YSDHVIDQSE CDPDYIPETD QDCSTSPCPQ RTPDSGLAQH PFQSEDYGPR SAGPSRTHVL
VGNQWRTGPW GACSSTCAGG SQRRVVVCQD ENGYTANDCV ERIKPDEQRA CESGPCPQWA
YGSWGECTKL CGGGLRTRLV VCQRPSGERF PDLSCEILDK PPDREQCNTH ACPPDAAWNT
GPWSSCSVSC GRGHKQRNVY CMAKDGSHLE SDYCKHLAKP NGHRKCRGGR CPKWKAGAWS
QCSVSCGQGT RRRSVGCQMG AHKIARESEC NPYTRPESER VCQAPPCPLY AWRAEEWQEC
TKTCGEGSRY RKVVCVDADK GSEVHGVQCD LSQRPVDRES CSLQPCEYVW ITGEWSECSV
TCGKGYKQRL VSCSEIYPGK ENYEYSYQTT INCPGTQPPS VHPCYLRECP VSATWRVGNW
GSCSVSCGVG VTHRSVHCLT NEDQPSHLCP ADLKPEERKT CHNIYHCELP QNCKEVKRLK
GTREDGEHFL LIKGKLLKIF CAGMQSDHPK EYITLVHGDS ENFSEVYGHR LHNPTECPYN
GSRRDDCQCR KDYTAAGFSS FQKIRIDLTT MQIITTDLQF ARTSDGHPVP FATAGDCYSA
AKCPQGRFSI NLYGTGLSLT ESARWISQGN YAVSDIKKSR DGTRVIGKCG GYCGKCTPSS
GTGLEVRIL
//
