ID A0A452F339_CAPHI Unreviewed; 1882 AA.
AC A0A452F339;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 9 {ECO:0000313|Ensembl:ENSCHIP00000018590.1};
GN Name=ADAMTS9 {ECO:0000313|Ensembl:ENSCHIP00000018590.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000018590.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000018590.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000018590.1}
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 -!- 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 EMBL; LWLT01000024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013828998.1; XM_013973544.2.
DR Ensembl; ENSCHIT00000026404.1; ENSCHIP00000018590.1; ENSCHIG00000017918.1.
DR GeneID; 102179423; -.
DR CTD; 56999; -.
DR GeneTree; ENSGT00940000156409; -.
DR OMA; DNDFQFA; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000291000; Chromosome 22.
DR Bgee; ENSCHIG00000017918; Expressed in uterus and 18 other cell types or tissues.
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; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 12.
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:SF33; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 9; 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; 12.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 13.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 12.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 13.
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:UP000291000};
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..1882
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019461509"
FT DOMAIN 293..499
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1682..1882
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 212..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 434
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 438
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 444
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 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 368..418
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 394..400
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 412..494
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 450..478
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 532..553
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 538..573
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 566..578
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 601..638
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 605..643
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 616..628
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1882 AA; 209984 MW; BC896CB7E3FA4248 CRC64;
MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI ASPVRVNALG
EPFPTNVHFK RRRRSINSAS DPWPGFASSS SSATSSQEHY RLSAFGQQFL FNLTAHAGFI
APMFTVTLLG APGVNQTKFY SEEEAELKHC FYKGHVNTKS EHTAVISLCS GMLGTFRSHD
GDYFIEPLLS IDEQEDEEAQ NKPHIIYRHS TRHREPATGR HACDTSEHRN SHSKDKRKTR
TRRWRGRSSL ADDMAVLNSS FTTSTLPANG SKTDSTRQKG THRRTKRFLS YPRFVEVMVV
ADNRMVLYHG ANLQHYILTL MSIVASIYKD PSIGNLINIV IVNLVVIHNE QEGPSISFNA
QTTLKNFCQW QHSKNHPGGI QHDTAVLVTR QDICRAHDKC DTLGLAELGT ICDPYRSCSI
SEDSGLSTAF TIAHELGHVF NMPHDDNNKC KEEGIKSPQH VMAPTLNFNT NPWMWSKCSR
KYITEFLDTG YGECLLNEPE YRPYPLPHQL PGLLYNVNKQ CELIFGPGSQ VCPYMMQCRR
LWCNNVDGAH KGCRTQHTPW ADGTECDEPG KHCKFGFCVP KEMEVPVTDG SWGSWSHFGT
CSRTCGGGIK TAIRECNRPE PRNGGKYCIG RRMKFKSCNT EPCPKQKRDF RDEQCAHFDG
KHFNINGLHP NVRWVPKYNG ILMKDRCKLF CRVAGSTAYY QLRDRVIDGT PCGQDTNDIC
VQGLCRQAGC DHVLNSKARR DKCGVCGGDN SSCKTVAGTF NTVHYGYNVV VLIPAGATNI
DVRQHSFSGK SEDDNYLALS SSKGEFLLNG DFVVTMSKRE IRIGNAVIEY SGSDNAVERI
NSTGRIEQEL LLQVLSVGKL YNPDVRYSFN IPIEDKPQQF YWNSHGPWQA CSKPCQGERK
RKPICTRESD QLTVSDQRCD RLPQPAPITE PCGTDCDLRW HVASRSECSA QCGLGYRTLD
IYCAKYSRLD GKTEKVDDSF CSSHPKPSNQ EKCSGECNTG GWRYSAWTEC SKSCDGGTQR
RRAICVNARN DVLDDSKCTH QEKVTIQKCS EFSCPEWKSG DWSECSVTCG QGYQLRAVKC
IIGTYMSVVD DNDCNAATRP TDTQDCELPS CQPPPAAPEA RRSTHSAPRT QWRFGSWTPC
SATCGKGTRM RYVSCRDEDG SVADDSACAT LPRPVAKEEC SVTPCGQWKA LDWNPCSVTC
GQGRTTRQVV CVNYSDHVID QSECDPDYIP ETDQDCSMSP CPQWTPDTDL SQNPFLNEDY
HPRSISPSRT HVLGGNQWRT GPWGACSSTC AGGSQRRVVV CQDENGYTAN DCVERIKPDE
HRACESGPCP QWAYGSWGEC TKLCGGGLRT RLVVCQRPSG ERFPDLSCEI LDKPPDREQC
NTHACPQDAA WSAGPWSSCS VSCGRGHKQR NVYCMAKDGS HLESDFCKHL AKPNGHRKCR
GGRCPKWKAG AWSQCSVSCG QGVRRRNVGC QMGTRKTARE TECNPYTRPE SERACQAPPC
PLYAWRAEEW QECTKTCGEG SRYRKVVCVD EERGGEVHGV HCGMSTRPVD RESCSLQPCE
YVWITGEWSE CSVTCGKGYK QRLVSCSEIY TGKENYEYSY QTTINCPGMQ PPSVQPCFLR
ECPVSATWRV GNWGSCSVSC GVGVMHRSVQ CLTNDDQPSH LCPADLKPEE RKTCHNIYNC
ELPQNCKEVK RLKGASEDGE YFLVVTGKLL KVFCAGMHSD HPKEYMTLVH GDSENFSEVY
GHRLHNPTEC PYNGSRRDDC QCRKDYTAAG FSSFQKVRID LTSMQIITTD LQFARTNEGH
PVPFATAGDC YSAAKCPQGR FSINLYGTGL SLTESARWIS QGNYAVSDIK KSPDGTRVIG
KCGGYCGKCA PSSGTGLEIR VL
//
