ID A0A2K6BDR2_MACNE Unreviewed; 1691 AA.
AC A0A2K6BDR2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 7 {ECO:0000313|Ensembl:ENSMNEP00000009533.1};
GN Name=ADAMTS7 {ECO:0000313|Ensembl:ENSMNEP00000009533.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000009533.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000009533.1}
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 RefSeq; XP_011758881.1; XM_011760579.1.
DR RefSeq; XP_011758882.1; XM_011760580.1.
DR RefSeq; XP_011758883.1; XM_011760581.1.
DR RefSeq; XP_011758884.1; XM_011760582.1.
DR STRING; 9545.ENSMNEP00000009533; -.
DR Ensembl; ENSMNET00000033706.1; ENSMNEP00000009533.1; ENSMNEG00000029214.1.
DR Ensembl; ENSMNET00000033720.1; ENSMNEP00000009546.1; ENSMNEG00000029214.1.
DR GeneID; 105493127; -.
DR KEGG; mni:105493127; -.
DR CTD; 11173; -.
DR GeneTree; ENSGT00940000159819; -.
DR OMA; DIHIVEV; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000029214; Expressed in bone marrow and 1 other cell type or tissue.
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:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
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; 8.
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; 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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 7.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 8.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 7.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 7.
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:UP000233120};
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};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1691
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014561464"
FT DOMAIN 242..452
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1637..1677
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1081..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1672..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 389
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 204
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 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 388
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 392
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 398
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 447
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="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 318..372
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 347..354
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 366..447
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 405..431
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 474..497
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 485..503
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..522
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 516..527
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 550..587
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 554..592
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 565..577
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1691 AA; 185082 MW; F678505C3B60CC96 CRC64;
MPGSPSPRSP AQLLRPLLLL LCALVPGAPG PAPGRATEGR AALDIVHPVR VDAGGSFLSY
ELWPRALRKR DVSVRRDAPA FYQLQYRGRE LRFNLTANQH LLAPGFVSET RRRGGLGRAH
IQAHTPTCHL LGEVQDPELE GGLAAISACD GLKGVFQLSN EDYFIEPLDG APARPGHAQP
HVVYKRQVPE RLAQWGDSSA PSTCGVQVSP ELEPRRERWE QRQQWQRPRL RRLHQRSVSK
EKWVETLVVA DAKMVEYHGQ PQVESYVLTI MNMVAGLFHD PSIGNPIHIT IVRLVLLEDE
EEDLKITHHA DNTLKSFCKW QKSINMKGDT HPLHHDTAIL LTRKDLCAAM NRPCETLGLS
HVAGMCQPHR SCSINEDTGL PLAFTVAHEL GHSFGIQHDG SGNDCEPVGK RPFIMSPQLL
YDAAPLTWSR CSRQYITRFL DRGWGLCLDD PPAKDIIDFP SVPPGVLYDV SHQCRLQYGA
YSAFCEDMDN VCHTLWCSVG TTCHSKLDAA VDGTRCGENK WCLNGECVPV GFRPEAVDGG
WSGWSAWSIC SRSCGVGVQS AERQCTQPTP KYKGRYCVGE RKRFRLCNLQ ACPAGRPSFR
HIQCSHFDAM LYKGQLHTWV PVVNDVNPCE LHCRPSNEYF AEKLRDAVVD GTPCYQVRAS
RDLCINGICK NVGCDFEIDS GAMEDRCGVC HGNGSTCHTV SGTFEEAEGL GYVDVGLIPA
GAREIRIQEV AEAANFLALR SEDPEKYFLN GGWTIQWNGD YQVAGTTFTY ARRGNWENLT
SPGPTNEPVW IQLLFQESNP GVRYEYTIHR EAGGHDEVPS PEFSWHYGPW TKCTVTCGRG
VQRQSVYCSE RQTGPVDEEH CDPLGRPDDR QRKCSEQPCP ARWWAGEWQL CSSSCGPWGL
SHRAVLCIRS VGLDEQSALE PPACEHLPQP PTETPCNRHV PCPATWAVGN WSQCSVTCGE
GTQHRNVLCT NDTGVPCDEA QQPASEVTCS LPPCRWPLDT LGPEGSGSGS SSHELFNEAD
FIPRHLAPRP SPVSSPKPAT MGNAIEEEAL ELDLPGPVFV DDFYYDYNFI NFHEDLSYGP
SEGPDLDLAE TGDQTPPPHS GPAVPSTGSP VPATEPPAAK EEGAPGPWSP SPWPSQAGHS
PPPPSEQTPG NPLINFLPEE DAPRGAPDLG LPSLPWPRVS IDGLQTPAAP ESQNDFPVGK
DSQSQLPPPW RDRTNEVFKD DEEPEGRGAP HPPLRPSPTL PPLSLPPLSP VGSTHSSPSP
DVTELWTGGT VAWEPTLEGG LGPVDSELWP TVGVAPPPPP PIAHLPEMKG RDSPLEPRTP
TFPTPGPGLW DVQTVAVWGT FLPTTLTGLG HTPEPALNPG PKGQPESLSP EVPLSSRLLS
TPAWDSPANS HRTPETQSLA PSLAEAVSPA DPLAVRNASW QAGNWSQCST TCGLGAVWRS
VRCSSGRDED CAPAGRPQPA RRCHLRPCAT WHSGNWSKCS RSCGGGSSVR DVQCVDTRDL
RLLRPFHCQP GPAKPPAHRP CGAQPCLSWY TSSWRECSEA CGGGEQQRLV TCPEPGLCEE
ALRPNTTRPC NTHPCTQWVV GPWGQCSAPC GGGVQRRLVK CVNTQTGLPE EDSDQCGHEA
WPESSRPCGT EDCEPVELPR CERDRLSFGF CERLRLLGRC QLPTIRMQCC RSCSPPSHGV
PSRGHQRVAR R
//
