ID A0A383ZER5_BALAS Unreviewed; 1593 AA.
AC A0A383ZER5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 7 {ECO:0000313|RefSeq:XP_007173566.1};
GN Name=ADAMTS7 {ECO:0000313|RefSeq:XP_007173566.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007173566.1};
RN [1] {ECO:0000313|RefSeq:XP_007173566.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007173566.1};
RG RefSeq;
RL Submitted (JAN-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_007173566.1; XM_007173504.1.
DR STRING; 310752.A0A383ZER5; -.
DR KEGG; bacu:103011709; -.
DR CTD; 11173; -.
DR InParanoid; A0A383ZER5; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000261681; Unplaced.
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; -; 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; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF142; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 7; 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; 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; 8.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 8.
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:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 153..363
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1539..1579
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 99..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1024
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1095
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 115
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 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 299
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 303
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 309
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 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 229..283
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 258..265
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 277..358
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 316..342
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 385..408
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 396..414
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 403..433
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 427..438
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 461..498
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 465..503
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 476..488
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1593 AA; 173385 MW; 11D0DF86E23B8EEF CRC64;
METEHATEGR AALDIVHPVR VDAGGSFLSY ELWPRALPCH LLGEVQDPEL EGGLAAISAC
DGLKGVFQLS NEDYFIEPLD GVPARPGRAQ PHVVYKRQAP ERWAEPGDPR APGTCGVKES
PELEPRRERW EQRQQWRRQR PRRLHQRSVS KEKWVETLVV ADAKMVEYHG QPNVESYVLT
IMNMVAGLFH DPSIGNPIHI TIVRLVLLED EEEDLKITHH ADNTLRSFCK WQKGINMKRD
AHPLHHDTAI LLTRKDLCAA MNQPCETLGL SHVAGMCQPH RSCNINEDTG LPLAFTVAHE
LGHSFGIQHD GSGNDCEPVG KRPFIMSPQL LYDAAPLTWS RCSREYITRF LDRGWGLCLD
DSPTKDVIDF PSIPPGVLYD VGHQCRLQYG AYSAFCDDMD NVCHTLWCSV GTTCHSKLDA
AVDGTRCGES KWCLNGECVP MGFRPEAVDG GWSGWSAWSV CSRSCGVGVQ SAERQCTQPA
PKYKGRYCVG ERKRFRLCNL QACPAGRPSF RQVQCSHFDA MLYKGQLHTW VPVVNDVNPC
ELHCRPSNEY FAEKLRDAVV DGTPCYQGQA SRDLCINGIC KNVGCDFEID SGAIEDRCGV
CHGNGSTCHT VSGTFEEAEG LGYVDVGLIP AGAREIRIEE VAEAANFLAL RSEDPDKYFL
NGGWIIQWNG DYQVAGTTFT YARTGNWENL TSPGPTDEPI WIQLLFQESN PGVRYEYIIH
READGHSQIQ PPEFSWHYGP WTKCTVTCGT GMQRQSARCV ERQAGPVDER HCEPLGRPDD
RQRKCSEEPC PARWWAGEWQ LCSSSCGPGG LSRRAVLCIH SVGLDEQSAL EPPACEHLPR
PPAETPCNRD VPCPATWAVG NWSECSVTCG PGTQHRSILC TNDTGVPCDE DQQPASEAAC
RLPPCPRALD VLGPEGSGSG SSSRELFNEV DFIPHRPAPR PPPPSSPKPA GMGNAIGEED
PELGPPGPMF VDDFYYDYNF INFHENLSYG PFGEPDADPA GTGGWMPPPP SSPAEPPAGT
PTPATEPSGP EDGGALGDWS PAPWPSQAGR SPPPPSEQTP GNSLVNFLFE EDAPIGAPDL
GLPSLPWPPT PVSMETPAAP GSQNKFLGGE DSHSQPPPPW WERTNEVSED SEEDLGRRAP
QRPSPTLPPL SSISTSHSSP SPDTVELWTS GTLAWEPALE GGLGPVGNEL WPTVGGAPPP
PPTASLPDTQ GTDSALEPGT STLSTPDLAL RDLQTLAMPG TFLLKAPTGL GHTPWVTALS
LGPLGQPESP SPETPPSPVP LSIPAQDSPA NSSRAPGPLD PSSAEEEPPV DLLPVRNASW
QVGNWSECST TCGLGAVWRP VRCSSGREED CTPAARPQPA RRCHLRPCAA WHTGSWSKCS
RSCGGGSSVR DVQCVDTRDL QPLRPFHCQP GPAKPPARRP CGAQPCLSWY ISSWRECSEA
CGGGEQQRLV TCPEPGLCEE ALRPNSTRPC NTHPCTQWVV GPWGQCSAPC GGGVQRRLVK
CVNTQTGLPE EDSDQCGHEA WPESSRPCGT QDCELTEPPP LGCERDRLSF GFCETLRLLG
RCQLPTVRTQ CCRSCPPPGR GAPSRGHQRV ARR
//
