ID H2TNA9_TAKRU Unreviewed; 1127 AA.
AC H2TNA9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 18 {ECO:0000313|Ensembl:ENSTRUP00000026165.3};
GN Name=ADAMTS18 {ECO:0000313|Ensembl:ENSTRUP00000026165.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000026165.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000026165.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000026165.3}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; H2TNA9; -.
DR STRING; 31033.ENSTRUP00000078708; -.
DR MEROPS; M12.030; -.
DR Ensembl; ENSTRUT00000026272.3; ENSTRUP00000026165.3; ENSTRUG00000010392.3.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000157553; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000005226; Chromosome 13.
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; 4.
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:SF167; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 18; 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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
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:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 232..437
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1089..1126
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 137..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 375
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 379
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 385
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 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 308..359
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 334..341
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 353..432
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 392..416
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 460..485
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 471..492
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 480..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 505..516
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 540..577
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 544..582
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 555..567
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1127 AA; 125897 MW; 7D605CD693001068 CRC64;
PRLWFLSHDV TGRSHRARRS LSPSVHYRLS AFGQDMQLDL HPSSVVGPGF TVQSLGSEGI
TTVTDDAGFH NCLYQGFVRN LSSSSAALST CSGLAGFIRM SQEEYLIAPL PQHLAEEHNY
RAPDGHHPHV IYKRSAEHVV HRGSSGTSSS RPANPYQQQH HHQQLHQQHH HHHDDQQEKL
ERKHFCGRRK QYAPKPPTDD RFIMPDEFAT PATDESGRAK RSPINSNRVG GLNVETLVVA
DRKMLEKHGR DNVTTYVLTV MNMVSSLFKD GTIGSDINIV VVSLLLLEED PLGLTISHHA
DQSLNSFCQW QSGLLGKGGK RHDHAVLLTG LDICSWKNEP CDTLGFAPIS GMCSKYRSCT
INEDTGLGLA FTIAHESGHN FGMIHDGEGN PCRKTEGNIM SPTLAGNNGV FFWSTCSRQY
LSRFLGTTQA SCLVDEPKQI GQYKYPEKLP GQLYDADTQC KWQFGSKAKL CSLDFVKDIC
KSLWCHRTGH RCETKFMPAA EGTTCGPDMW CRRGQCVKFG EHGPKAVHGQ WSAWSQWSDC
SRTCGGGVMY RERSCTSPRP QNNGKFCPGS SRFNQLCNTR PCPPNAVDFR AQQCAEYNSK
LFRGWYYKWK PYTKVDDEDI CKLYCIAEDF DFFFAMSSKV KDGTPCSKTE TNVCIEGVCE
EVGCDQILGS QASLDACGIC KGDNSTCKFF KGQYTLQHRA NEYYTMVVIP AGARSIHVQE
MAVSTSYLAV RSIKKKYYLT GDWTVDWPGK FHIGGTMFDY QRSFNKPESL YAAGPTNETL
VFEILLQGKN PGVVWEYTLP RTEKKPDYSW GVVSLSYDSV CVCVCLLVLS LCTSRNPSWA
PGDWGLCSRS CGGGQQTRPL RCLRKVTYQR EEVVAHSLCP IISPAQVQPC QTQTCPPEWS
TGSWSQCSKT CGRGLRKRSV FCSSTDPGVT AVVVPDSMCR QHHKPKAQET CVLRRCPKNE
RLQWFPTPWG EVTPVELTLR LFPCRNVEFP IRRCRNIARP LVDLQRSCNR SPCPEPSHAV
PGRSPSSAVV LGWYSSPWQQ CSVSCGGGVQ TRSIQCLRQG RPAAGCLPHQ RPVTSRACNT
QFCPAAPSAP PQCTDHFSWC HLVPQHGVCN HKFYGQQCCR SCSRKRP
//
