ID A0A1J1J1B9_9DIPT Unreviewed; 994 AA.
AC A0A1J1J1B9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=CLUMA_CG018759, isoform A {ECO:0000313|EMBL:CRL05730.1};
GN ORFNames=CLUMA_CG018759 {ECO:0000313|EMBL:CRL05730.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL05730.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRL05730.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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; CVRI01000065; CRL05730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1J1B9; -.
DR STRING; 568069.A0A1J1J1B9; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
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; 2.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF200; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF B, ISOFORM B; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 2.
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:UP000183832};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..994
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012949849"
FT DOMAIN 267..478
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 111..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..133
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 414
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 208
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 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 413
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 417
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 423
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 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 345..397
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 374..379
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 391..473
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 430..457
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..527
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 515..533
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 522..552
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 546..557
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 580..617
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 584..622
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 595..607
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 994 AA; 112398 MW; 872CDB644E28918D CRC64;
MLFISVCIIK LFLIATLASG AIEHRGIFSN SLREANLIIP RKVNNEGDFI SHDLVHHHAH
DYYNEETGDS EDHKVHYHID LHNETLHLEL EPSTSFVAPM MIVERHKRDL RERHKKSHHK
TQCHYHGKIR GHQHSKVALS TCNGLAGYVR TNKNEYLIEP SRNHKVSNNG HPHVVFHRSA
VKNNHESDKK GAQKRRKKRR KRRHHSNCGT REPRRSADTK IEWQAQGKVI VQGGRRVRNH
RERERERERE RKHHNKRRVT RSVIKPRHVE ALVVADPSMM QFHEGGDVET YLLTIMNMVS
SLYKDPTIGN SVHVVVVKII LLEEEDAYQD LNVTQVATAT LESFCRWQRT LNPKQDDDPQ
HHDVAILVTR QNICSNAGCA TLGIANVGGM CRADKSCSVN EDNGITLAHT ITHELGHNFG
MYHDTAKTGC DHRSGPILHI MTPSFEADTV QVSWSNCSRR DITHFLDQGL GKCLEDPPTP
LEEYQYPELP AGAMYNADLQ CRLQFNATDE DMKVCSQLDE ICSQLWCLLN GTCTTLLRPA
APGTHCARHK WCQDQKCVDI EDLPAPVDGG WGNWSEWGQC SRACGAGVSL QTRECDHPTP
VHGGSFCIGE RARYKTCNID PCPADESSFR AQQCSKQNSK PIKGQLYNWS PFLDTHDPCK
LYCTDQDDTL IHAFDAAEDG TSCNTGTNDM CIGGICKKVG CDWIVGSNTT EDQCGICGGD
GSTCSTIKGE FTKKINMSEG YYEITLIPSG SRHIIIEEMG PSKNFIGIGK ADSKDFYLNG
DRLISMSGEY DIAGSVGLYE RESEQEKLKI PGPIKEDISL YIVFKGKHKN LGVQYEYTLP
SNSTNDKTYH WKLSDFTPCT KTCGGGVQQR FPVCYKRYEG IVEEELCWKN AENKRPEKIS
RTCNDEPCSA YWWVGPWQPC PVTCQRITDI HKPLKKRTIL CVDQNEYALP SEQCQDQTRP
SDYEPCSLIL PPCSLDDNIL NNSDFSDNEI PDTI
//
