ID U3JC10_FICAL Unreviewed; 1226 AA.
AC U3JC10;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 18 {ECO:0000313|Ensembl:ENSFALP00000000314.1};
GN Name=ADAMTS18 {ECO:0000313|Ensembl:ENSFALP00000000314.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000000314.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000000314.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000000314.1}
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_005052782.1; XM_005052725.2.
DR RefSeq; XP_016156727.1; XM_016301241.1.
DR AlphaFoldDB; U3JC10; -.
DR STRING; 59894.ENSFALP00000000314; -.
DR MEROPS; M12.028; -.
DR Ensembl; ENSFALT00000000317.2; ENSFALP00000000314.1; ENSFALG00000000306.2.
DR GeneID; 101813050; -.
DR KEGG; fab:101813050; -.
DR CTD; 170692; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000157553; -.
DR HOGENOM; CLU_000660_1_0_1; -.
DR OMA; IQPCHTQ; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000016665; Chromosome 11.
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:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
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; 6.
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; 5.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 6.
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:UP000016665};
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}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1226
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004645209"
FT DOMAIN 295..500
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1189..1226
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 210..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 439
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 442
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 448
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 495
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 371..422
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 397..404
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 416..495
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 455..479
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 523..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 534..555
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 543..574
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 568..579
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 603..640
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 607..645
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 618..630
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1226 AA; 136007 MW; 3BAA84129F7BFEEF CRC64;
MDCLLLAVWT LPAAILGGSS MPFQTLPWLG STVKTLQLCC LCCLSHAATL TSDSISELTH
DYVFVTPVRV DASGSYISHD VLHSTRRKRS TQSSKSSLHY KFSAFGQELH LELKPSTILS
NSFIVQVLGK DGVSHSQEHE IEQCFYQGFI RNDSTSSVAI STCVGLSGLI RTRQMEFLIS
PLPQQLAREH NFTSPAGHHP HVLYKRTAEG KVHLSPARPH PKSSPGRRRA RASRGPHAPA
SAYRHGRFQK LHFCGRRKKY APKPPTAETY IRSDEYGTSA RFKRSSAKIQ KNGSLNVETL
VVADKKMLEK HGKENVTTYI LTVMNMVSSL FKDGTIGSDI NIIVVSLLLL EQEPGGLLIN
HHADQSLNSF CQWQSALVGK NGKRHDHAIL LTGLDICSWK NEPCDTLGFA PISGMCSKYR
SCTINEDTGL GLAFTIAHES GHNFGMIHDG EGNACRKAEG NIMSPTLTGN NGVFSWSVCS
RQYLNKFLST AQAACLIDEP KQTGQYKYPD KLPGQIYDAD TQCKWQFGMK AKLCNLSFVK
DICKSLWCHK VGHRCETKFM PAAEGTACGI SMWCRRGQCV RYGDHGPRAV NGQWSAWSQW
SECTRTCGGG VTYQERHCNN PKPQYGGKFC QGSSRVYQLC NKQPCPADSL DFRALQCAEY
NSKPFRGWFY KWKPYTKVEE EDRCKLYCTA EDFDFFFAMS SKVKDGTLCS PNNYDVCIDG
ICEQVGCDHG LGSKAVLDAC GVCKGDNSTC KFFKGQYLIQ HKANDYYAVV TVPAGARSIQ
LQEMHVSPSY LAVRSLASRY YLTGDWTIDW PGKFPFAGTV FDYQRSFSHP ESLYAAGPTN
ETLVFEILLQ GKNPGISWEY TFAKSSIENK TSVRKHSYSW VTVQSECSVT CGGGHITAKA
VCLEDHRARV NSSLCGPRTK PLTETKLCNT HPCPAYWSAG EWSTCSKSCG GGQQSRLIQC
VQKRAFQREE VVAHSLCPVS TPAQVQVCST QDCPPEWSPG PWSQCSKTCG RGIKKRDVYC
KSTGSPKVKI LPEDMCSTDP KPESQQTCVL GRCPKNDRLQ WVISSWSECS ASCGPGLRQR
ELKCGEKSIH GKLVTFPQRR CRNIKKPNTN LEEACNKGAC PSQTLYNMVS GWYSSPWQQC
TVSCGGGVQT RSVQCLRQGR PAAGCLPQQK PAVLRACNTN FCPAPGKRDD PSCVDFFTWC
HLVPQHGVCN HKFYGKQCCK SCTKKN
//
