ID A0A1S3KTE1_SALSA Unreviewed; 1235 AA.
AC A0A1S3KTE1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 18-like isoform X1 {ECO:0000313|RefSeq:XP_013981976.1};
GN Name=LOC106561991 {ECO:0000313|RefSeq:XP_013981976.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013981976.1};
RN [1] {ECO:0000313|RefSeq:XP_013981976.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013981976.1};
RG RefSeq;
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 RefSeq; XP_013981976.1; XM_014126501.1.
DR AlphaFoldDB; A0A1S3KTE1; -.
DR STRING; 8030.ENSSSAP00000061704; -.
DR PaxDb; 8030-ENSSSAP00000061704; -.
DR Ensembl; ENSSSAT00000091700; ENSSSAP00000061704; ENSSSAG00000055869.
DR GeneID; 106561991; -.
DR KEGG; sasa:106561991; -.
DR CTD; 170692; -.
DR OMA; IQPCHTQ; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
DR Bgee; ENSSSAG00000055869; Expressed in nose and 4 other cell types or tissues.
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; 5.
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; 4.
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; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
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:UP000087266};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1235
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010226420"
FT DOMAIN 292..494
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1197..1234
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 211..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 433
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 432
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 436
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 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 368..416
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 391..398
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 410..489
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 449..473
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 517..542
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 528..549
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 537..568
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 562..573
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 597..634
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 601..639
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 612..624
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1235 AA; 137552 MW; 55BBFCA8F1548EB5 CRC64;
MDCLFLLIWT LPIPLVSCTS VKILSTLWFW NTLKTLHIYC SHSIYSVSST FASDTSGLNH
DYVFVTPIEV DAQGGYVSHD MLRRGRNKRS LPSMGGPVHY RLSAFGWDMH LDLQPSMVVA
EGFTVQVLGT EGITTLAQEP AHQDCLYQGF IHNLTASSAA ISTCSGLSGL IRMSDDEYFI
TPLPQHLAAE HNYSSPSGHH PHVVYKRSAE HKVHGGQGSI HSSQPDNPYL QHHHQHHHDY
QHGKLQRQHF CGRRRQYTPK PPAKDRLIMP DEFELPGRAK RSPITSNKVG GLNVETLVVA
DRKMLEKHGR ENVTTYVLTV MNMVSSLFKD GTIGTDINIV VVSLLLLEQD PLGLSINHHA
DQSLNSFCQW QSGLIGKRHD HAVLLTGLDI CSWKNEPCDT LGFAPISGMC SKYRSCTINE
DTGLGLAFTI AHESGHNFGM IHDGEGNPCR KAEGNIMSPT LAGNNGVFSW SACSRQYLSR
FLGTAQASCL VDEPRQIGQY KYPEKLPGQL YDADTQCKWQ FGSKAKLCNL DFVKDICKSL
WCHRTGHRCE TKFMPAAEGT SCGTDMWCRR GQCVKYGDHG PRAVNGQWSG WFEWSDCSRT
CGGGVMYRER SCTSPRPQHN GKFCQGSARL NQLCNTKPCQ PSGVDFRAQQ CAEYNSKPFR
GWYYKWKPYT KVEAEDICKL YCIAEDFAFF FAMASKVKDG TSCSDHRGDV CIEGVCEPVG
CDQVLGSKAT LDACGVCRGD NSTCKFFKGH YVLQHRANEY YAMVTIPPGA RSIHVQEMEI
STSYLAVRTL KRKYYLTGDW TVDWPGKFQF GGTVFDYQRS FNRPESLYAA GPTNETLVFE
ILLQGKNPGV VWEYTLPRSE RKPNYTWGVV RSDCSAPCAG GQISTKAICL QDQRTQVNST
QCNPQTRPVL SSHLCNTQPC PAYWTTGNWG PCSQSCGGGQ QTRHIQCLRK VTYQREEVVA
HSLCPVIAPA QVQPCHTQAC PPEWSSGAWS QCSKSCGRGM RKRGVFCRST DPGAKAVVVP
DSMCKPHLKP KAQETCVLRR CPKNDRLQWF TTPWGECSTS CGPGVRRREL RCGERDSQGD
YTDFPMRRCR NLPKPSGDLQ QTCSRGPCPE PRLVAQGRTA SAVVLGWYSS PWQQCSVSCG
GGVQSRSIQC LRQGRPAAGC LNHQRPVTSR ACNTHFCPAP PIHVPAHVPA PAPTLKDEQS
CVDYFSWCHL VPQHSVCNHK FYGQQCCKSC NGKKL
//
