ID A0A287B361_PIG Unreviewed; 1557 AA.
AC A0A287B361;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 20 {ECO:0000313|Ensembl:ENSSSCP00000050705.2};
GN Name=ADAMTS20 {ECO:0000313|Ensembl:ENSSSCP00000050705.2,
GN ECO:0000313|VGNC:VGNC:85082};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000050705.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000050705.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000050705.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000050705.2}
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 Ensembl; ENSSSCT00000063436.3; ENSSSCP00000050705.2; ENSSSCG00000000795.5.
DR VGNC; VGNC:85082; ADAMTS20.
DR GeneTree; ENSGT00940000158636; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000795; Expressed in heart left ventricle and 29 other cell types or tissues.
DR ExpressionAtlas; A0A287B361; baseline and differential.
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; 9.
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:SF165; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 20; 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; 11.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 11.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 11.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 11.
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:UP000008227};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1557
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023827056"
FT DOMAIN 262..459
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 395
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 394
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 398
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 404
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 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 337..378
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 372..454
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 410..438
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..503
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..513
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 498..532
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 526..537
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 560..597
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 564..602
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 575..587
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1557 AA; 175908 MW; D81489731FC5614D CRC64;
MRVAKWLTGL LYQLSLFITR SWEVHLHPRQ EALVRTLASY EVVTPARVNE FGEVFPQSHH
FSRRKRSSEA PEPTPFRTHY RIRAYGQLFQ LNLSADAAFL AAGYTEVHLG APARQAEDRS
AVPPDLRHCF YRGQVNARED NTAVFSICGG LMGTFKAHDG EYFLEPIMKA DGSEHDEDHN
KPHLIYRQEV KRNYFLPSHK PCEVSESQIK KTTLPFHNYS NVSEDLNIKE EIVLGYSSKN
VSLEHERSQI HSRKKRFLSY PRYVEVMVTA DAKMVHHHGQ NLQHYVLTLM SIVAAIYKDS
SIGNLINIVI VKLIIIHDEQ EGPVVSFNAA TTLRNFCLWQ QTQNVLDDAH PSHHDTAVLI
TRYGLAELGT LCDPLRSCSI SEENGLSAAF TIAHELGHVF NVPHDDSFKC KETGTKHQYH
VMAPTLNYHT SPWTWSKCSQ KYITEFLDTG HGECLLDKPN GRIYDLSLQL PGLMYDVNKQ
CELMFGPGSQ VCPYLKQCRR LWCTSAEGVH KGCRTQHMPL ADGTNCGPGM HCHHGLCVNK
EMETRPVDGE WGPWGPYSSC SRTCGGGIKS TTRLCNRPEP RNGGKYCVGR RMKFRSCNTD
SCPKGKQDFR EKQCSDFDGK HLNINGLSPN VRWLPKYSGI AIKDRCKLYC RVAGTTSFYQ
LKDRVADGTP CGTETNDICV QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCRTLAGVFN
SAHYGYNVVV KIPPGATNID ILQHSYSGKP EDDNYLALSD TQGNFLLNGN FVVSMSKKEI
NIQGAIFEYS GSNNSIERIN STDRLEEELV LQVLCVGNLY NPDVRYSFSI PTEEKSDLFT
WDPYGPWQDC TKMCQGLHRR KITCVRKSDH MVVSDQRCDH LPLPLLVTER CNTDCELRWH
ITGKSECSSL CGQGYKSLDI HCMKYSIHKG QTVPVDDRYC GDQLKPPTRE PCHGDCVLTR
WHYSEWSQCS RSCGGGEKSR ESYCMNNFGH RLADRECQGL PRVTIENCNE FSCPRWATSE
WSECLVTCGK GTKQRQVWCQ LNEDHLSDGF CDPSTKPESL RPCELHTCAS WQVGPWGSCS
VSCGRGSQAR YVSCRDAHDE IADESYCAHI PRPADISLCF SPCGEWQTGN WSPVSIFIPC
GLLSSCGHGK TTRQVLCINY HQPINENYCD PEVRPLIEQE CNLAACPPTY DHFPSSSEQP
SHFRGRNFPL THKPEDNQNQ GFHPSIRGNQ WRTGPWGSCS SSCAAGVQRR VVVCQDENGQ
SASYCDAASR PPELKHCDLG PCPRWSYGSW GECTQTCGGG IKSRFVICQF PNGQISREQN
CDLVNKPPSV VQCHMHACPD DVSWHRGPWK SCSASCGKGL KYREVLCVDR FHGKLEEKYC
SHLRKPRTHK ACRSARCPSW KANRWKQCSV TCGSGLQQRD VYCRLRGVGR VAEEKCDRST
RPYFQRQCWH QDCIQYQWVA GGWLDCSTSC KQRETRRQVR CVDARNLQVN ESFCDPLTRP
LSIKRCGNPP CKYIVVTGDS SQVRQRKDVE NFRSWKIQLG LKSDPVETGS EFEHGSK
//
