ID A0A0D9RNG0_CHLSB Unreviewed; 1211 AA.
AC A0A0D9RNG0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 19 {ECO:0000313|Ensembl:ENSCSAP00000010149.1};
GN Name=ADAMTS19 {ECO:0000313|Ensembl:ENSCSAP00000010149.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000010149.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000010149.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000010149.1}
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 EMBL; AQIB01044061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01044062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01044063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01044064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9RNG0; -.
DR STRING; 60711.ENSCSAP00000010149; -.
DR Ensembl; ENSCSAT00000012103.1; ENSCSAP00000010149.1; ENSCSAG00000014053.1.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000161018; -.
DR OMA; QHAEPDG; -.
DR Proteomes; UP000029965; Chromosome 23.
DR Bgee; ENSCSAG00000014053; Expressed in adrenal cortex and 2 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; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF197; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 19; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 5.
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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
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|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1211
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002345730"
FT DOMAIN 329..549
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1164..1203
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 53..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 487
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 298
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 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 434
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 486
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 490
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 496
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 544
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 405..470
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 445..452
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 464..544
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 503..528
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 573..597
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 584..605
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 592..624
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 618..629
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 649..684
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 653..689
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 664..674
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1211 AA; 134479 MW; E118BFC834393C5A CRC64;
KNREMRLTHI CCCCLLYQLG FLSNGIVSEL QFAPDREEWE VVFPALWRRE PVDTAGGSGG
SADPGWVRGV GGGGSARAQA AGSSREVRSV APVPLEDPVE DRSESRLRPP PPSEGEEDEE
LESQELPRGS SGVAALSPGA PASWHPPPPP QPPPSPPPAQ PAEPDGDEVL LRIPAFSRDL
YLLLRRDGRF LAPRFAVEQR PNPGPGPTGA ASAPHPPAPP DAGCFYTGAV LRHPGSLASF
STCGGGLMGF IQLNEDFIFI EPLNDTMAIT GHPHRVYRQK RSMEEKVTEK SALHSHYCGI
ISDKGRPRSR KIAESGRGKR YSYKLPQEYN IETVVVADPA MVSYHGADAA RRFILTILNM
VFNLFQHKSL GVQVNLRVIK LILLHETPPD LYIGHHGEKM LESFCKWQHE EFGKKNDIHL
EMSTSWGEDM TSVDAAILIT RKDFCVHKDE PCDTVGIAYL SGMCSEKRKC IIAEDNGLNL
AFTIAHEMGH NMGINHDNDH PSCADGLHIM SGEWIKGQNL GDVSWSRCSK EDLERFLRSK
ASNCLQQTNP QSVNSVMVPS KLPGMTYTAD EQCQILFGPL ASFCQEMQHV ICTGLWCKVE
GEKECKTKLD PPMDGTDCDP GKWCKAGECT SRTSAPEHLA GEWSLWSPCS RTCSAGISSR
ERKCPGLGSE ARDCNGPRKQ YRICENPPCP AGLPGFRDWQ CQAYSVRTSS PKHVLQWQAV
LDEEKPCALF CSPIGKEQPI LLSEKVMDGT SCGYQGLDIC ANGRCQKVGC DGLLGSLARE
DHCGVCNGNG KSCKIIKGDF NHTRGAGYVE VLVIPAGARR IKVVEEKPAH SYLALRDAGK
QSINSDWKIE HSGAFHLAGT TVHYVRRGLW EKISAKGPTT APLHLLVLLF QDQNYGLHYE
YTIPSDPLPE NQSSKAPEPL FMWTHTSWED CDATCGGGER KTTVSCTKIM SKNISIVDNK
KCKYLTKPEP QIRKCNEQPC QTRWMMTEWT PCSRTCGKGM QSRQVACTQQ LSNGTLIRAR
ERDCIGPKPA SAQRCEGQDC MTVWEAGVWS ECSVKCGKGV RHRTVRCTNP RKKCVLSTRP
REAEDCEDYS KCYVWRMGDW SKCSITCGKG MQSRVIQCMH KITGRHGNEC FSSEKPAAYR
PCHLQPCNEK INVNTITSPR LAALTFKCLG DQWPVYCRVI REKNLCQDMR WYQRCCETCR
DFYAQKLQQK S
//
