ID A0A2K6MDL7_RHIBE Unreviewed; 1155 AA.
AC A0A2K6MDL7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 19 {ECO:0000313|Ensembl:ENSRBIP00000033893.1};
GN Name=ADAMTS19 {ECO:0000313|Ensembl:ENSRBIP00000033893.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000033893.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000033893.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000033893.1}
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 AlphaFoldDB; A0A2K6MDL7; -.
DR STRING; 61621.ENSRBIP00000033893; -.
DR Ensembl; ENSRBIT00000057876.1; ENSRBIP00000033893.1; ENSRBIG00000040676.1.
DR GeneTree; ENSGT00940000161018; -.
DR OMA; QHAEPDG; -.
DR Proteomes; UP000233180; Unplaced.
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 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; 3.
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; 1.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 3.
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: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:UP000233180};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1155
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014455233"
FT DOMAIN 318..527
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1108..1147
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 55..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 287
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 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 464
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 468
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 474
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 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 383..448
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 423..430
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 442..522
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 481..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 551..570
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 559..578
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 565..597
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 591..602
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 622..657
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 626..662
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 637..647
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1155 AA; 128090 MW; B243DC1980C08145 CRC64;
MGKNREMRLT HICCCCLLYQ LGFLSNGIVS ELQFAPDREE WEVVFPALWR REPVDTAGGS
GGSADPGWVR GVGGGGSARA QAAGSSREVR SVAPVPLEEP VEGRSESRLR PPPPSEGEED
EELESQELPR GSSGAAALSP AAPSPPPAQH AEPDGDEVLL RIPAFSRDLY LLLRRDGRFL
APRFAVEQRP NPGPGPTGAA SAPQPPAPPD AGCFYTGAVL RHPGSLASFS TCGGGLMGFI
QLNEDFIFIE PLNDTMAITG HPHRVYRQKR SMEEKVTEKS ALHSHYCGII SDKGRPRSRK
IAESGRGKRY SYKLPQEYNI ETVVVADPAM VSYHGADAAR RFILTILNMV GQSPGVIKPY
FCSMKTPNLY IGHHGEKMLE SFCKWQHEEF GKKNDIHLEM STSWGEDMNS VDAAILITRK
DFCVHKDEPC DTVGIAYLSG MCSEKRKCII AEDNGLNLAF TIAHEMGHNM GINHDNDHPS
CADGLHIMSG EWIKGQNLGD VSWSRCSKEE LERFLRSKAS NCLLQTNPQS VNSVMVPSKL
PGMTYTADEQ CQILLVCLCF QHVICTGLWC KVEGEKECKT KLDPPMDGTD CDPGKWCKAG
ECTSRTSAPE HLAGEWSLWS PCSRTCSAGI SSRERKCPGL GSEARDCNGP RKQYRICENP
PCPAGLPGFR DWQCQAYSVR TSSPKHVLQW QAVLDEEKPC ALFCSPVGKE QPILLSEKVM
DGTSCGYQGL DICANGRCQK VGCDGLLGSL AREDHCGVCN GNGKSCKIIK GDFNHTRGAG
YVEVLVIPAG ARRIKVVEEK PAHSYLALRD AGKQSINSDW KIEHSGAFNL AGTTVHYVRR
GLWEKISAKG PTTAPLHLLV LLFQDQNYGL HYEYTIPSDP LPENQSSKAP EPLFMWTHTS
WEDCDATCGG GEGFLNMYLS KTSQNISIVD NKKCKYLTKP EPQIRKCNEQ PCQTRRLRQE
NACSELRSGH STPAWSIIYI SYSPTLSKTS DVIFQCSVKC GKGVRHRTVR CTNPRKKCVL
STRPREAEDC EDYSKCYVWR MGDWSKCSIT CGKGMQSRVI QCMHKITGRH GNECFSSEKP
AAYRPCHLQP CNEKINVNTI TSPRLAALTF KCLGDQWPVY CRVIREKNLC QDMRWYQRCC
ETCRDFYAQK LQQKS
//
