ID A0A1X7SBR9_HUMAN Unreviewed; 1213 AA.
AC A0A1X7SBR9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 19 {ECO:0000313|Ensembl:ENSP00000274487.5};
GN Name=ADAMTS19 {ECO:0000313|Ensembl:ENSP00000274487.5};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000274487.5, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000274487.5, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2] {ECO:0000313|Ensembl:ENSP00000274487.5}
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; AC008425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_598377.4; NM_133638.4.
DR AlphaFoldDB; A0A1X7SBR9; -.
DR SMR; A0A1X7SBR9; -.
DR MassIVE; A0A1X7SBR9; -.
DR Antibodypedia; 52899; 129 antibodies from 21 providers.
DR DNASU; 171019; -.
DR Ensembl; ENST00000274487.9; ENSP00000274487.5; ENSG00000145808.10.
DR GeneID; 171019; -.
DR KEGG; hsa:171019; -.
DR MANE-Select; ENST00000274487.9; ENSP00000274487.5; NM_133638.6; NP_598377.4.
DR CTD; 171019; -.
DR HGNC; HGNC:17111; ADAMTS19.
DR VEuPathDB; HostDB:ENSG00000145808; -.
DR GeneTree; ENSGT00940000161018; -.
DR OMA; QHAEPDG; -.
DR OrthoDB; 2910701at2759; -.
DR ChiTaRS; ADAMTS19; human.
DR GenomeRNAi; 171019; -.
DR Proteomes; UP000005640; Chromosome 5.
DR Bgee; ENSG00000145808; Expressed in adrenal tissue and 97 other cell types or tissues.
DR ExpressionAtlas; A0A1X7SBR9; 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; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|EPD:A0A1X7SBR9,
KW ECO:0007829|PeptideAtlas:A0A1X7SBR9};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
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..1213
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010852630"
FT DOMAIN 331..551
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1166..1205
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 55..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..221
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 COMPBIAS 143..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 300
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 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 488
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 492
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 498
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 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 407..472
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 447..454
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 466..546
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 505..530
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 575..599
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 586..607
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 594..626
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 620..631
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 651..686
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 655..691
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 666..676
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1213 AA; 134764 MW; A274B4147302F03F CRC64;
MGKNREMRLT HICCCCLLYQ LGFLSNGIVS ELQFAPDREE WEVVFPALWR REPVDPAGGS
GGSADPGWVR GVGGGGSARA QAAGSSREVR SVAPVPLEEP VEGRSESRLR PPPPSEGEED
EELESQELPR GSSGAAALSP GAPASWQPPP PPQPPPSPPP AQHAEPDGDE VLLRIPAFSR
DLYLLLRRDG RFLAPRFAVE QRPNPGPGPT GAASAPQPPA PPDAGCFYTG AVLRHPGSLA
SFSTCGGGLM GFIQLNEDFI FIEPLNDTMA ITGHPHRVYR QKRSMEEKVT EKSALHSHYC
GIISDKGRPR SRKIAESGRG KRYSYKLPQE YNIETVVVAD PAMVSYHGAD AARRFILTIL
NMVFNLFQHK SLSVQVNLRV IKLILLHETP PELYIGHHGE KMLESFCKWQ HEEFGKKNDI
HLEMSTNWGE DMTSVDAAIL ITRKDFCVHK DEPCDTVGIA YLSGMCSEKR KCIIAEDNGL
NLAFTIAHEM GHNMGINHDN DHPSCADGLH IMSGEWIKGQ NLGDVSWSRC SKEDLERFLR
SKASNCLLQT NPQSVNSVMV PSKLPGMTYT ADEQCQILFG PLASFCQEMQ HVICTGLWCK
VEGEKECRTK LDPPMDGTDC DLGKWCKAGE CTSRTSAPEH LAGEWSLWSP CSRTCSAGIS
SRERKCPGLD SEARDCNGPR KQYRICENPP CPAGLPGFRD WQCQAYSVRT SSPKHILQWQ
AVLDEEKPCA LFCSPVGKEQ PILLSEKVMD GTSCGYQGLD ICANGRCQKV GCDGLLGSLA
REDHCGVCNG NGKSCKIIKG DFNHTRGAGY VEVLVIPAGA RRIKVVEEKP AHSYLALRDA
GKQSINSDWK IEHSGAFNLA GTTVHYVRRG LWEKISAKGP TTAPLHLLVL LFQDQNYGLH
YEYTIPSDPL PENQSSKAPE PLFMWTHTSW EDCDATCGGG ERKTTVSCTK IMSKNISIVD
NEKCKYLTKP EPQIRKCNEQ PCQTRWMMTE WTPCSRTCGK GMQSRQVACT QQLSNGTLIR
ARERDCIGPK PASAQRCEGQ DCMTVWEAGV WSECSVKCGK GIRHRTVRCT NPRKKCVLST
RPREAEDCED YSKCYVWRMG DWSKCSITCG KGMQSRVIQC MHKITGRHGN ECFSSEKPAA
YRPCHLQPCN EKINVNTITS PRLAALTFKC LGDQWPVYCR VIREKNLCQD MRWYQRCCET
CRDFYAQKLQ QKS
//
