ID A0A452F7D6_CAPHI Unreviewed; 1212 AA.
AC A0A452F7D6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 19 {ECO:0000313|Ensembl:ENSCHIP00000020065.1};
GN Name=ADAMTS19 {ECO:0000313|Ensembl:ENSCHIP00000020065.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000020065.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000020065.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000020065.1}
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 EMBL; LWLT01000008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452F7D6; -.
DR STRING; 9925.ENSCHIP00000020065; -.
DR Ensembl; ENSCHIT00000027893.1; ENSCHIP00000020065.1; ENSCHIG00000018817.1.
DR GeneTree; ENSGT00940000161018; -.
DR Proteomes; UP000291000; Chromosome 7.
DR Bgee; ENSCHIG00000018817; Expressed in uterus and 13 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; 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; 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 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:UP000291000};
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}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1212
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019271515"
FT DOMAIN 323..543
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1165..1204
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 53..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 481
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 292
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 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 480
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 484
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 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 399..464
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 439..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 458..538
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 497..522
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 567..591
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 578..599
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 586..618
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 612..623
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 643..678
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 647..683
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 658..668
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1212 AA; 134476 MW; 524840C0C661294F CRC64;
MGREMRLTHI CCCCLLYQLG VLSNGVVAGL QFASDREEWE VVFPALWRRE PVDSAGGSGG
SADPGWARGA TGGGGVRAPA ASSSREVRSV APAPPQEPVE GGSEPRPRPS PPGGEEDEEL
ESHELPRGSS GAAALSPSAP ASWQPPPPSP PPAQPAEPDG EEVLLRIPAF SRDLYLLLRR
DGRFLAPRFA VEQRPSPGPG PTRAAAAPRP PAPPDAACFY TGAVLRQPGS LASFSTCGGG
LMGFIQLNED FIFIEPLNDT VAITGHPHRV YRRKRSMEEK VTEKSVPHSH YCGVISDKGR
PKSKKITESG RGKRYSYKLP QEYNIETVVV ADPAMVSYHG ADAARRFILT ILNMVFNLFQ
HKSLGVQVNL RVIKLILLHE TPADLYIGHH GEKMLESFCK WQHEEFGKKN DIHLEMSTSW
GEDMTSVDAA ILITRKDFCV HKDEPCDTVG IAYLSGMCSE KRKCIIAEDN GLNLAFTIAH
EMGHNMGINH DNDHPSCADG LHIMSGEWIK GQNLGDVSWS RCSKEDLERF LRSKASNCLL
QTNPHSVNSV MVPSKLPEMT YTADEQCQIL FGPLASFCQE MQHVICTGLW CKVEGEKECK
TKLDPPMDGT DCDIGKWCKA GECTSRTAAP GLAAGEWSTW SPCSRTCSSG ISSRERKCPG
LGSEARDCNG PRKQYRICEN PPCPAGLPGF RDWQCQAYSV RTSYPKHVLQ WHAVMDEEKP
CALFCSSVGK EQPILLSEKV LDGTSCGYQG LDVCANGRCQ KVGCDGLLGS LAREDHCGVC
NGNGKSCKII KGDFNHTRGA GDYFFSKLLI QTVFGDRNYV ELDLEITFLI VENFSLRDTE
KQSINSDWKI EHSGAFNIAG TTVHYVRRGL WEKISAKGPT TTPLHLLVLL FQDQNYGLHY
EYTIPSDPPP ENQSSKAPEP LFMWTHTGWE DCDATCGGGE RKTTVSCTKI MNKNISIVDN
KKCKYLTKPE PQIRKCNEQP CQTRWMMTEW TPCSRTCGKG MQSRQVACTQ QLSNGTLTRA
RERDCAGPKP ASAQRCEGQD CMTVWEAGVW SECSVKCGKG VRHRTVRCTN PRKKCVLSTR
PREAEDCEDY SKCYVWRMGD WSKCSVTCGK GMQSRVIQCM HKITGRHGNE CFSSEKPAAY
RPCHLQPCNE KINVNTITSP RLAALTFKCL GDQWPVYCRV IREKNLCQDM RWYQRCCETC
RDFYAQKLQQ KS
//
