ATS19_MOUSE
ID ATS19_MOUSE Reviewed; 1210 AA.
AC P59509;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 19;
DE Short=ADAM-TS 19;
DE Short=ADAM-TS19;
DE Short=ADAMTS-19;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Adamts19;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary;
RX PubMed=12617826; DOI=10.1016/s1567-133x(02)00022-4;
RA Menke D.B., Page D.C.;
RT "Sexually dimorphic gene expression in the developing mouse gonad.";
RL Gene Expr. Patterns 2:359-367(2002).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in fetal ovary, low levels
CC of expression is also detected in kidney, heart, skeletal muscle, lung
CC and testis.
CC -!- DEVELOPMENTAL STAGE: Expression is strongest in anterior and ventral
CC regions of the ovary at 12.5 and 13.5 dpc before becoming more uniform.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
CC threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-
CC G of the TSP type-1 repeat domains where C1 and C2 are the first and
CC second cysteine residue of the repeat, respectively. Fucosylated
CC repeats can then be further glycosylated by the addition of a beta-1,3-
CC glucose residue by the glucosyltransferase, B3GALTL. Fucosylation
CC mediates the efficient secretion of ADAMTS family members. Can also be
CC C-glycosylated with one or two mannose molecules on tryptophan residues
CC within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated.
CC These other glycosylations can also facilitate secretion (By
CC similarity). {ECO:0000250}.
CC -!- CAUTION: By homology with the human sequence, it is uncertain whether
CC Met-1 or Met-5 is the initiator. {ECO:0000305}.
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DR EMBL; AY135183; AAN10155.1; -; mRNA.
DR CCDS; CCDS29266.1; -.
DR RefSeq; NP_780715.1; NM_175506.4.
DR AlphaFoldDB; P59509; -.
DR SMR; P59509; -.
DR BioGRID; 232190; 2.
DR STRING; 10090.ENSMUSP00000050535; -.
DR MEROPS; M12.029; -.
DR GlyGen; P59509; 7 sites.
DR iPTMnet; P59509; -.
DR PhosphoSitePlus; P59509; -.
DR jPOST; P59509; -.
DR MaxQB; P59509; -.
DR PaxDb; P59509; -.
DR PRIDE; P59509; -.
DR ProteomicsDB; 277225; -.
DR Antibodypedia; 52899; 129 antibodies from 21 providers.
DR DNASU; 240322; -.
DR Ensembl; ENSMUST00000052907; ENSMUSP00000050535; ENSMUSG00000053441.
DR GeneID; 240322; -.
DR KEGG; mmu:240322; -.
DR UCSC; uc008ezs.1; mouse.
DR CTD; 171019; -.
DR MGI; MGI:2442875; Adamts19.
DR VEuPathDB; HostDB:ENSMUSG00000053441; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000161018; -.
DR HOGENOM; CLU_000660_8_1_1; -.
DR InParanoid; P59509; -.
DR OMA; SAPHSHY; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; P59509; -.
DR TreeFam; TF313537; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 240322; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Adamts19; mouse.
DR PRO; PR:P59509; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P59509; protein.
DR Bgee; ENSMUSG00000053441; Expressed in mesentery of stomach and 63 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..319
FT /evidence="ECO:0000250"
FT /id="PRO_0000029204"
FT CHAIN 320..1210
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 19"
FT /id="PRO_0000029205"
FT DOMAIN 328..548
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 549..636
FT /note="Disintegrin"
FT DOMAIN 637..689
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 918..978
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 979..1040
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1042..1086
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1090..1147
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1163..1202
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 55..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..917
FT /note="Spacer"
FT MOTIF 295..302
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1012
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 404..469
FT /evidence="ECO:0000250"
FT DISULFID 444..451
FT /evidence="ECO:0000250"
FT DISULFID 463..543
FT /evidence="ECO:0000250"
FT DISULFID 502..527
FT /evidence="ECO:0000250"
FT DISULFID 572..596
FT /evidence="ECO:0000250"
FT DISULFID 583..604
FT /evidence="ECO:0000250"
FT DISULFID 591..623
FT /evidence="ECO:0000250"
FT DISULFID 617..628
FT /evidence="ECO:0000250"
FT DISULFID 648..683
FT /evidence="ECO:0000250"
FT DISULFID 652..688
FT /evidence="ECO:0000250"
FT DISULFID 663..673
FT /evidence="ECO:0000250"
FT DISULFID 991..1034
FT /evidence="ECO:0000250"
FT DISULFID 995..1039
FT /evidence="ECO:0000250"
FT DISULFID 1006..1023
FT /evidence="ECO:0000250"
SQ SEQUENCE 1210 AA; 134561 MW; 0AB812ABAB4BB7A2 CRC64;
MGPEMRLTRI CCCCCLLYQL GFLSHGTTSG LQLTPDLEEW EVVFPALWRR ESLNATGLSG
GSSDPGSGRS SGGGGRGQAS GSSREVRSVA RAPQEEATRG QSEPWFGSPL EPGAEDEEEL
ESQELPRGSS GDTALSSGTP ASWQPPLPPQ RPSSPPPAQQ EEPSAEEVLL RIPALSRDLY
LLLRRDGRFL AQRFAVEQWP KPGPDPTRAT ADPGSSLLPD ASCFYTGTVL RHPGSLASFS
TCGGGLMGFI QLNEDFLFIE PFNDTMAIIG HPHRLYRQKR STEEKVTENS AVHRHHCGVI
SDKGRPRSKK IADNRREKRY SYKLSQEYNI ETVVVADPAM VSYHGADAAR RFILTILNMV
FNLFQHKSLG VQVNLRVLKL ILLHETPADL YIGHHGEKML ESFCKWQHEE FGRRNDVHLE
MSTSWGEDIA AVDAAILITR KDFCVHKDEP CDTVGIAYLN GMCSEKRKCI IAEDNGLNLA
FTIAHEMGHN MGINHDNDHP SCADGLHIMS GEWIKGQNLG DVSWSRCSKE DLERFLRSKA
SSCLLHTDPQ SLSSVLVPSK LPGMAYTADE QCQILFGPLA SFCQEMQHVI CTGLWCKVEG
EAECRTKLDP PMDGTDCDPG KWCKAGECTR RTPAPEHLAG EWSPWSSCSR SCSSGVSSRE
RKCPGLGSEA RDCNGPRKQY RICENPPCPA GLPGFRDWQC QAYSVRTSYP KHALQWQAVF
DEEKPCALFC SPVGKEQPVL LSEKVMDGTS CGYQGLDICA NGRCQKAGCD GLLGSLARED
HCGVCNGNGK SCKVIKGDFN HTRGAGYVEV LVIPAGARRI KVVEEKPAHS FLALRDASKQ
SINSDWKIEH SGAFSLAGTT VHYLRRGLWE KISAKGPTTT PLHLLVLLFQ DQNYGLHYEY
TVPSDPLPDN QSSKEPGPLF MWTHAGWGDC NATCGGGERK TMVSCTKIMS KNISLVDNKK
CKDLTKPEPQ IRKCNEQPCQ TRWMMTEWTT CSRTCGKGVQ SRQVACTQQL ENGTLIRAWE
RDCLGPKPAT VQRCEGQDCM TVWEAGVWSE CSVKCGKGVR HRTVRCTNPR KKCVLSTRPR
EAEDCEDYSK CYVWRVGDWS KCSITCGKGM QSRVIQCMHK ITGRHGNECF SSEKPAAYRP
CHLQPCNEKI NVNTITSPRL AALTFKCLGD QWPVYCRVIR EKNLCQDMRW YQRCCETCRD
FYAQKLQQKS
