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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 19

Gene

Adamts19

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi297Zinc; in inhibited formBy similarity1
Metal bindingi485Zinc; catalyticBy similarity1
Active sitei486PROSITE-ProRule annotation1
Metal bindingi489Zinc; catalyticBy similarity1
Metal bindingi495Zinc; catalyticBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.029.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 19 (EC:3.4.24.-)
Short name:
ADAM-TS 19
Short name:
ADAM-TS19
Short name:
ADAMTS-19
Gene namesi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:2442875. Adamts19.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
PropeptideiPRO_000002920431 – 319By similarityAdd BLAST289
ChainiPRO_0000029205320 – 1210A disintegrin and metalloproteinase with thrombospondin motifs 19Add BLAST891

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi54N-linked (GlcNAc...)Sequence analysis1
Glycosylationi263N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi404 ↔ 469By similarity
Disulfide bondi444 ↔ 451By similarity
Disulfide bondi463 ↔ 543By similarity
Disulfide bondi502 ↔ 527By similarity
Disulfide bondi572 ↔ 596By similarity
Disulfide bondi583 ↔ 604By similarity
Disulfide bondi591 ↔ 623By similarity
Disulfide bondi617 ↔ 628By similarity
Disulfide bondi648 ↔ 683By similarity
Disulfide bondi652 ↔ 688By similarity
Disulfide bondi663 ↔ 673By similarity
Glycosylationi800N-linked (GlcNAc...)Sequence analysis1
Glycosylationi910N-linked (GlcNAc...)Sequence analysis1
Glycosylationi931N-linked (GlcNAc...)Sequence analysis1
Glycosylationi952N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi991 ↔ 1034By similarity
Disulfide bondi995 ↔ 1039By similarity
Disulfide bondi1006 ↔ 1023By similarity
Glycosylationi1012N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP59509.
PaxDbiP59509.
PRIDEiP59509.

PTM databases

iPTMnetiP59509.
PhosphoSitePlusiP59509.

Expressioni

Tissue specificityi

Expressed predominantly in fetal ovary, low levels of expression is also detected in kidney, heart, skeletal muscle, lung and testis.

Developmental stagei

Expression is strongest in anterior and ventral regions of the ovary at 12.5 and 13.5 dpc before becoming more uniform.

Gene expression databases

BgeeiENSMUSG00000053441.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050535.

Structurei

3D structure databases

ProteinModelPortaliP59509.
SMRiP59509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini328 – 548Peptidase M12BPROSITE-ProRule annotationAdd BLAST221
Domaini549 – 636DisintegrinAdd BLAST88
Domaini637 – 689TSP type-1 1PROSITE-ProRule annotationAdd BLAST53
Domaini918 – 978TSP type-1 2PROSITE-ProRule annotationAdd BLAST61
Domaini979 – 1040TSP type-1 3PROSITE-ProRule annotationAdd BLAST62
Domaini1042 – 1086TSP type-1 4PROSITE-ProRule annotationAdd BLAST45
Domaini1090 – 1147TSP type-1 5PROSITE-ProRule annotationAdd BLAST58
Domaini1163 – 1202PLACPROSITE-ProRule annotationAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni794 – 917SpacerAdd BLAST124

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi295 – 302Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi690 – 793Cys-richAdd BLAST104

Domaini

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 5 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG050621.
InParanoidiP59509.
KOiK08633.
OMAiKECKTKL.
OrthoDBiEOG091G14M8.
PhylomeDBiP59509.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P59509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPEMRLTRI CCCCCLLYQL GFLSHGTTSG LQLTPDLEEW EVVFPALWRR
60 70 80 90 100
ESLNATGLSG GSSDPGSGRS SGGGGRGQAS GSSREVRSVA RAPQEEATRG
110 120 130 140 150
QSEPWFGSPL EPGAEDEEEL ESQELPRGSS GDTALSSGTP ASWQPPLPPQ
160 170 180 190 200
RPSSPPPAQQ EEPSAEEVLL RIPALSRDLY LLLRRDGRFL AQRFAVEQWP
210 220 230 240 250
KPGPDPTRAT ADPGSSLLPD ASCFYTGTVL RHPGSLASFS TCGGGLMGFI
260 270 280 290 300
QLNEDFLFIE PFNDTMAIIG HPHRLYRQKR STEEKVTENS AVHRHHCGVI
310 320 330 340 350
SDKGRPRSKK IADNRREKRY SYKLSQEYNI ETVVVADPAM VSYHGADAAR
360 370 380 390 400
RFILTILNMV FNLFQHKSLG VQVNLRVLKL ILLHETPADL YIGHHGEKML
410 420 430 440 450
ESFCKWQHEE FGRRNDVHLE MSTSWGEDIA AVDAAILITR KDFCVHKDEP
460 470 480 490 500
CDTVGIAYLN GMCSEKRKCI IAEDNGLNLA FTIAHEMGHN MGINHDNDHP
510 520 530 540 550
SCADGLHIMS GEWIKGQNLG DVSWSRCSKE DLERFLRSKA SSCLLHTDPQ
560 570 580 590 600
SLSSVLVPSK LPGMAYTADE QCQILFGPLA SFCQEMQHVI CTGLWCKVEG
610 620 630 640 650
EAECRTKLDP PMDGTDCDPG KWCKAGECTR RTPAPEHLAG EWSPWSSCSR
660 670 680 690 700
SCSSGVSSRE RKCPGLGSEA RDCNGPRKQY RICENPPCPA GLPGFRDWQC
710 720 730 740 750
QAYSVRTSYP KHALQWQAVF DEEKPCALFC SPVGKEQPVL LSEKVMDGTS
760 770 780 790 800
CGYQGLDICA NGRCQKAGCD GLLGSLARED HCGVCNGNGK SCKVIKGDFN
810 820 830 840 850
HTRGAGYVEV LVIPAGARRI KVVEEKPAHS FLALRDASKQ SINSDWKIEH
860 870 880 890 900
SGAFSLAGTT VHYLRRGLWE KISAKGPTTT PLHLLVLLFQ DQNYGLHYEY
910 920 930 940 950
TVPSDPLPDN QSSKEPGPLF MWTHAGWGDC NATCGGGERK TMVSCTKIMS
960 970 980 990 1000
KNISLVDNKK CKDLTKPEPQ IRKCNEQPCQ TRWMMTEWTT CSRTCGKGVQ
1010 1020 1030 1040 1050
SRQVACTQQL ENGTLIRAWE RDCLGPKPAT VQRCEGQDCM TVWEAGVWSE
1060 1070 1080 1090 1100
CSVKCGKGVR HRTVRCTNPR KKCVLSTRPR EAEDCEDYSK CYVWRVGDWS
1110 1120 1130 1140 1150
KCSITCGKGM QSRVIQCMHK ITGRHGNECF SSEKPAAYRP CHLQPCNEKI
1160 1170 1180 1190 1200
NVNTITSPRL AALTFKCLGD QWPVYCRVIR EKNLCQDMRW YQRCCETCRD
1210
FYAQKLQQKS
Length:1,210
Mass (Da):134,561
Last modified:April 4, 2003 - v1
Checksum:i0AB812ABAB4BB7A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY135183 mRNA. Translation: AAN10155.1.
CCDSiCCDS29266.1.
RefSeqiNP_780715.1. NM_175506.4.
UniGeneiMm.71963.

Genome annotation databases

EnsembliENSMUST00000052907; ENSMUSP00000050535; ENSMUSG00000053441.
GeneIDi240322.
KEGGimmu:240322.
UCSCiuc008ezs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY135183 mRNA. Translation: AAN10155.1.
CCDSiCCDS29266.1.
RefSeqiNP_780715.1. NM_175506.4.
UniGeneiMm.71963.

3D structure databases

ProteinModelPortaliP59509.
SMRiP59509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050535.

Protein family/group databases

MEROPSiM12.029.

PTM databases

iPTMnetiP59509.
PhosphoSitePlusiP59509.

Proteomic databases

MaxQBiP59509.
PaxDbiP59509.
PRIDEiP59509.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052907; ENSMUSP00000050535; ENSMUSG00000053441.
GeneIDi240322.
KEGGimmu:240322.
UCSCiuc008ezs.1. mouse.

Organism-specific databases

CTDi171019.
MGIiMGI:2442875. Adamts19.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG050621.
InParanoidiP59509.
KOiK08633.
OMAiKECKTKL.
OrthoDBiEOG091G14M8.
PhylomeDBiP59509.
TreeFamiTF313537.

Miscellaneous databases

PROiP59509.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000053441.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATS19_MOUSE
AccessioniPrimary (citable) accession number: P59509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: April 4, 2003
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

By homology with the human sequence, it is uncertain whether Met-1 or Met-5 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.