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Q8BNJ2

- ATS4_MOUSE

UniProt

Q8BNJ2 - ATS4_MOUSE

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene
Adamts4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site By similarity.

Catalytic activityi

Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi190 – 1901Zinc; in inhibited form By similarity
Metal bindingi357 – 3571Zinc; catalytic By similarity
Active sitei358 – 3581 By similarity
Metal bindingi361 – 3611Zinc; catalytic By similarity
Metal bindingi367 – 3671Zinc; catalytic By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: MGI
  2. metallopeptidase activity Source: MGI
  3. protein binding Source: MGI
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. defense response to bacterium Source: MGI
  2. proteolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM12.221.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
Short name:
ADAM-TS 4
Short name:
ADAM-TS4
Short name:
ADAMTS-4
Alternative name(s):
Aggrecanase-1
Gene namesi
Name:Adamts4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1339949. Adamts4.

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4949 Reviewed predictionAdd
BLAST
Propeptidei50 – 208159 By similarityPRO_0000029166Add
BLAST
Chaini209 – 833625A disintegrin and metalloproteinase with thrombospondin motifs 4PRO_0000029167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi289 ↔ 341 By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi318 ↔ 323 By similarity
Disulfide bondi335 ↔ 419 By similarity
Disulfide bondi373 ↔ 403 By similarity
Disulfide bondi445 ↔ 468 By similarity
Disulfide bondi456 ↔ 478 By similarity
Disulfide bondi463 ↔ 497 By similarity
Disulfide bondi491 ↔ 502 By similarity
Disulfide bondi528 ↔ 565 By similarity
Disulfide bondi532 ↔ 570 By similarity
Disulfide bondi543 ↔ 555 By similarity

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.

Keywords - PTMi

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

Proteomic databases

PaxDbiQ8BNJ2.
PRIDEiQ8BNJ2.

PTM databases

PhosphoSiteiQ8BNJ2.

Expressioni

Gene expression databases

ArrayExpressiQ8BNJ2.
BgeeiQ8BNJ2.
GenevestigatoriQ8BNJ2.

Interactioni

Subunit structurei

Interacts with SRPX2 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ8BNJ2.
SMRiQ8BNJ2. Positions 211-801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 424211Peptidase M12BAdd
BLAST
Domaini433 – 51583DisintegrinAdd
BLAST
Domaini516 – 57156TSP type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni682 – 833152SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi188 – 1958Cysteine switch By similarity

Domaini

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.
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.
Contains 1 TSP type-1 domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG271890.
GeneTreeiENSGT00650000092972.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ8BNJ2.
KOiK07764.
OrthoDBiEOG7WDN1M.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BNJ2-1 [UniParc]FASTAAdd to Basket

« Hide

MSQMGLHPRR GLTGHWLQRF QPCLPLHTVQ WRRLLLLAFL LSLAWPASPL    50
PREEEIVFPE KLNGSSILPG SGVPARLLYR LPAFGEMLLL ELEQDPGVQV 100
EGLTVQYLGQ APEMLGGAEP GTYLTGTING DPESVASLHW DGGALLGVLQ 150
YRGAELHLQP LEGGALNSAG GPGAHILRRK SPASSQGPMC TVKAPSGSPS 200
PISRRTKRFA SLSRFVETLV VADDKMAAFH GTGLKRYLLT VMAAAAKAFK 250
HPSIRNPVNL VVTRLVILGS GQEGPQVGPS AAQTLRSFCT WQRGLNTPND 300
SDPDHFDTAI LFTRQDLCGV STCDTLGMAD VGTVCDPARS CAIVEDDGLQ 350
SAFTAAHELG HVFNMLHDNS KPCTNLNGQG GSSRHVMAPV MAHVDPEEPW 400
SPCSARFITD FLDNGYGHCL LDKPEAPLHL PATFPGKDYD ADRQCQLTFG 450
PDSSHCPQLP PPCAALWCSG HLNGHAMCQT KHSPWADGTP CGSSQACMGG 500
RCLHVDQLKD FNVPQAGGWG PWGPWGDCSR TCGGGVQFSS RDCTRPVPRN 550
GGKYCEGRRT RFRSCNTENC PHGSALTFRE EQCAAYNHRT DLFKSFPGPM 600
DWVPRYTGVA PRDQCKLTCQ ARALGYYYVL EPRVADGTPC SPDTSSVCVQ 650
GRCIHAGCDR IIGSKKKFDK CMVCGGDGSR CSKQSGSFKK FRYGYSDVVT 700
IPAGATHILV RQQGGSGLKS IYLALKLSDG SYALNGEYTL MPSPTDVVLP 750
GAVSLRYSGA TAASETLSGH GPLAQPLTLQ VLVAGNPQNA RLRYSFFVPR 800
PVPSTPRPPP QDWLQRRAEI LKILRKRPWA GRK 833
Length:833
Mass (Da):90,070
Last modified:May 10, 2005 - v2
Checksum:i6512B9ED2617F3A4
GO

Sequence cautioni

The sequence BAC38944.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181Q → R in AAH27773. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK083534 mRNA. Translation: BAC38944.1. Different initiation.
BC027773 mRNA. Translation: AAH27773.1.
RefSeqiNP_766433.1. NM_172845.2.
UniGeneiMm.491147.

Genome annotation databases

EnsembliENSMUST00000111315; ENSMUSP00000106947; ENSMUSG00000006403.
GeneIDi240913.
KEGGimmu:240913.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK083534 mRNA. Translation: BAC38944.1 . Different initiation.
BC027773 mRNA. Translation: AAH27773.1 .
RefSeqi NP_766433.1. NM_172845.2.
UniGenei Mm.491147.

3D structure databases

ProteinModelPortali Q8BNJ2.
SMRi Q8BNJ2. Positions 211-801.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M12.221.

PTM databases

PhosphoSitei Q8BNJ2.

Proteomic databases

PaxDbi Q8BNJ2.
PRIDEi Q8BNJ2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000111315 ; ENSMUSP00000106947 ; ENSMUSG00000006403 .
GeneIDi 240913.
KEGGi mmu:240913.

Organism-specific databases

CTDi 9507.
MGIi MGI:1339949. Adamts4.

Phylogenomic databases

eggNOGi NOG271890.
GeneTreei ENSGT00650000092972.
HOGENOMi HOG000004799.
HOVERGENi HBG004313.
InParanoidi Q8BNJ2.
KOi K07764.
OrthoDBi EOG7WDN1M.

Enzyme and pathway databases

Reactomei REACT_199052. Degradation of the extracellular matrix.

Miscellaneous databases

NextBioi 384802.
PROi Q8BNJ2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BNJ2.
Bgeei Q8BNJ2.
Genevestigatori Q8BNJ2.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiATS4_MOUSE
AccessioniPrimary (citable) accession number: Q8BNJ2
Secondary accession number(s): Q8K384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: September 3, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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