ATS10_MOUSE
ID ATS10_MOUSE Reviewed; 1104 AA.
AC P58459; Q497H1; Q78TI1; Q8CG28;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 10;
DE Short=ADAM-TS 10;
DE Short=ADAM-TS10;
DE Short=ADAMTS-10;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Adamts10;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA Nagaraja R.;
RT "Gene content of the 750-kb critical region for mouse embryonic ectoderm
RT lethal tcl-w5.";
RL Mamm. Genome 15:265-276(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Czech II; TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 655-1104 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15355968; DOI=10.1074/jbc.m409036200;
RA Somerville R.P.T., Jungers K.A., Apte S.S.;
RT "Discovery and characterization of a novel, widely expressed
RT metalloprotease, ADAMTS10, and its proteolytic activation.";
RL J. Biol. Chem. 279:51208-51217(2004).
CC -!- FUNCTION: Metalloprotease that participate in microfibrils assembly.
CC Microfibrils are extracellular matrix components occurring
CC independently or along with elastin in the formation of elastic tissues
CC (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with FBN1; this interaction promotes microfibrils
CC assembly. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P58459-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58459-2; Sequence=VSP_026109, VSP_026110;
CC Name=3;
CC IsoId=P58459-3; Sequence=VSP_026108, VSP_026111, VSP_026112;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues.
CC {ECO:0000269|PubMed:15355968}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed throughout embryo development.
CC Widespread expression in embryo until 12.5 days of gestation, after
CC which it is then expressed in a more restricted fashion, with
CC especially strong expression in developing lung, bone, and craniofacial
CC region. {ECO:0000269|PubMed:15355968}.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix. {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 -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00559.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI00559.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO17380.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK046333; BAC32684.1; -; mRNA.
DR EMBL; AF528163; AAO17380.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC100558; AAI00559.1; ALT_SEQ; mRNA.
DR EMBL; AF302012; AAK97226.1; -; mRNA.
DR CCDS; CCDS37566.1; -. [P58459-1]
DR RefSeq; NP_766207.2; NM_172619.4. [P58459-1]
DR AlphaFoldDB; P58459; -.
DR SMR; P58459; -.
DR STRING; 10090.ENSMUSP00000084905; -.
DR MEROPS; M12.235; -.
DR GlyGen; P58459; 5 sites.
DR iPTMnet; P58459; -.
DR PhosphoSitePlus; P58459; -.
DR PaxDb; P58459; -.
DR PRIDE; P58459; -.
DR Antibodypedia; 51079; 163 antibodies from 29 providers.
DR DNASU; 224697; -.
DR Ensembl; ENSMUST00000087623; ENSMUSP00000084905; ENSMUSG00000024299. [P58459-1]
DR Ensembl; ENSMUST00000234715; ENSMUSP00000157264; ENSMUSG00000024299. [P58459-2]
DR GeneID; 224697; -.
DR KEGG; mmu:224697; -.
DR UCSC; uc008bym.2; mouse. [P58459-2]
DR UCSC; uc008byn.2; mouse. [P58459-3]
DR UCSC; uc008byp.2; mouse. [P58459-1]
DR CTD; 81794; -.
DR MGI; MGI:2449112; Adamts10.
DR VEuPathDB; HostDB:ENSMUSG00000024299; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158404; -.
DR HOGENOM; CLU_000660_1_1_1; -.
DR InParanoid; P58459; -.
DR OMA; HRSCNTE; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; P58459; -.
DR TreeFam; TF313537; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 224697; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Adamts10; mouse.
DR PRO; PR:P58459; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P58459; protein.
DR Bgee; ENSMUSG00000024299; Expressed in humerus cartilage element and 195 other tissues.
DR ExpressionAtlas; P58459; baseline and differential.
DR Genevisible; P58459; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0001527; C:microfibril; ISS:UniProtKB.
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; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
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; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
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 Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..233
FT /evidence="ECO:0000250"
FT /id="PRO_0000270149"
FT CHAIN 234..1104
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 10"
FT /id="PRO_0000078211"
FT DOMAIN 239..457
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 460..546
FT /note="Disintegrin"
FT DOMAIN 547..602
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 825..885
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 888..943
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 944..1003
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1004..1058
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1066..1104
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 706..818
FT /note="Spacer"
FT /evidence="ECO:0000250"
FT ACT_SITE 393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 315..376
FT /evidence="ECO:0000250"
FT DISULFID 351..358
FT /evidence="ECO:0000250"
FT DISULFID 370..452
FT /evidence="ECO:0000250"
FT DISULFID 409..436
FT /evidence="ECO:0000250"
FT DISULFID 479..501
FT /evidence="ECO:0000250"
FT DISULFID 490..508
FT /evidence="ECO:0000250"
FT DISULFID 496..531
FT /evidence="ECO:0000250"
FT DISULFID 521..536
FT /evidence="ECO:0000250"
FT DISULFID 559..596
FT /evidence="ECO:0000250"
FT DISULFID 563..601
FT /evidence="ECO:0000250"
FT DISULFID 574..586
FT /evidence="ECO:0000250"
FT DISULFID 837..879
FT /evidence="ECO:0000250"
FT DISULFID 841..884
FT /evidence="ECO:0000250"
FT DISULFID 852..866
FT /evidence="ECO:0000250"
FT VAR_SEQ 80..145
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026108"
FT VAR_SEQ 146..147
FT /note="HG -> VS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026109"
FT VAR_SEQ 148..1104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026110"
FT VAR_SEQ 272..279
FT /note="AKLFQDSS -> SAFLGLES (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026111"
FT VAR_SEQ 280..1104
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026112"
SQ SEQUENCE 1104 AA; 121086 MW; 57811356FCB390FF CRC64;
MASACQILRW ALALGLGLTF KVTHAFRSQD ELLSSLESYE IAFPTRVDHN GAMLAFSPPA
FRRQRRGAGA TTESRLFYKV AAPSTHFLLN LTRSPRLLAG HVSVEYWTRE GLAWQRAARA
HCLYAGHLQG QAGSSHVAVS TCGGLHGLIV ADDEEYLIEP LQGGPKGHRG PEESGPHVVY
KRSSLRHPHL DTACGVRDEK PWKGRPWWLR TLKPPPARPL GNESERGQLG LKRSVSRERY
VETLVVADKM MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GNIVNILVTR LILLTEDQPT
LEITHHAGKS LDSFCKWQKS IVSHSGHGNA IPENGVANHD TAVLITRYDI CIYKNKPCGT
LGLAPVGGMC ERERSCSINE DIGLATAFTI AHEIGHTFGM NHDGVGNGCG ARGQDPAKLM
AAHITMKTNP FVWSSCSRDY ITSFLDSGLG LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR
FQHGVKSRQC KYGEVCSELW CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG
SRPEGVDGAW GPWTPWGDCS RSCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTND
CPPGSQDFRE MQCSEFDSVP FRGKFYTWKT YRGGGVKACS LTCLAEGFNF YTERAAAVVD
GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG DGSACETIEG VFSPALPGTG
YEDVVWIPKG SVHIFIQDLN LSLSHLALKG DQESLLLEGL PGTPQPHRLP LAGTTFHLRQ
GPDQAQSLEA LGPINASLII MVLAQAELPA LHYRFNAPIA RDALPPYSWH YAPWTKCSAQ
CAGGSQVQVV ECRNQLDSSA VAPHYCSGHS KLPKRQRACN TEPCPPDWVV GNWSRCSRSC
DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACQ GPMCPPEWAT LDWSECTPSC
GPGLRHRVVL CKSADQRSTL PPGHCLPAAK PPSTMRCNLR RCPPARWVTS EWGECSTQCG
LGQQQRTVRC TSHTGQPSRE CTEALRPSTM QQCEAKCDSV VPPGDGPEEC KDVNKVAYCP
LVLKFQFCSR AYFRQMCCKT CQGR
