ATS2_MOUSE
ID ATS2_MOUSE Reviewed; 1213 AA.
AC Q8C9W3;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 2;
DE Short=ADAM-TS 2;
DE Short=ADAM-TS2;
DE Short=ADAMTS-2;
DE EC=3.4.24.14;
DE AltName: Full=Procollagen I N-proteinase;
DE Short=PC I-NP;
DE AltName: Full=Procollagen I/II amino propeptide-processing enzyme;
DE AltName: Full=Procollagen N-endopeptidase;
DE Short=pNPI;
DE Flags: Precursor;
GN Name=Adamts2;
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].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 1058-1068, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Cleaves the propeptides of type I and II collagen prior to
CC fibril assembly (By similarity). Does not act on type III collagen (By
CC similarity). Cleaves lysyl oxidase LOX at a site downstream of its
CC propeptide cleavage site to produce a short LOX form with reduced
CC collagen-binding activity (By similarity).
CC {ECO:0000250|UniProtKB:O95450, ECO:0000250|UniProtKB:P79331}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-|-
CC Gln and of alpha1(II) and alpha2(I) at Ala-|-Gln.; EC=3.4.24.14;
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: May belong to a multimeric complex. Binds specifically to
CC collagen type XIV (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix.
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}.
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DR EMBL; AK040370; BAC30572.1; -; mRNA.
DR EMBL; BC046456; AAH46456.1; -; mRNA.
DR CCDS; CCDS24636.1; -.
DR RefSeq; NP_783574.1; NM_175643.3.
DR AlphaFoldDB; Q8C9W3; -.
DR SMR; Q8C9W3; -.
DR BioGRID; 229775; 3.
DR STRING; 10090.ENSMUSP00000040171; -.
DR MEROPS; M12.301; -.
DR GlyGen; Q8C9W3; 9 sites.
DR iPTMnet; Q8C9W3; -.
DR PhosphoSitePlus; Q8C9W3; -.
DR CPTAC; non-CPTAC-3691; -.
DR MaxQB; Q8C9W3; -.
DR PaxDb; Q8C9W3; -.
DR PRIDE; Q8C9W3; -.
DR ProteomicsDB; 277201; -.
DR Antibodypedia; 17642; 181 antibodies from 29 providers.
DR DNASU; 216725; -.
DR Ensembl; ENSMUST00000040523; ENSMUSP00000040171; ENSMUSG00000036545.
DR GeneID; 216725; -.
DR KEGG; mmu:216725; -.
DR UCSC; uc007iso.2; mouse.
DR CTD; 9509; -.
DR MGI; MGI:1347356; Adamts2.
DR VEuPathDB; HostDB:ENSMUSG00000036545; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156647; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; Q8C9W3; -.
DR OMA; VPYKIHG; -.
DR OrthoDB; 79609at2759; -.
DR PhylomeDB; Q8C9W3; -.
DR TreeFam; TF313537; -.
DR BRENDA; 3.4.24.14; 3474.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 216725; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Adamts2; mouse.
DR PRO; PR:Q8C9W3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C9W3; protein.
DR Bgee; ENSMUSG00000036545; Expressed in ascending aorta and 186 other tissues.
DR ExpressionAtlas; Q8C9W3; baseline and differential.
DR Genevisible; Q8C9W3; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 2.20.100.10; -; 4.
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; IPR013275; Pept_M12B_ADAM-TS2.
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; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01859; ADAMTS2.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF82895; SSF82895; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 1: Evidence at protein level;
KW Collagen degradation; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..260
FT /evidence="ECO:0000250"
FT /id="PRO_0000029161"
FT CHAIN 261..1213
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 2"
FT /id="PRO_0000029160"
FT DOMAIN 267..471
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 480..560
FT /note="Disintegrin"
FT DOMAIN 561..617
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 855..913
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 915..975
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 976..1030
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1060..1098
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 211..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..851
FT /note="Spacer"
FT MOTIF 692..694
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 950
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1032
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1099
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 344..393
FT /evidence="ECO:0000250"
FT DISULFID 387..466
FT /evidence="ECO:0000250"
FT DISULFID 426..452
FT /evidence="ECO:0000250"
FT DISULFID 493..518
FT /evidence="ECO:0000250"
FT DISULFID 504..527
FT /evidence="ECO:0000250"
FT DISULFID 513..546
FT /evidence="ECO:0000250"
FT DISULFID 540..551
FT /evidence="ECO:0000250"
FT DISULFID 574..611
FT /evidence="ECO:0000250"
FT DISULFID 578..616
FT /evidence="ECO:0000250"
FT DISULFID 589..601
FT /evidence="ECO:0000250"
FT DISULFID 988..1024
FT /evidence="ECO:0000250"
FT DISULFID 992..1029
FT /evidence="ECO:0000250"
FT DISULFID 1003..1013
FT /evidence="ECO:0000250"
SQ SEQUENCE 1213 AA; 135299 MW; B27431E00443EDB5 CRC64;
MDPPAGAARR LLCPALLLLL LPPPPLLLLP PPPASVRLVA ATEPPGGPPG QGAERILAVP
VRTDAQGRLV SHVVSLETAG AGVRARRAAL DQTSGLPGGA AQDPGGRLFY NLTVFGRDLH
LRLRPNARLV APGATVEWQG ETGDTRVEPL LGSCLYVGDV ADLPKASSVA LSNCDGLAGL
IRMEEEEFFI EPLEKGQTDQ EAEQGRVHVV YRRPPTPKPP PVSEPQALDT GVSQGNLDSL
SRALGVLEER INSSRRRVRR HATDDDYNIE VLLGVDDSVV QFHGKEHVQK YLLTLMNIVN
EIYHDESLGA HINVVLVRII LLSHAKSMSL IEIGNPSQSL ENVCRWAYLQ QKPDTDHDEY
HDHAIFLTRQ DFGPSGMQGY APVTGMCHPV RSCTLNHEDG FSSAFVVAHE TGHVLGMEHD
GQGNRCGDEV RLGSIMAPLV QAAFHRFHWS RCSQQELSRY LHSYDCLRDD PFAHDWPALP
QLPGLHYSMN EQCRFDFGLG YMMCTAFRTF DPCKQLWCSH PDNPYFCKTK KGPPLDGTMC
APGKHCFKGH CIWLTPDILK RDGNWGAWTP FGSCSRTCGT GVKFRTRQCD NPHPANGGRT
CSGLAYDFQL CNPQDCPNSL ADFREEQCQQ WDLYFEHGDV QHHWLPHEHR DAKERCHLYC
ESKETGEVVS MKRMVHDGTR CSYKDAFSLC VRGDCRKVGC DGVIGSRKQE DKCGVCGGDN
THCKVVKGTF TRSPRKQDYI KMFEIPAGAR HLLIQEADTT SHHLSVKNLE TGKFILNEEN
HLDPNSRSFI AMGVEWEYRN EDERETLQTI GPLHGTITVL VIPEGDTRIS LTYKYMIHED
SLNVDDNNVL EDDAVRHEWA LKKWSPCSKP CGGGSQFTKY GCRRRLDSKM VHRAFCSALA
KPKAIRRACN PQECSQPVWV TGEWEPCTQS CGRTGMQVRS VRCIQPLHNN TTRSVHTKHC
NDHRPESRRA CNRELCPGRW RAGSWSQCSV TCGNGTQERP VLCRTADDNF GVCREERPET
ARICRLAPCP RNGSDPSKKS YVVQWLSRPD PDSPIQKISS KDQCQGDKSM FCRMEVLSRY
CSIPSYNKLC CKSCNPPRNL SNTEDGGVEP PPGKHNDIDV FMPTLPGPTV ATQVQPSPGP
PLEAPLNVSS TNATEDHPET NAVDVPYKIH GVDEEVPSPN LIPRRPSLYV KTRNQRIQEL
INAVQRKEKP GKF
