ATS2_BOVIN
ID ATS2_BOVIN Reviewed; 1205 AA.
AC P79331;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
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; Synonyms=NPI;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=9122202; DOI=10.1073/pnas.94.6.2374;
RA Colige A., Li S.W., Sieron A.L., Nusgens B.V., Prockop D.J., Lapiere C.M.;
RT "cDNA cloning and expression of bovine procollagen I N-proteinase: a new
RT member of the superfamily of zinc-metalloproteinases with binding sites for
RT cells and other matrix components.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2374-2379(1997).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=7622483; DOI=10.1074/jbc.270.28.16724;
RA Colige A., Beschin A., Samyn B., Goebels Y., Van Beeumen J., Nusgens B.V.,
RA Lapiere C.M.;
RT "Characterization and partial amino acid sequencing of a 107-kDa
RT procollagen I N-proteinase purified by affinity chromatography on
RT immobilized type XIV collagen.";
RL J. Biol. Chem. 270:16724-16730(1995).
CC -!- FUNCTION: Cleaves the propeptides of type I and II collagen prior to
CC fibril assembly (PubMed:7622483). Does not act on type III collagen
CC (PubMed:7622483). 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:0000269|PubMed:7622483}.
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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Enzymatic activity is detected at high level in all
CC type I collagen-rich tissues such as skin, bones, tendons and aorta and
CC at low level in brain and thymus. The mRNA levels were
CC disproportionately high in heart, liver, retina and muscle.
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 N-terminus is blocked.
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 -!- DISEASE: Note=Defects in ADAMTS2 are the cause of dermatosparaxis, a
CC recessively inherited disorder characterized by severe skin fragility
CC and biochemically by the presence in skin of procollagen incompletely
CC processed at the N-terminus. {ECO:0000305|PubMed:7622483}.
CC -!- CAUTION: Has sometimes been referred to as ADAMTS3. {ECO:0000305}.
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DR EMBL; X96389; CAA65253.1; -; mRNA.
DR PIR; T18517; T18517.
DR RefSeq; NP_777056.1; NM_174631.2.
DR AlphaFoldDB; P79331; -.
DR SMR; P79331; -.
DR STRING; 9913.ENSBTAP00000019526; -.
DR MEROPS; M12.301; -.
DR PaxDb; P79331; -.
DR PRIDE; P79331; -.
DR Ensembl; ENSBTAT00000019526; ENSBTAP00000019526; ENSBTAG00000014665.
DR GeneID; 282401; -.
DR KEGG; bta:282401; -.
DR CTD; 9509; -.
DR VEuPathDB; HostDB:ENSBTAG00000014665; -.
DR VGNC; VGNC:25624; ADAMTS2.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156647; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; P79331; -.
DR OMA; VPYKIHG; -.
DR OrthoDB; 79609at2759; -.
DR TreeFam; TF313537; -.
DR BRENDA; 3.4.24.14; 908.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014665; Expressed in fornix of vagina and 104 other tissues.
DR ExpressionAtlas; P79331; baseline.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032964; P:collagen biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; IC:BHF-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0097435; P:supramolecular fiber organization; IC:BHF-UCL.
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 Cleavage on pair of basic residues; Collagen degradation;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..253
FT /evidence="ECO:0000250"
FT /id="PRO_0000029156"
FT CHAIN 254..1205
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 2"
FT /id="PRO_0000029157"
FT DOMAIN 260..464
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 474..554
FT /note="Disintegrin"
FT DOMAIN 555..610
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 848..906
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 908..968
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 969..1023
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1053..1091
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 717..845
FT /note="Spacer"
FT REGION 1163..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 685..687
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 943
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 987
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1092
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 337..386
FT /evidence="ECO:0000250"
FT DISULFID 380..459
FT /evidence="ECO:0000250"
FT DISULFID 419..445
FT /evidence="ECO:0000250"
FT DISULFID 486..511
FT /evidence="ECO:0000250"
FT DISULFID 497..520
FT /evidence="ECO:0000250"
FT DISULFID 506..539
FT /evidence="ECO:0000250"
FT DISULFID 533..544
FT /evidence="ECO:0000250"
FT DISULFID 567..604
FT /evidence="ECO:0000250"
FT DISULFID 571..609
FT /evidence="ECO:0000250"
FT DISULFID 582..594
FT /evidence="ECO:0000250"
FT DISULFID 981..1017
FT /evidence="ECO:0000250"
FT DISULFID 985..1022
FT /evidence="ECO:0000250"
FT DISULFID 996..1006
FT /evidence="ECO:0000250"
SQ SEQUENCE 1205 AA; 133888 MW; 7B5B232A45320371 CRC64;
MDPPAGAAGR LLCPALLLLL LLPLPADARL AAAAADPPGG PQGHGAERIL AVPVRTDAQG
RLVSHVVSAA TAPAGVRTRR AAPAQIPGLS GGSEEDPGGR LFYNVTVFGR DLHLRLRPNA
RLVAPGATVE WQGESGATRV EPLLGTCLYV GDVAGLAESS SVALSNCDGL AGLIRMEEEE
FFIEPLEKGL AAKEAEQGRV HVVYHRPTTS RPPPLGGPQA LDTGISADSL DSLSRALGVL
EERVNSSRRR MRRHAADDDY NIEVLLGVDD SVVQFHGTEH VQKYLLTLMN IVNEIYHDES
LGAHINVVLV RIILLSYGKS MSLIEIGNPS QSLENVCRWA YLQQKPDTDH DEYHDHAIFL
TRQDFGPSGM QGYAPVTGMC HPVRSCTLNH EDGFSSAFVV AHETGHVLGM EHDGQGNRCG
DEVRLGSIMA PLVQAAFHRF HWSRCSQQEL SRYLHSYDCL RDDPFTHDWP ALPQLPGLHY
SMNEQCRFDF GLGYMMCTAF RTFDPCKQLW CSHPDNPYFC KTKKGPPLDG TMCAPGKHCF
KGHCIWLTPD ILKRDGNWGA WSPFGSCSRT CGTGVKFRTR QCDNPHPANG GRTCSGLAYD
FQLCNSQDCP DALADFREEQ CRQWDLYFEH GDAQHHWLPH EHRDAKERCH LYCESKETGE
VVSMKRMVHD GTRCSYKDAF SLCVRGDCRK VGCDGVIGSS KQEDKCGVCG GDNSHCKVVK
GTFSRSPKKL GYIKMFEIPA GARHLLIQEA DTTSHHLAVK NLETGKFILN EENDVDPNSK
TFIAMGVEWE YRDEDGRETL QTMGPLHGTI TVLVIPEGDA RISLTYKYMI HEDSLNVDDN
NVLEDDSVGY EWALKKWSPC SKPCGGGSQF TKYGCRRRLD HKMVHRGFCD SVSKPKAIRR
TCNPQECSQP VWVTGEWEPC SRSCGRTGMQ VRSVRCVQPL HNNTTRSVHT KHCNDARPEG
RRACNRELCP GRWRAGSWSQ CSVTCGNGTQ ERPVLCRTAD DSFGVCREER PETARICRLG
PCPRNTSDPS KKSYVVQWLS RPDPNSPVQE TSSKGRCQGD KSVFCRMEVL SRYCSIPGYN
KLCCKSCNPH DNLTDVDDRA EPPSGKHNDI EELMPTLSVP TLVMEVQPPP GIPLEVPLNT
SSTNATEDHP ETNAVDVPYK IPGLEDEVQP PNLIPRRPSP YEKTRNQRIQ ELIDEMRKKE
MLGKF
