GenomeNet

Database: UniProt
Entry: Q9WVM6
LinkDB: Q9WVM6
Original site: Q9WVM6 
  All links  
No link information was found.   
ID   TLL2_MOUSE              Reviewed;        1012 AA.
AC   Q9WVM6; A2RTK3;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   10-APR-2019, entry version 131.
DE   RecName: Full=Tolloid-like protein 2;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=Tll2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=10479448; DOI=10.1006/dbio.1999.9383;
RA   Scott I.C., Blitz I.L., Pappano W.N., Imamura Y., Clark T.G.,
RA   Steiglitz B.M., Thomas C.L., Maas S.A., Takahara K., Cho K.W.,
RA   Greenspan D.S.;
RT   "Mammalian BMP-1/Tolloid-related metalloproteinases, including novel
RT   family member mammalian Tolloid-like 2, have differential enzymatic
RT   activities and distributions of expression relevant to patterning and
RT   skeletogenesis.";
RL   Dev. Biol. 213:283-300(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=11313359; DOI=10.1074/jbc.M102352200;
RA   Uzel M.I., Scott I.C., Babakhanlou-Chase H., Palamakumbura A.H.,
RA   Pappano W.N., Hong H.-H., Greenspan D.S., Trackman P.C.;
RT   "Multiple bone morphogenetic protein 1-related mammalian
RT   metalloproteinases process pro-lysyl oxidase at the correct
RT   physiological site and control lysyl oxidase activation in mouse
RT   embryo fibroblast cultures.";
RL   J. Biol. Chem. 276:22537-22543(2001).
RN   [4]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-960 AND ARG-963, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Protease which specifically processes pro-lysyl oxidase.
CC       Required for the embryonic development. Predominant protease,
CC       which in the development, influences dorsal-ventral patterning and
CC       skeletogenesis.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 7.5 dpc, in a limited way, in
CC       the posterior portion of the egg cylinder in the nascent mesoderm
CC       streaming off the primitive streak. At the distant end of the
CC       embryo cylinder, expression ended at the node. Later in the
CC       development, expression seems to be limited to developing skeletal
CC       muscle and central nervous system. {ECO:0000269|PubMed:10479448}.
DR   EMBL; AF073526; AAD42993.1; -; mRNA.
DR   EMBL; BC132537; AAI32538.1; -; mRNA.
DR   CCDS; CCDS37986.1; -.
DR   RefSeq; NP_036034.1; NM_011904.3.
DR   UniGene; Mm.89983; -.
DR   ProteinModelPortal; Q9WVM6; -.
DR   SMR; Q9WVM6; -.
DR   STRING; 10090.ENSMUSP00000025986; -.
DR   MEROPS; M12.018; -.
DR   iPTMnet; Q9WVM6; -.
DR   PhosphoSitePlus; Q9WVM6; -.
DR   MaxQB; Q9WVM6; -.
DR   PaxDb; Q9WVM6; -.
DR   PRIDE; Q9WVM6; -.
DR   Ensembl; ENSMUST00000025986; ENSMUSP00000025986; ENSMUSG00000025013.
DR   GeneID; 24087; -.
DR   KEGG; mmu:24087; -.
DR   UCSC; uc008hlr.1; mouse.
DR   CTD; 7093; -.
DR   MGI; MGI:1346044; Tll2.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   GeneTree; ENSGT00940000160572; -.
DR   HOGENOM; HOG000236339; -.
DR   HOVERGEN; HBG004859; -.
DR   InParanoid; Q9WVM6; -.
DR   KO; K13047; -.
DR   OMA; SSMFLRF; -.
DR   OrthoDB; 170905at2759; -.
DR   PhylomeDB; Q9WVM6; -.
DR   TreeFam; TF314351; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-2214320; Anchoring fibril formation.
DR   PRO; PR:Q9WVM6; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000025013; Expressed in 9 organ(s), highest expression level in female gonad.
DR   ExpressionAtlas; Q9WVM6; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; IMP:MGI.
DR   CDD; cd00041; CUB; 5.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 5.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR015446; BMP_1/tolloid-like.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR034036; ZnMP_TLD/BMP1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 5.
DR   Pfam; PF07645; EGF_CA; 1.
DR   PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 5.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 5.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cleavage on pair of basic residues; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Methylation; Protease; Reference proteome; Repeat;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   PROPEP       22    146       {ECO:0000250}.
FT                                /FTId=PRO_0000046038.
FT   CHAIN       147   1012       Tolloid-like protein 2.
FT                                /FTId=PRO_0000046039.
FT   DOMAIN      146    346       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      348    460       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      461    573       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      573    614       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      617    729       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      729    769       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      773    885       CUB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      886   1002       CUB 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   ACT_SITE    240    240       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       239    239       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       243    243       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       249    249       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   MOD_RES     960    960       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     963    963       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   CARBOHYD    168    168       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    358    358       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    389    389       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    625    625       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    802    802       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    189    345       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    209    231       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    211    212       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    348    374       {ECO:0000250}.
FT   DISULFID    401    423       {ECO:0000250}.
FT   DISULFID    461    487       {ECO:0000250}.
FT   DISULFID    514    536       {ECO:0000250}.
FT   DISULFID    577    589       {ECO:0000250}.
FT   DISULFID    585    598       {ECO:0000250}.
FT   DISULFID    600    613       {ECO:0000250}.
FT   DISULFID    617    643       {ECO:0000250}.
FT   DISULFID    670    692       {ECO:0000250}.
FT   DISULFID    733    744       {ECO:0000250}.
FT   DISULFID    740    753       {ECO:0000250}.
FT   DISULFID    755    768       {ECO:0000250}.
FT   DISULFID    773    799       {ECO:0000250}.
FT   DISULFID    826    848       {ECO:0000250}.
FT   DISULFID    886    916       {ECO:0000250}.
FT   DISULFID    943    965       {ECO:0000250}.
SQ   SEQUENCE   1012 AA;  113252 MW;  72EEE268A4D8C5FE CRC64;
     MPLATTLGTL VLLLLLPLPR GAEVTGDHSN VALDYGALEG EEGTEQQLHY HDPCKAAVFW
     GDIALDEDDL KLFHIDKAED WTKPSIDKPG HDTGGLEETS ARWPNDTASN ASIQAPRKDG
     KDATTFLPNP GTSNTTAKTF SARVRRATTS RTERIWPGGV IPYVIGGNFT GTQRAIFKQA
     MRHWEKHTCV TFVERTDEES FIVFSYRTCG CCSYVGRRGG GPQAISIGKN CDKFGIVAHE
     LGHVVGFWHE HTRPDRDQHV TIIRENIQPG QEYNFLKMEA GEVSSLGETY DFDSIMHYAR
     NTFSRGVFLD TILPRRDDNG VRPTIGQRVR LSQGDIAQAR KLYKCPACGE TLQDTTGNFS
     APGFPNGYPS YSHCVWRISV TPGEKIILNF TSMDLFKSRL CWYDYVEIRD GYWRKAPLLG
     RFCGDKIPES LVSSDSRLWV EFRSSSSSLG KGFFAVYEAM CGGDITKDAG QIQSPNYPDD
     YRPSKECVWR ITVPDGFHVG LTFQSFEIER HDSCAYDYLE IRDGPTEDST LIGHFCGYEK
     PEAVKSSANR LWVKFVSDGS INKAGFAANF FKEVDECSWP DHGGCEQRCV NTLGSYTCAC
     DPGYELAADK KTCEVACGGF ITKLNGTITS PGWPKEYPTN KNCVWQVVAP VQYRISLQFE
     AFELEGNDVC KYDFVEVRSG LSPDAKLHGK FCGSETPEVI TSQSNNMRVE FKSDNTVSKR
     GFRAHFFSDK DECAKDNGGC QQECVNTFGS YLCRCRNGYR LHENGHDCKE AGCAYKISSA
     EGTLMSPNWP DKYPSRKECT WNISSTAGHR VKITFSEFEI EQHQECAYDH LELYDGTDSL
     APILGRFCGS KKPDPVVATG SSLFLRFYSD ASVQRKGFQA VHSTECGGRL KAEVQTKELY
     SHAQFGDNNY PSQARCDWVI VAEDGYGVEL IFRTFEVEEE ADCGYDFMEA YDGYDSSAPR
     LGRFCGSGPL EEIYSAGDSL MIRFHTDDTI NKKGFHARYT STKFQDALHM RK
//
DBGET integrated database retrieval system