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Database: UniProt
Entry: Q9Y6L7
LinkDB: Q9Y6L7
Original site: Q9Y6L7 
ID   TLL2_HUMAN              Reviewed;        1015 AA.
AC   Q9Y6L7; A6NDK0; Q2M1H1; Q6PJN5; Q9UQ00;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   29-OCT-2014, entry version 118.
DE   RecName: Full=Tolloid-like protein 2;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=TLL2; Synonyms=KIAA0932;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 150-154.
RC   TISSUE=Placenta;
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=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA   Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [6]
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).
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: Binds 1 zinc ion per subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M12A family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 5 CUB domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00059}.
CC   -!- SIMILARITY: Contains 2 EGF-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA76776.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF059516; AAD42979.1; -; mRNA.
DR   EMBL; AB023149; BAA76776.2; ALT_INIT; mRNA.
DR   EMBL; AL138765; CAI13580.1; -; Genomic_DNA.
DR   EMBL; AL136181; CAI13580.1; JOINED; Genomic_DNA.
DR   EMBL; AL391136; CAI13580.1; JOINED; Genomic_DNA.
DR   EMBL; AL136181; CAH72983.1; -; Genomic_DNA.
DR   EMBL; AL138765; CAH72983.1; JOINED; Genomic_DNA.
DR   EMBL; AL391136; CAH72983.1; JOINED; Genomic_DNA.
DR   EMBL; AL391136; CAH72234.1; -; Genomic_DNA.
DR   EMBL; AL136181; CAH72234.1; JOINED; Genomic_DNA.
DR   EMBL; AL138765; CAH72234.1; JOINED; Genomic_DNA.
DR   EMBL; BC013871; AAH13871.1; -; mRNA.
DR   EMBL; BC112341; AAI12342.1; -; mRNA.
DR   EMBL; BC112366; AAI12367.1; -; mRNA.
DR   EMBL; BC113577; AAI13578.1; -; mRNA.
DR   CCDS; CCDS7449.1; -.
DR   RefSeq; NP_036597.1; NM_012465.3.
DR   UniGene; Hs.154296; -.
DR   ProteinModelPortal; Q9Y6L7; -.
DR   SMR; Q9Y6L7; 150-1003.
DR   STRING; 9606.ENSP00000350630; -.
DR   MEROPS; M12.018; -.
DR   PhosphoSite; Q9Y6L7; -.
DR   DMDM; 74762080; -.
DR   MaxQB; Q9Y6L7; -.
DR   PaxDb; Q9Y6L7; -.
DR   PRIDE; Q9Y6L7; -.
DR   DNASU; 7093; -.
DR   Ensembl; ENST00000357947; ENSP00000350630; ENSG00000095587.
DR   GeneID; 7093; -.
DR   KEGG; hsa:7093; -.
DR   UCSC; uc001kml.2; human.
DR   CTD; 7093; -.
DR   GeneCards; GC10M098114; -.
DR   H-InvDB; HIX0009074; -.
DR   HGNC; HGNC:11844; TLL2.
DR   MIM; 606743; gene.
DR   neXtProt; NX_Q9Y6L7; -.
DR   PharmGKB; PA36546; -.
DR   eggNOG; NOG70307; -.
DR   GeneTree; ENSGT00760000119018; -.
DR   HOGENOM; HOG000236339; -.
DR   HOVERGEN; HBG004859; -.
DR   InParanoid; Q9Y6L7; -.
DR   KO; K13047; -.
DR   OMA; NNYPSQA; -.
DR   OrthoDB; EOG7N8ZTV; -.
DR   PhylomeDB; Q9Y6L7; -.
DR   TreeFam; TF314351; -.
DR   Reactome; REACT_118572; Degradation of the extracellular matrix.
DR   Reactome; REACT_121139; Collagen biosynthesis and modifying enzymes.
DR   Reactome; REACT_150206; Crosslinking of collagen fibrils.
DR   Reactome; REACT_150268; Anchoring fibril formation.
DR   GeneWiki; TLL2; -.
DR   GenomeRNAi; 7093; -.
DR   NextBio; 27747; -.
DR   PRO; PR:Q9Y6L7; -.
DR   Bgee; Q9Y6L7; -.
DR   CleanEx; HS_TLL2; -.
DR   Genevestigator; Q9Y6L7; -.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
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; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
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; SM00179; EGF_CA; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 5.
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; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   PROPEP       26    149       {ECO:0000269|PubMed:10479448}.
FT                                /FTId=PRO_0000046036.
FT   CHAIN       150   1015       Tolloid-like protein 2.
FT                                /FTId=PRO_0000046037.
FT   DOMAIN      351    463       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      464    576       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      576    617       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      620    732       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      732    772       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      776    888       CUB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      889   1005       CUB 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   REGION      150    350       Metalloprotease. {ECO:0000250}.
FT   ACT_SITE    243    243       {ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       242    242       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       246    246       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       252    252       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   CARBOHYD    171    171       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    361    361       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    392    392       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    628    628       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    805    805       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    351    377       {ECO:0000250}.
FT   DISULFID    404    426       {ECO:0000250}.
FT   DISULFID    464    490       {ECO:0000250}.
FT   DISULFID    517    539       {ECO:0000250}.
FT   DISULFID    580    592       {ECO:0000250}.
FT   DISULFID    588    601       {ECO:0000250}.
FT   DISULFID    603    616       {ECO:0000250}.
FT   DISULFID    620    646       {ECO:0000250}.
FT   DISULFID    673    695       {ECO:0000250}.
FT   DISULFID    736    747       {ECO:0000250}.
FT   DISULFID    743    756       {ECO:0000250}.
FT   DISULFID    758    771       {ECO:0000250}.
FT   DISULFID    776    802       {ECO:0000250}.
FT   DISULFID    829    851       {ECO:0000250}.
FT   DISULFID    889    919       {ECO:0000250}.
FT   DISULFID    946    968       {ECO:0000250}.
FT   CONFLICT    495    495       T -> M (in Ref. 2; BAA76776).
FT                                {ECO:0000305}.
FT   CONFLICT    576    593       EVDECSWPDHGGCEHRCV -> GKKKKKKKKKKKKKKKKK
FT                                (in Ref. 5; AAH13871). {ECO:0000305}.
SQ   SEQUENCE   1015 AA;  113557 MW;  25F5B23065861593 CRC64;
     MPRATALGAL VSLLLLLPLP RGAGGLGERP DATADYSELD GEEGTEQQLE HYHDPCKAAV
     FWGDIALDED DLKLFHIDKA RDWTKQTVGA TGHSTGGLEE QASESSPDTT AMDTGTKEAG
     KDGRENTTLL HSPGTLHAAA KTFSPRVRRA TTSRTERIWP GGVIPYVIGG NFTGSQRAIF
     KQAMRHWEKH TCVTFIERTD EESFIVFSYR TCGCCSYVGR RGGGPQAISI GKNCDKFGIV
     AHELGHVVGF WHEHTRPDRD QHVTIIRENI QPGQEYNFLK MEAGEVSSLG ETYDFDSIMH
     YARNTFSRGV FLDTILPRQD DNGVRPTIGQ RVRLSQGDIA QARKLYKCPA CGETLQDTTG
     NFSAPGFPNG YPSYSHCVWR ISVTPGEKIV LNFTSMDLFK SRLCWYDYVE VRDGYWRKAP
     LLGRFCGDKI PEPLVSTDSR LWVEFRSSSN ILGKGFFAAY EATCGGDMNK DAGQIQSPNY
     PDDYRPSKEC VWRITVSEGF HVGLTFQAFE IERHDSCAYD YLEVRDGPTE ESALIGHFCG
     YEKPEDVKSS SNRLWMKFVS DGSINKAGFA ANFFKEVDEC SWPDHGGCEH RCVNTLGSYK
     CACDPGYELA ADKKMCEVAC GGFITKLNGT ITSPGWPKEY PTNKNCVWQV VAPAQYRISL
     QFEVFELEGN DVCKYDFVEV RSGLSPDAKL HGRFCGSETP EVITSQSNNM RVEFKSDNTV
     SKRGFRAHFF SDKDECAKDN GGCQHECVNT FGSYLCRCRN GYWLHENGHD CKEAGCAHKI
     SSVEGTLASP NWPDKYPSRR ECTWNISSTA GHRVKLTFNE FEIEQHQECA YDHLEMYDGP
     DSLAPILGRF CGSKKPDPTV ASGSSMFLRF YSDASVQRKG FQAVHSTECG GRLKAEVQTK
     ELYSHAQFGD NNYPSEARCD WVIVAEDGYG VELTFRTFEV EEEADCGYDY MEAYDGYDSS
     APRLGRFCGS GPLEEIYSAG DSLMIRFRTD DTINKKGFHA RYTSTKFQDA LHMKK
//
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