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TLL2_HUMAN
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   03-AUG-2022, entry version 171.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 family
RT   member mammalian Tolloid-like 2, have differential enzymatic activities and
RT   distributions of expression relevant to patterning and 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., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   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., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., 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 project:
RT   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 metalloproteinases
RT   process pro-lysyl oxidase at the correct physiological site and control
RT   lysyl oxidase activation in mouse 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, which in
CC       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   -!- 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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391136; -; NOT_ANNOTATED_CDS; 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   AlphaFoldDB; Q9Y6L7; -.
DR   SMR; Q9Y6L7; -.
DR   BioGRID; 112948; 28.
DR   IntAct; Q9Y6L7; 1.
DR   STRING; 9606.ENSP00000350630; -.
DR   BindingDB; Q9Y6L7; -.
DR   ChEMBL; CHEMBL4295995; -.
DR   DrugBank; DB01989; Methyl N-{[(1R)-1-({1-[(benzyloxy)carbonyl]-L-prolyl-6-ammonio-L-norleucyl}amino)-2-phenylethyl](hydroxy)phosphoryl}-L-alanyl-L-prolinate.
DR   MEROPS; M12.018; -.
DR   GlyConnect; 1820; 1 N-Linked glycan (1 site).
DR   GlyGen; Q9Y6L7; 5 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9Y6L7; -.
DR   PhosphoSitePlus; Q9Y6L7; -.
DR   BioMuta; TLL2; -.
DR   DMDM; 74762080; -.
DR   MassIVE; Q9Y6L7; -.
DR   MaxQB; Q9Y6L7; -.
DR   PaxDb; Q9Y6L7; -.
DR   PeptideAtlas; Q9Y6L7; -.
DR   PRIDE; Q9Y6L7; -.
DR   ProteomicsDB; 86720; -.
DR   Antibodypedia; 53639; 51 antibodies from 18 providers.
DR   DNASU; 7093; -.
DR   Ensembl; ENST00000357947.4; ENSP00000350630.3; ENSG00000095587.9.
DR   GeneID; 7093; -.
DR   KEGG; hsa:7093; -.
DR   MANE-Select; ENST00000357947.4; ENSP00000350630.3; NM_012465.4; NP_036597.1.
DR   UCSC; uc001kml.3; human.
DR   CTD; 7093; -.
DR   DisGeNET; 7093; -.
DR   GeneCards; TLL2; -.
DR   HGNC; HGNC:11844; TLL2.
DR   HPA; ENSG00000095587; Tissue enhanced (brain, heart muscle, tongue).
DR   MIM; 606743; gene.
DR   neXtProt; NX_Q9Y6L7; -.
DR   OpenTargets; ENSG00000095587; -.
DR   PharmGKB; PA36546; -.
DR   VEuPathDB; HostDB:ENSG00000095587; -.
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00940000160572; -.
DR   HOGENOM; CLU_005140_0_0_1; -.
DR   InParanoid; Q9Y6L7; -.
DR   OMA; WTKQTVG; -.
DR   OrthoDB; 170905at2759; -.
DR   PhylomeDB; Q9Y6L7; -.
DR   TreeFam; TF314351; -.
DR   PathwayCommons; Q9Y6L7; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-2214320; Anchoring fibril formation.
DR   Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR   SignaLink; Q9Y6L7; -.
DR   BioGRID-ORCS; 7093; 12 hits in 1072 CRISPR screens.
DR   ChiTaRS; TLL2; human.
DR   GeneWiki; TLL2; -.
DR   GenomeRNAi; 7093; -.
DR   Pharos; Q9Y6L7; Tchem.
DR   PRO; PR:Q9Y6L7; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9Y6L7; protein.
DR   Bgee; ENSG00000095587; Expressed in buccal mucosa cell and 113 other tissues.
DR   Genevisible; Q9Y6L7; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030199; P:collagen fibril organization; TAS:Reactome.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR   GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
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; 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; Developmental protein;
KW   Differentiation; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Methylation; Protease; Reference proteome; Repeat; Secreted; Signal; Zinc;
KW   Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..149
FT                   /evidence="ECO:0000269|PubMed:10479448"
FT                   /id="PRO_0000046036"
FT   CHAIN           150..1015
FT                   /note="Tolloid-like protein 2"
FT                   /id="PRO_0000046037"
FT   DOMAIN          149..349
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DOMAIN          351..463
FT                   /note="CUB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          464..576
FT                   /note="CUB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          576..617
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          620..732
FT                   /note="CUB 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          732..772
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          776..888
FT                   /note="CUB 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          889..1005
FT                   /note="CUB 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   REGION          24..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   MOD_RES         963
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM6"
FT   MOD_RES         966
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WVM6"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        628
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        805
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        192..348
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        212..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        214..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT   DISULFID        351..377
FT                   /evidence="ECO:0000250"
FT   DISULFID        404..426
FT                   /evidence="ECO:0000250"
FT   DISULFID        464..490
FT                   /evidence="ECO:0000250"
FT   DISULFID        517..539
FT                   /evidence="ECO:0000250"
FT   DISULFID        580..592
FT                   /evidence="ECO:0000250"
FT   DISULFID        588..601
FT                   /evidence="ECO:0000250"
FT   DISULFID        603..616
FT                   /evidence="ECO:0000250"
FT   DISULFID        620..646
FT                   /evidence="ECO:0000250"
FT   DISULFID        673..695
FT                   /evidence="ECO:0000250"
FT   DISULFID        736..747
FT                   /evidence="ECO:0000250"
FT   DISULFID        743..756
FT                   /evidence="ECO:0000250"
FT   DISULFID        758..771
FT                   /evidence="ECO:0000250"
FT   DISULFID        776..802
FT                   /evidence="ECO:0000250"
FT   DISULFID        829..851
FT                   /evidence="ECO:0000250"
FT   DISULFID        889..919
FT                   /evidence="ECO:0000250"
FT   DISULFID        946..968
FT                   /evidence="ECO:0000250"
FT   CONFLICT        495
FT                   /note="T -> M (in Ref. 2; BAA76776)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576..593
FT                   /note="EVDECSWPDHGGCEHRCV -> GKKKKKKKKKKKKKKKKK (in Ref. 5;
FT                   AAH13871)"
FT                   /evidence="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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