Reviewed,
UniProtKB/Swiss-Prot Q61810 (LTBP3_MOUSE)
Last modified
June 16, 2009.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Latent-transforming growth factor beta-binding protein 3 Short name=LTBP-3 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1268 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May be involved in the assembly, secretion and targeting of TGF- beta1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGF-beta1. May have a structural role in the extra cellular matrix (ECM). |
| Subunit structure | Forms part of the large latent transforming growth factor beta (TGFB1) precursor complex; removal is essential for activation of complex. |
| Subcellular location | Secreted. Note: Secretion occurs after coexpression with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 propeptide. |
| Developmental stage | At 8.5-9.0 dpc highly expressed in liver. Significant expression was also seen in the developing central nervous, somites and cardiovascular tissue. At 13.5-16.5 dpc expression was seen in osteoblasts, respiratory epithelial cells, and nephrons and dermal connective tissue. |
| Domain | Associates covalently with small latent TGF-beta complex via Repeat C. |
| Post-translational modification | Contains hydroxylated asparagine residues By similarity. |
| Sequence similarities | Belongs to the LTBP family. Contains 13 EGF-like domains. Contains 3 TB (TGF-beta binding) domains. |
| Sequence caution | The sequence AAB53015.1 differs from that shown. Reason: Frameshift at positions 6, 38, 56, 155, 158, 160, 480 and 775. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Coding sequence diversity | Alternative splicing |
| Domain | EGF-like domain Repeat Signal |
| Ligand | Growth factor binding |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | skeletal system development Inferred from mutant phenotype. Source: MGI transforming growth factor beta receptor signaling pathway Ref.1Inferred from mutant phenotype. Source: MGI |
| Cellular component | extracellular region Ref.1 Inferred from direct assay. Source: MGI |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: InterPro growth factor bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q61810-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q61810-2) The sequence of this isoform differs from the canonical sequence as follows: 860-882: KKDIDECSQDPGLCLPHACENLQ → QGMRSWPGILKGEAGQCDLFDTL 883-1268: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 38 | 38 | Potential | ||||||||
| Chain | 39 – 1268 | 1230 | Latent-transforming growth factor beta-binding protein 3 | PRO_0000007647 | |||||||
Regions | |||||||||||
| Domain | 106 – 138 | 33 | EGF-like 1 | ||||||||
| Domain | 274 – 328 | 55 | TB 1 | ||||||||
| Domain | 352 – 392 | 41 | EGF-like 2; calcium-binding Potential | ||||||||
| Domain | 400 – 452 | 53 | TB 2 | ||||||||
| Domain | 570 – 611 | 42 | EGF-like 3 | ||||||||
| Domain | 612 – 655 | 44 | EGF-like 4; calcium-binding Potential | ||||||||
| Domain | 656 – 698 | 43 | EGF-like 5; calcium-binding Potential | ||||||||
| Domain | 740 – 779 | 40 | EGF-like 6; calcium-binding Potential | ||||||||
| Domain | 780 – 820 | 41 | EGF-like 7; calcium-binding Potential | ||||||||
| Domain | 821 – 860 | 40 | EGF-like 8; calcium-binding Potential | ||||||||
| Domain | 862 – 903 | 42 | EGF-like 9; calcium-binding Potential | ||||||||
| Domain | 912 – 966 | 55 | TB 3 | ||||||||
| Domain | 988 – 1030 | 43 | EGF-like 10; calcium-binding Potential | ||||||||
| Domain | 1031 – 1070 | 40 | EGF-like 11; calcium-binding Potential | ||||||||
| Domain | 1201 – 1246 | 46 | EGF-like 12; calcium-binding Potential | ||||||||
| Compositional bias | 21 – 32 | 12 | Poly-Leu | ||||||||
| Compositional bias | 47 – 52 | 6 | Poly-Gly | ||||||||
| Compositional bias | 191 – 292 | 102 | Pro-rich | ||||||||
| Compositional bias | 480 – 556 | 77 | Pro-rich | ||||||||
| Compositional bias | 574 – 889 | 316 | Cys-rich | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 86 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 346 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 840 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 931 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1222 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 110 ↔ 120 | By similarity | |||||||||
| Disulfide bond | 114 ↔ 126 | By similarity | |||||||||
| Disulfide bond | 128 ↔ 137 | By similarity | |||||||||
| Disulfide bond | 356 ↔ 367 | By similarity | |||||||||
| Disulfide bond | 363 ↔ 376 | By similarity | |||||||||
| Disulfide bond | 378 ↔ 391 | By similarity | |||||||||
| Disulfide bond | 574 ↔ 586 | By similarity | |||||||||
| Disulfide bond | 581 ↔ 595 | By similarity | |||||||||
| Disulfide bond | 597 ↔ 610 | By similarity | |||||||||
| Disulfide bond | 616 ↔ 628 | By similarity | |||||||||
| Disulfide bond | 621 ↔ 637 | By similarity | |||||||||
| Disulfide bond | 639 ↔ 654 | By similarity | |||||||||
| Disulfide bond | 660 ↔ 672 | By similarity | |||||||||
| Disulfide bond | 666 ↔ 681 | By similarity | |||||||||
| Disulfide bond | 683 ↔ 697 | By similarity | |||||||||
| Disulfide bond | 744 ↔ 755 | By similarity | |||||||||
| Disulfide bond | 750 ↔ 764 | By similarity | |||||||||
| Disulfide bond | 766 ↔ 778 | By similarity | |||||||||
| Disulfide bond | 784 ↔ 795 | By similarity | |||||||||
| Disulfide bond | 790 ↔ 804 | By similarity | |||||||||
| Disulfide bond | 806 ↔ 819 | By similarity | |||||||||
| Disulfide bond | 825 ↔ 836 | By similarity | |||||||||
| Disulfide bond | 831 ↔ 845 | By similarity | |||||||||
| Disulfide bond | 847 ↔ 859 | By similarity | |||||||||
| Disulfide bond | 866 ↔ 878 | By similarity | |||||||||
| Disulfide bond | 873 ↔ 887 | By similarity | |||||||||
| Disulfide bond | 889 ↔ 902 | By similarity | |||||||||
| Disulfide bond | 992 ↔ 1005 | By similarity | |||||||||
| Disulfide bond | 1000 ↔ 1014 | By similarity | |||||||||
| Disulfide bond | 1016 ↔ 1029 | By similarity | |||||||||
| Disulfide bond | 1035 ↔ 1046 | By similarity | |||||||||
| Disulfide bond | 1041 ↔ 1055 | By similarity | |||||||||
| Disulfide bond | 1057 ↔ 1070 | By similarity | |||||||||
| Disulfide bond | 1205 ↔ 1220 | By similarity | |||||||||
| Disulfide bond | 1215 ↔ 1229 | By similarity | |||||||||
| Disulfide bond | 1231 ↔ 1245 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 860 – 882 | 23 | KKDID…CENLQ → QGMRSWPGILKGEAGQCDLF DTL in isoform 2. | VSP_009242 | |||||||
| Alternative sequence | 883 – 1268 | 386 | Missing in isoform 2. | VSP_009243 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 16 | 1 | H → R in AAB53015. Ref.1 | ||||||||
| Sequence conflict | 20 | 1 | A → G in AAB53015. Ref.1 | ||||||||
| Sequence conflict | 35 | 1 | Missing in AAB53015. Ref.1 | ||||||||
| Sequence conflict | 45 | 1 | E → Q in AAB53015. Ref.1 | ||||||||
| Sequence conflict | 104 | 1 | A → G in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 172 | 1 | E → Q in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 263 | 1 | P → Q in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 328 | 1 | V → G in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 361 – 363 | 3 | NVC → MCR in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 387 – 389 | 3 | LAA → SRT in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 453 | 1 | P → PA in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 661 | 1 | A → T in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 768 | 1 | Q → QG in BAC38053. Ref.2 | ||||||||
| Sequence conflict | 849 | 1 | L → Q in BAC38053. Ref.2 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation of a novel latent transforming growth factor-beta binding protein gene (LTBP-3)." Yin W., Smiley E., Germiller J., Mecham R.P., Florer J.B., Wenstrup R.J., Bonadio J. J. Biol. Chem. 270:10147-10160(1995) [PubMed: 7730318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Adipose tissue. |
| [3] | "8-cysteine TGF-BP structural motifs are the site of covalent binding between mouse LTBP-3, LTBP-2, and latent TGF-beta 1." Yin W., Fang J., Smiley E., Bonadio J. Biochim. Biophys. Acta 1383:340-350(1998) [PubMed: 9602168] [Abstract] Cited for: INTERACTION WITH TGFB1. |
| [4] | "Latent TGF-beta binding protein-3 (LTBP-3) requires binding to TGF-beta for secretion." Chen Y., Dabovic B., Annes J.P., Rifkin D.B. FEBS Lett. 517:277-280(2002) [PubMed: 12062452] [Abstract] Cited for: INTERACTION WITH TGFB1. |
| [5] | "Latent transforming growth factor-beta binding proteins (LTBPs) --structural extracellular matrix proteins for targeting TGF-beta action." Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J. Cytokine Growth Factor Rev. 10:99-117(1999) [PubMed: 10743502] [Abstract] Cited for: REVIEW. |
| [6] | "The latent transforming growth factor beta binding protein (LTBP) family." Oklu R., Hesketh R. Biochem. J. 352:601-610(2000) [PubMed: 11104663] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| L40459 mRNA. Translation: AAB53015.1. Sequence problems. AK080869 mRNA. Translation: BAC38053.1. | |
| IPI | IPI00407364. IPI00828508. |
| PIR | A57293. |
| RefSeq | NP_032546.2. |
| UniGene | Mm.182396 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BF9 based on UniProtKB P08709. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q61810. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000024940. Mus musculus. [Contig view] |
| GeneID | 16998. |
| KEGG | mmu:16998. |
Organism-specific databases | |
| MGI | MGI:1101355. Ltbp3. |
Phylogenomic databases | |
| HOGENOM | Q61810. |
| HOVERGEN | Q61810. |
Gene expression databases | |
| ArrayExpress | Q61810. |
| Bgee | Q61810. |
| GermOnline | ENSMUSG00000024940. Mus musculus. |
Family and domain databases | |
| InterPro | IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_CS. IPR000742. EGF_3. IPR001881. EGF_Ca_bd. IPR013091. EGF_Ca_bd_2. IPR018097. EGF_Ca_bd_CS. IPR002212. Fibril-assoc. IPR017878. TFG_b-bd. [Graphical view] |
| Gene3D | G3DSA:3.90.290.10. Fibril-assoc. 2 hits. |
| Pfam | PF00008. EGF. 1 hit. PF07645. EGF_CA. 11 hits. PF00683. TB. 3 hits. [Graphical view] |
| SMART | SM00181. EGF. 2 hits. SM00179. EGF_CA. 12 hits. [Graphical view] |
| PROSITE | PS00010. ASX_HYDROXYL. 10 hits. PS00022. EGF_1. 2 hits. PS01186. EGF_2. 5 hits. PS50026. EGF_3. 12 hits. PS01187. EGF_CA. 11 hits. PS51364. TB. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 291104. |
| SOURCE | Search... |
Entry information
| Entry name | LTBP3_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q61810 Secondary accession number(s): Q8BNQ6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


