Reviewed,
UniProtKB/Swiss-Prot Q8CG19 (LTBP1_MOUSE)
Last modified
July 7, 2009.
Version 68.
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 1 Short name=LTBP-1 Alternative name(s): Transforming growth factor beta-1-binding protein 1 Short name=TGF-beta1-BP-1 | ||
| 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 | 1712 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM). |
| Subunit structure | The large latent complex of TGFB1 from platelets is composed of the TGFB1 molecule non-covalently associated with a disulfide-bonded complex of a dimer of the N-terminal propeptide of the TGFB1 precursor and LTBP1. LTBP1 does not bind directly to active TGFB1. Binds to FBN1 and FBN2. Interacts with ADAMTSL2 By similarity. |
| Subcellular location | Secreted By similarity. UniProtKB Q14766 |
| Domain | Associates covalently with small latent TGF-beta complex via domain TB 3 By similarity. |
| Post-translational modification | Contains hydroxylated asparagine residues By similarity. UniProtKB P22064 The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity. |
| Sequence similarities | Belongs to the LTBP family. Contains 18 EGF-like domains. Contains 4 TB (TGF-beta binding) domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Coding sequence diversity | Alternative splicing |
| Domain | EGF-like domain Repeat Signal |
| Ligand | Growth factor binding |
| PTM | Disulfide bond Glycoprotein Hydroxylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | transforming growth factor beta receptor signaling pathway Traceable author statement. Source: MGI |
| Cellular component | proteinaceous extracellular matrix 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 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Long (identifier: Q8CG19-1) Also known as: LTBP-1L; 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 Short (identifier: Q8CG19-2) Also known as: LTBP-1S; The sequence of this isoform differs from the canonical sequence as follows: 1-318: Missing. 319-336: EGSFSLRYGQEQGTAPFQ → MDTKLMCLLFFLCLPLLL | ||||||
| Isoform 3 (identifier: Q8CG19-3) The sequence of this isoform differs from the canonical sequence as follows: 1-318: Missing. 319-336: EGSFSLRYGQEQGTAPFQ → MDTKLMCLLFFLCLPLLL 716-768: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||||
| Chain | 24 – 1712 | 1689 | Latent-transforming growth factor beta-binding protein 1 | PRO_0000007637 | |||||||
Regions | |||||||||||
| Domain | 181 – 213 | 33 | EGF-like 1 | ||||||||
| Domain | 391 – 423 | 33 | EGF-like 2 | ||||||||
| Domain | 549 – 601 | 53 | TB 1 | ||||||||
| Domain | 618 – 658 | 41 | EGF-like 3; calcium-binding Potential | ||||||||
| Domain | 669 – 721 | 53 | TB 2 | ||||||||
| Domain | 865 – 906 | 42 | EGF-like 4; calcium-binding Potential | ||||||||
| Domain | 907 – 948 | 42 | EGF-like 5; calcium-binding Potential | ||||||||
| Domain | 949 – 989 | 41 | EGF-like 6; calcium-binding Potential | ||||||||
| Domain | 990 – 1029 | 40 | EGF-like 7; calcium-binding Potential | ||||||||
| Domain | 1030 – 1070 | 41 | EGF-like 8; calcium-binding Potential | ||||||||
| Domain | 1071 – 1111 | 41 | EGF-like 9; calcium-binding Potential | ||||||||
| Domain | 1112 – 1152 | 41 | EGF-like 10; calcium-binding Potential | ||||||||
| Domain | 1153 – 1193 | 41 | EGF-like 11; calcium-binding Potential | ||||||||
| Domain | 1194 – 1235 | 42 | EGF-like 12; calcium-binding Potential | ||||||||
| Domain | 1236 – 1277 | 42 | EGF-like 13; calcium-binding Potential | ||||||||
| Domain | 1278 – 1320 | 43 | EGF-like 14; calcium-binding Potential | ||||||||
| Domain | 1338 – 1392 | 55 | TB 3 | ||||||||
| Domain | 1415 – 1457 | 43 | EGF-like 15; calcium-binding Potential | ||||||||
| Domain | 1458 – 1498 | 41 | EGF-like 16; calcium-binding Potential | ||||||||
| Domain | 1515 – 1568 | 54 | TB 4 | ||||||||
| Domain | 1612 – 1652 | 41 | EGF-like 17 | ||||||||
| Domain | 1653 – 1697 | 45 | EGF-like 18; calcium-binding Potential | ||||||||
| Compositional bias | 96 – 124 | 29 | Pro-rich | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 966 | 1 | (3R)-3-hydroxyasparagine By similarity | ||||||||
| Modified residue | 1129 | 1 | (3R)-3-hydroxyasparagine By similarity | ||||||||
| Modified residue | 1588 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 1591 | 1 | Phosphotyrosine By similarity | ||||||||
| Glycosylation | 339 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 370 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 416 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 612 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1042 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1242 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1357 | 1 | N-linked (GlcNAc...) By similarity | ||||||||
| Disulfide bond | 185 ↔ 195 | By similarity | |||||||||
| Disulfide bond | 189 ↔ 201 | By similarity | |||||||||
| Disulfide bond | 203 ↔ 212 | By similarity | |||||||||
| Disulfide bond | 395 ↔ 405 | By similarity | |||||||||
| Disulfide bond | 399 ↔ 411 | By similarity | |||||||||
| Disulfide bond | 413 ↔ 422 | By similarity | |||||||||
| Disulfide bond | 622 ↔ 633 | By similarity | |||||||||
| Disulfide bond | 628 ↔ 642 | By similarity | |||||||||
| Disulfide bond | 644 ↔ 657 | By similarity | |||||||||
| Disulfide bond | 869 ↔ 881 | By similarity | |||||||||
| Disulfide bond | 876 ↔ 890 | By similarity | |||||||||
| Disulfide bond | 892 ↔ 905 | By similarity | |||||||||
| Disulfide bond | 911 ↔ 923 | By similarity | |||||||||
| Disulfide bond | 918 ↔ 932 | By similarity | |||||||||
| Disulfide bond | 934 ↔ 947 | By similarity | |||||||||
| Disulfide bond | 953 ↔ 964 | By similarity | |||||||||
| Disulfide bond | 959 ↔ 973 | By similarity | |||||||||
| Disulfide bond | 976 ↔ 988 | By similarity | |||||||||
| Disulfide bond | 994 ↔ 1005 | By similarity | |||||||||
| Disulfide bond | 1000 ↔ 1014 | By similarity | |||||||||
| Disulfide bond | 1017 ↔ 1028 | By similarity | |||||||||
| Disulfide bond | 1034 ↔ 1045 | By similarity | |||||||||
| Disulfide bond | 1040 ↔ 1054 | By similarity | |||||||||
| Disulfide bond | 1056 ↔ 1069 | By similarity | |||||||||
| Disulfide bond | 1075 ↔ 1086 | By similarity | |||||||||
| Disulfide bond | 1081 ↔ 1095 | By similarity | |||||||||
| Disulfide bond | 1097 ↔ 1110 | By similarity | |||||||||
| Disulfide bond | 1116 ↔ 1127 | By similarity | |||||||||
| Disulfide bond | 1122 ↔ 1136 | By similarity | |||||||||
| Disulfide bond | 1138 ↔ 1151 | By similarity | |||||||||
| Disulfide bond | 1157 ↔ 1169 | By similarity | |||||||||
| Disulfide bond | 1164 ↔ 1178 | By similarity | |||||||||
| Disulfide bond | 1180 ↔ 1192 | By similarity | |||||||||
| Disulfide bond | 1198 ↔ 1210 | By similarity | |||||||||
| Disulfide bond | 1204 ↔ 1219 | By similarity | |||||||||
| Disulfide bond | 1221 ↔ 1234 | By similarity | |||||||||
| Disulfide bond | 1240 ↔ 1252 | By similarity | |||||||||
| Disulfide bond | 1246 ↔ 1261 | By similarity | |||||||||
| Disulfide bond | 1263 ↔ 1276 | By similarity | |||||||||
| Disulfide bond | 1282 ↔ 1294 | By similarity | |||||||||
| Disulfide bond | 1289 ↔ 1303 | By similarity | |||||||||
| Disulfide bond | 1305 ↔ 1319 | By similarity | |||||||||
| Disulfide bond | 1340 ↔ 1363 | By similarity | |||||||||
| Disulfide bond | 1350 ↔ 1375 | By similarity | |||||||||
| Disulfide bond | 1364 ↔ 1380 | By similarity | |||||||||
| Disulfide bond | 1365 ↔ 1392 | By similarity | |||||||||
| Disulfide bond | 1419 ↔ 1432 | By similarity | |||||||||
| Disulfide bond | 1427 ↔ 1441 | By similarity | |||||||||
| Disulfide bond | 1443 ↔ 1456 | By similarity | |||||||||
| Disulfide bond | 1462 ↔ 1473 | By similarity | |||||||||
| Disulfide bond | 1468 ↔ 1482 | By similarity | |||||||||
| Disulfide bond | 1484 ↔ 1497 | By similarity | |||||||||
| Disulfide bond | 1616 ↔ 1627 | By similarity | |||||||||
| Disulfide bond | 1622 ↔ 1636 | By similarity | |||||||||
| Disulfide bond | 1638 ↔ 1651 | By similarity | |||||||||
| Disulfide bond | 1657 ↔ 1672 | By similarity | |||||||||
| Disulfide bond | 1667 ↔ 1681 | By similarity | |||||||||
| Disulfide bond | 1683 ↔ 1696 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1 – 318 | 318 | Missing in isoform Short and isoform 3. | VSP_036968 | |||||||
| Alternative sequence | 319 – 336 | 18 | EGSFS…TAPFQ → MDTKLMCLLFFLCLPLLL in isoform Short and isoform 3. | VSP_036969 | |||||||
| Alternative sequence | 716 – 768 | 53 | Missing in isoform 3. | VSP_036970 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 313 | 1 | S → F in AAN77250. Ref.1 | ||||||||
| Sequence conflict | 506 | 1 | A → T in AAN77250. Ref.1 | ||||||||
| Sequence conflict | 506 | 1 | A → T in AAN77251. Ref.1 | ||||||||
| Sequence conflict | 506 | 1 | A → T in AAC33307. Ref.3 | ||||||||
| Sequence conflict | 559 | 1 | Q → QQ in AAN77250. Ref.1 | ||||||||
| Sequence conflict | 559 | 1 | Q → QQ in AAC33307. Ref.3 | ||||||||
| Sequence conflict | 1033 | 1 | E → K in AAC33307. Ref.3 | ||||||||
| Sequence conflict | 1111 | 1 | E → G in BAC34222. Ref.6 | ||||||||
| Sequence conflict | 1216 | 1 | S → F in BAC34222. Ref.6 | ||||||||
| Sequence conflict | 1631 | 1 | Q → H in AAN77250. Ref.1 | ||||||||
| Sequence conflict | 1631 | 1 | Q → H in AAN77251. Ref.1 | ||||||||
| Sequence conflict | 1659 | 1 | E → G in BAC34222. Ref.6 | ||||||||
| Sequence conflict | 1712 | 1 | E → N in AAC33307. Ref.3 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of the mouse Ltbp-1 gene reveals tissue specific expression of alternatively spliced forms." Noguera I., Obata H., Gualandris A., Cowin P., Rifkin D.B. Gene 308:31-41(2003) [PubMed: 12711388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS LONG AND SHORT). |
| [2] | "The murine latent transforming growth factor-beta binding protein (Ltbp-1) is alternatively spliced, and maps to a region syntenic to human chromosome 2p21-22." Weiskirchen R., Moser M., Guenther K., Weiskirchen S., Gressner A.M. Gene 308:43-52(2003) [PubMed: 12711389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. Strain: 129/SvJ. |
| [3] | Noguera I., Cowin P., Rifkin D.B. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). Strain: BALB/c. Tissue: Heart. |
| [4] | The mouse genome sequencing consortium Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). Strain: C57BL/6. Tissue: Brain. |
| [6] | "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] OF 1111-1712. Strain: C57BL/6J. Tissue: Aorta, Liver and Vein. |
| [7] | "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. |
| [8] | "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 | |
|---|---|
AF346465 AF346464 Genomic DNA. Translation: AAN77250.1. AF346465 AF346464 Genomic DNA. Translation: AAN77251.1. AY143161 Genomic DNA. Translation: AAN38831.1. AF022889 mRNA. Translation: AAC33307.1. CT033758 AC154491 Genomic DNA. Translation: CAM24102.1. CT033758, AC118018, AC154491 Genomic DNA. Translation: CAM24104.1. CT033758, AC118018, AC154491 Genomic DNA. Translation: CAM24103.1. BC094612 mRNA. Translation: AAH94612.1. AK050380 mRNA. Translation: BAC34222.1. AK080024 mRNA. Translation: BAC37808.1. | |
| IPI | IPI00352982. IPI00828560. IPI00830551. |
| RefSeq | NP_064303.2. NP_996841.1. |
| UniGene | Mm.269747 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BF9 based on UniProtKB P08709. |
| SMR | Q8CG19. Positions 1333-1404. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q8CG19. 1 interaction. |
PTM databases | |
| PhosphoSite | Q8CG19. |
Proteomic databases | |
| PRIDE | Q8CG19. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000001870. Mus musculus. [Contig view] |
| GeneID | 268977. |
Organism-specific databases | |
| MGI | MGI:109151. Ltbp1. |
Phylogenomic databases | |
| HOGENOM | Q8CG19. |
| HOVERGEN | Q8CG19. |
Gene expression databases | |
| ArrayExpress | Q8CG19. |
| Bgee | Q8CG19. |
| GermOnline | ENSMUSG00000001870. 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. IPR013111. EGF_extracell. IPR002212. Fibril-assoc. IPR017878. TFG_b-bd. [Graphical view] |
| Gene3D | G3DSA:3.90.290.10. Fibril-assoc. 3 hits. |
| Pfam | PF00008. EGF. 4 hits. PF07974. EGF_2. 1 hit. PF07645. EGF_CA. 11 hits. PF00683. TB. 4 hits. [Graphical view] |
| SMART | SM00181. EGF. 5 hits. SM00179. EGF_CA. 13 hits. [Graphical view] |
| PROSITE | PS00010. ASX_HYDROXYL. 13 hits. PS00022. EGF_1. 2 hits. PS01186. EGF_2. 11 hits. PS50026. EGF_3. 14 hits. PS01187. EGF_CA. 15 hits. PS51364. TB. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | LTBP1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8CG19 Secondary accession number(s): B1B1D9 Q8CIR0 | ||||||||
| 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


