O08999 (LTBP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 115.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Latent-transforming growth factor beta-binding protein 2 Short name=LTBP-2 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1813 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 play an integral structural role in elastic-fiber architectural organization and/or assembly. May be involved in the assembly, secretion and targeting of TGF- beta to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGF-beta. May have a structural role in the extra cellular matrix (ECM). |
| Subunit structure | Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4 By similarity. Ref.1 |
| Subcellular location | Secreted By similarity. Note: Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers By similarity. |
| Tissue specificity | Expressed in the anterior chamber of the eye. Ref.7 |
| Domain | Associates covalently with small latent TGF-beta complex via Repeat B and Repeat C. |
| Post-translational modification | Contains hydroxylated asparagine residues By similarity. |
| Sequence similarities | Belongs to the LTBP family. Contains 20 EGF-like domains. Contains 4 TB (TGF-beta binding) domains. |
| Sequence caution | The sequence AAB61611.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC35229.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | EGF-like domain Repeat Signal |
| Ligand | Growth factor binding Heparin-binding |
| PTM | Disulfide bond Glycoprotein Hydroxylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | calcium ion binding Inferred from electronic annotation. Source: InterPro heparin bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 35 | 35 | Potential | ||||||||
| Chain | 36 – 1813 | 1778 | Latent-transforming growth factor beta-binding protein 2 | PRO_0000007644 | |||||||
Regions | |||||||||||
| Domain | 181 – 213 | 33 | EGF-like 1 | ||||||||
| Domain | 381 – 413 | 33 | EGF-like 2 | ||||||||
| Domain | 536 – 588 | 53 | TB 1 | ||||||||
| Domain | 609 – 649 | 41 | EGF-like 3; calcium-binding Potential | ||||||||
| Domain | 659 – 711 | 53 | TB 2 | ||||||||
| Domain | 835 – 877 | 43 | EGF-like 4 | ||||||||
| Domain | 878 – 920 | 43 | EGF-like 5; calcium-binding Potential | ||||||||
| Domain | 921 – 960 | 40 | EGF-like 6; calcium-binding Potential | ||||||||
| Domain | 961 – 1000 | 40 | EGF-like 7; calcium-binding Potential | ||||||||
| Domain | 1001 – 1041 | 41 | EGF-like 8; calcium-binding Potential | ||||||||
| Domain | 1042 – 1083 | 42 | EGF-like 9; calcium-binding Potential | ||||||||
| Domain | 1084 – 1125 | 42 | EGF-like 10; calcium-binding Potential | ||||||||
| Domain | 1126 – 1166 | 41 | EGF-like 11; calcium-binding Potential | ||||||||
| Domain | 1167 – 1208 | 42 | EGF-like 12; calcium-binding Potential | ||||||||
| Domain | 1209 – 1250 | 42 | EGF-like 13; calcium-binding Potential | ||||||||
| Domain | 1251 – 1294 | 44 | EGF-like 14; calcium-binding Potential | ||||||||
| Domain | 1295 – 1336 | 42 | EGF-like 15; calcium-binding Potential | ||||||||
| Domain | 1337 – 1379 | 43 | EGF-like 16; calcium-binding Potential | ||||||||
| Domain | 1403 – 1455 | 53 | TB 3 | ||||||||
| Domain | 1477 – 1519 | 43 | EGF-like 17; calcium-binding Potential | ||||||||
| Domain | 1520 – 1559 | 40 | EGF-like 18; calcium-binding Potential | ||||||||
| Domain | 1576 – 1628 | 53 | TB 4 | ||||||||
| Domain | 1725 – 1765 | 41 | EGF-like 19; calcium-binding Potential | ||||||||
| Domain | 1766 – 1810 | 45 | EGF-like 20; calcium-binding Potential | ||||||||
| Region | 94 – 115 | 22 | Heparin-binding By similarity | ||||||||
| Region | 226 – 243 | 18 | Heparin-binding By similarity | ||||||||
| Region | 329 – 339 | 11 | Heparin-binding By similarity | ||||||||
| Compositional bias | 847 – 1364 | 518 | Cys-rich | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 491 | 1 | Phosphoserine Ref.6 | ||||||||
| Glycosylation | 175 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 328 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 406 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 603 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1161 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1301 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1422 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1560 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 185 ↔ 195 | By similarity | |||||||||
| Disulfide bond | 189 ↔ 201 | By similarity | |||||||||
| Disulfide bond | 203 ↔ 212 | By similarity | |||||||||
| Disulfide bond | 385 ↔ 395 | By similarity | |||||||||
| Disulfide bond | 389 ↔ 401 | By similarity | |||||||||
| Disulfide bond | 403 ↔ 412 | By similarity | |||||||||
| Disulfide bond | 613 ↔ 624 | By similarity | |||||||||
| Disulfide bond | 619 ↔ 633 | By similarity | |||||||||
| Disulfide bond | 635 ↔ 648 | By similarity | |||||||||
| Disulfide bond | 839 ↔ 852 | By similarity | |||||||||
| Disulfide bond | 847 ↔ 861 | By similarity | |||||||||
| Disulfide bond | 863 ↔ 876 | By similarity | |||||||||
| Disulfide bond | 882 ↔ 893 | By similarity | |||||||||
| Disulfide bond | 887 ↔ 902 | By similarity | |||||||||
| Disulfide bond | 904 ↔ 919 | By similarity | |||||||||
| Disulfide bond | 925 ↔ 936 | By similarity | |||||||||
| Disulfide bond | 931 ↔ 945 | By similarity | |||||||||
| Disulfide bond | 947 ↔ 959 | By similarity | |||||||||
| Disulfide bond | 965 ↔ 976 | By similarity | |||||||||
| Disulfide bond | 971 ↔ 985 | By similarity | |||||||||
| Disulfide bond | 988 ↔ 999 | By similarity | |||||||||
| Disulfide bond | 1005 ↔ 1016 | By similarity | |||||||||
| Disulfide bond | 1011 ↔ 1025 | By similarity | |||||||||
| Disulfide bond | 1027 ↔ 1040 | By similarity | |||||||||
| Disulfide bond | 1046 ↔ 1057 | By similarity | |||||||||
| Disulfide bond | 1052 ↔ 1066 | By similarity | |||||||||
| Disulfide bond | 1069 ↔ 1082 | By similarity | |||||||||
| Disulfide bond | 1088 ↔ 1099 | By similarity | |||||||||
| Disulfide bond | 1094 ↔ 1108 | By similarity | |||||||||
| Disulfide bond | 1111 ↔ 1124 | By similarity | |||||||||
| Disulfide bond | 1130 ↔ 1142 | By similarity | |||||||||
| Disulfide bond | 1137 ↔ 1151 | By similarity | |||||||||
| Disulfide bond | 1153 ↔ 1165 | By similarity | |||||||||
| Disulfide bond | 1171 ↔ 1183 | By similarity | |||||||||
| Disulfide bond | 1177 ↔ 1192 | By similarity | |||||||||
| Disulfide bond | 1194 ↔ 1207 | By similarity | |||||||||
| Disulfide bond | 1213 ↔ 1224 | By similarity | |||||||||
| Disulfide bond | 1219 ↔ 1233 | By similarity | |||||||||
| Disulfide bond | 1235 ↔ 1249 | By similarity | |||||||||
| Disulfide bond | 1255 ↔ 1268 | By similarity | |||||||||
| Disulfide bond | 1263 ↔ 1277 | By similarity | |||||||||
| Disulfide bond | 1281 ↔ 1293 | By similarity | |||||||||
| Disulfide bond | 1299 ↔ 1311 | By similarity | |||||||||
| Disulfide bond | 1305 ↔ 1320 | By similarity | |||||||||
| Disulfide bond | 1322 ↔ 1335 | By similarity | |||||||||
| Disulfide bond | 1341 ↔ 1353 | By similarity | |||||||||
| Disulfide bond | 1348 ↔ 1362 | By similarity | |||||||||
| Disulfide bond | 1364 ↔ 1378 | By similarity | |||||||||
| Disulfide bond | 1481 ↔ 1494 | By similarity | |||||||||
| Disulfide bond | 1489 ↔ 1503 | By similarity | |||||||||
| Disulfide bond | 1505 ↔ 1518 | By similarity | |||||||||
| Disulfide bond | 1524 ↔ 1534 | By similarity | |||||||||
| Disulfide bond | 1529 ↔ 1543 | By similarity | |||||||||
| Disulfide bond | 1545 ↔ 1558 | By similarity | |||||||||
| Disulfide bond | 1729 ↔ 1740 | By similarity | |||||||||
| Disulfide bond | 1735 ↔ 1749 | By similarity | |||||||||
| Disulfide bond | 1751 ↔ 1764 | By similarity | |||||||||
| Disulfide bond | 1770 ↔ 1785 | By similarity | |||||||||
| Disulfide bond | 1780 ↔ 1794 | By similarity | |||||||||
| Disulfide bond | 1796 ↔ 1809 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 14 | 1 | Q → R in BAC35229. Ref.2 | ||||||||
| Sequence conflict | 74 | 1 | E → G in BAC35229. Ref.2 | ||||||||
| Sequence conflict | 97 | 1 | W → R in BAC35229. Ref.2 | ||||||||
| Sequence conflict | 498 | 1 | H → R in BAC35229. Ref.2 | ||||||||
| Sequence conflict | 553 | 1 | S → E in BAC35229. Ref.2 | ||||||||
| Sequence conflict | 580 – 582 | 3 | Missing in BAC35229. Ref.2 | ||||||||
| Sequence conflict | 778 | 1 | D → L in BAC35229. Ref.2 | ||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TGFB1. |
| [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-778. Strain: C57BL/6J. Tissue: Head. |
| [3] | Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 205-211, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus. |
| [4] | "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] [Europe PMC] [Abstract] Cited for: REVIEW. |
| [5] | "The latent transforming growth factor beta binding protein (LTBP) family." Oklu R., Hesketh R. Biochem. J. 352:601-610(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW. |
| [6] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, MASS SPECTROMETRY. Tissue: Melanoma. |
| [7] | "Null mutations in LTBP2 cause primary congenital glaucoma." Ali M., McKibbin M., Booth A., Parry D.A., Jain P., Riazuddin S.A., Hejtmancik J.F., Khan S.N., Firasat S., Shires M., Gilmour D.F., Towns K., Murphy A.L., Azmanov D., Tournev I., Cherninkova S., Jafri H., Raashid Y. Inglehearn C.F.Am. J. Hum. Genet. 84:664-671(2009) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF004874 mRNA. Translation: AAB61611.1. Different initiation. AK052980 mRNA. Translation: BAC35229.1. Different initiation. |
| IPI | IPI00874393. |
| RefSeq | NP_038617.3. NM_013589.3. |
| UniGene | Mm.3900. |
3D structure databases | |
| ProteinModelPortal | O08999. |
| SMR | O08999. Positions 146-215, 536-717, 854-1558, 1727-1811. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-4100636. |
PTM databases | |
| PhosphoSite | O08999. |
Proteomic databases | |
| PaxDb | O08999. |
| PRIDE | O08999. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 16997. |
| KEGG | mmu:16997. |
Organism-specific databases | |
| CTD | 4053. |
| MGI | MGI:99502. Ltbp2. |
Phylogenomic databases | |
| eggNOG | NOG318792. |
| HOGENOM | HOG000293153. |
| HOVERGEN | HBG052370. |
| InParanoid | O08999. |
| KO | K08023. |
Gene expression databases | |
| Genevestigator | O08999. |
| GermOnline | ENSMUSG00000002020. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.90.290.10. 5 hits. |
| InterPro | IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR009030. Growth_fac_rcpt_N_dom. IPR017878. TB_dom. [Graphical view] |
| Pfam | PF00008. EGF. 1 hit. PF07645. EGF_CA. 15 hits. PF00683. TB. 4 hits. [Graphical view] |
| SMART | SM00181. EGF. 4 hits. SM00179. EGF_CA. 16 hits. [Graphical view] |
| SUPFAM | SSF57581. Fibril-assoc. 4 hits. SSF57184. Grow_fac_recept. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00010. ASX_HYDROXYL. 12 hits. PS00022. EGF_1. 2 hits. PS01186. EGF_2. 10 hits. PS50026. EGF_3. 15 hits. PS01187. EGF_CA. 16 hits. PS51364. TB. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | LTBP2. mouse. |
| NextBio | 291100. |
| SOURCE | Search... |
Entry information
| Entry name | LTBP2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O08999 Secondary accession number(s): Q8C6W9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
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
