Q9JM99 (PRG4_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 87.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Proteoglycan 4 Alternative name(s): Lubricin Megakaryocyte-stimulating factor Superficial zone proteoglycan Cleaved into the following chain: | ||||
| Gene names |
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| 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 | 1054 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 | Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface. Ref.3 |
| Subunit structure | Homodimer; disulfide-linked. Ref.4 |
| Subcellular location | Secreted By similarity. |
| Tissue specificity | Highly expressed in cartilage, bone and liver and weakly expressed in heart, brain and muscle. Expressed in the surface chondrocytes and in synovial intimal cells. Isoform B is expressed in bone, small intestine, muscle, testis, heart, liver and lung. Isoform C and isoform D are widely expressed. Ref.1 Ref.3 |
| Developmental stage | First detected at the forming joint surface from E15.5, after cavitation has begun. At later stages of morphogenesis, strong expression is observed in cartilage surface cells (superficial zone chondocytes) and in the newly forming synovium. Ref.3 |
| Post-translational modification | N-glycosylated By similarity. O-glycosylated; contains glycosaminoglycan chondroitin sulfate and keratan sulfate By similarity. The disulfide bond between Cys-795 and Cys-1053 is essential for protein cleavage. |
| Disruption phenotype | Mice are viable and fertile. In the newborn period, their joints appear normal. The aged mice exhibit abnormal protein deposits on the cartilage surface and disappearance of underlying superficial zone chondrocytes. In addition to cartilage surface changes and subsequent cartilage deterioration, intimal cells in the synovium surrounding the joint space become hyperplastic, which further contribute to joint failure. Ref.3 |
| Miscellaneous | Different forms varying in molecular weight have been observed. Such forms are possibly due to different levels of glycosylation and protein cleavage. |
| Sequence similarities | Contains 2 hemopexin-like domains. Contains 2 SMB (somatomedin-B) domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat Signal |
| PTM | Disulfide bond Glycoprotein Proteoglycan |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | hematopoietic stem cell proliferation Inferred from mutant phenotype PubMed 21939632. Source: MGI immune responseInferred from electronic annotation. Source: InterPro negative regulation of interleukin-6 biosynthetic processInferred from mutant phenotype PubMed 21939632. Source: MGI regulation of cell proliferationInferred from mutant phenotype Ref.3. Source: MGI |
| Cellular_component | extracellular space Inferred from direct assay Ref.3. Source: MGI |
| Molecular_function | polysaccharide binding Inferred from electronic annotation. Source: InterPro scavenger receptor activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform A (identifier: Q9JM99-1) 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 B (identifier: Q9JM99-2) The sequence of this isoform differs from the canonical sequence as follows: 26-66: Missing. | ||||||
| Isoform C (identifier: Q9JM99-3) The sequence of this isoform differs from the canonical sequence as follows: 107-194: Missing. | ||||||
| Isoform D (identifier: Q9JM99-4) The sequence of this isoform differs from the canonical sequence as follows: 26-66: Missing. 107-194: Missing. | ||||||
| Isoform E (identifier: Q9JM99-5) The sequence of this isoform differs from the canonical sequence as follows: 107-194: Missing. 224-766: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Potential | ||||||||
| Chain | 25 – 1054 | 1030 | Proteoglycan 4 | PRO_0000043234 | |||||||
| Chain | 956 – 1054 | 99 | Proteoglycan 4 C-terminal part | PRO_0000043235 | |||||||
Regions | |||||||||||
| Domain | 26 – 69 | 44 | SMB 1 | ||||||||
| Domain | 66 – 108 | 43 | SMB 2 | ||||||||
| Repeat | 317 – 324 | 8 | 1; approximate | ||||||||
| Repeat | 325 – 332 | 8 | 2; approximate | ||||||||
| Repeat | 333 – 340 | 8 | 3; approximate | ||||||||
| Repeat | 349 – 356 | 8 | 4; approximate | ||||||||
| Repeat | 357 – 364 | 8 | 5 | ||||||||
| Repeat | 365 – 371 | 7 | 6; approximate | ||||||||
| Repeat | 372 – 379 | 8 | 7 | ||||||||
| Repeat | 380 – 387 | 8 | 8 | ||||||||
| Repeat | 388 – 395 | 8 | 9 | ||||||||
| Repeat | 396 – 403 | 8 | 10 | ||||||||
| Repeat | 404 – 411 | 8 | 11 | ||||||||
| Repeat | 412 – 418 | 7 | 12; approximate | ||||||||
| Repeat | 419 – 426 | 8 | 13 | ||||||||
| Repeat | 427 – 434 | 8 | 14 | ||||||||
| Repeat | 435 – 442 | 8 | 15 | ||||||||
| Repeat | 443 – 450 | 8 | 16; approximate | ||||||||
| Repeat | 451 – 458 | 8 | 17 | ||||||||
| Repeat | 459 – 466 | 8 | 18 | ||||||||
| Repeat | 467 – 474 | 8 | 19 | ||||||||
| Repeat | 475 – 482 | 8 | 20 | ||||||||
| Repeat | 483 – 490 | 8 | 21 | ||||||||
| Repeat | 491 – 498 | 8 | 22 | ||||||||
| Repeat | 499 – 506 | 8 | 23 | ||||||||
| Repeat | 507 – 514 | 8 | 24 | ||||||||
| Repeat | 515 – 522 | 8 | 25 | ||||||||
| Repeat | 523 – 530 | 8 | 26 | ||||||||
| Repeat | 531 – 538 | 8 | 27 | ||||||||
| Repeat | 539 – 546 | 8 | 28 | ||||||||
| Repeat | 547 – 554 | 8 | 29 | ||||||||
| Repeat | 555 – 562 | 8 | 30 | ||||||||
| Repeat | 563 – 570 | 8 | 31 | ||||||||
| Repeat | 571 – 578 | 8 | 32 | ||||||||
| Repeat | 579 – 586 | 8 | 33 | ||||||||
| Repeat | 587 – 594 | 8 | 34 | ||||||||
| Repeat | 595 – 602 | 8 | 35 | ||||||||
| Repeat | 603 – 610 | 8 | 36 | ||||||||
| Repeat | 611 – 618 | 8 | 37 | ||||||||
| Domain | 800 – 842 | 43 | Hemopexin-like 1 | ||||||||
| Domain | 844 – 890 | 47 | Hemopexin-like 2 | ||||||||
| Region | 317 – 618 | 302 | 37 X 8 AA repeats of K-X-P-X-P-T-T-X | ||||||||
| Compositional bias | 157 – 184 | 28 | Ser-rich | ||||||||
| Compositional bias | 350 – 606 | 257 | Glu-rich | ||||||||
| Compositional bias | 659 – 699 | 41 | Lys-rich | ||||||||
Sites | |||||||||||
| Site | 955 – 956 | 2 | Cleavage; by subtilisin-like proprotein convertase 4 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 109 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 938 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 30 ↔ 46 | Alternate By similarity | |||||||||
| Disulfide bond | 30 ↔ 34 | By similarity | |||||||||
| Disulfide bond | 34 ↔ 64 | Alternate By similarity | |||||||||
| Disulfide bond | 44 ↔ 57 | Alternate By similarity | |||||||||
| Disulfide bond | 44 ↔ 46 | By similarity | |||||||||
| Disulfide bond | 50 ↔ 56 | By similarity | |||||||||
| Disulfide bond | 57 ↔ 64 | By similarity | |||||||||
| Disulfide bond | 70 ↔ 86 | Alternate By similarity | |||||||||
| Disulfide bond | 70 ↔ 74 | By similarity | |||||||||
| Disulfide bond | 74 ↔ 104 | Alternate By similarity | |||||||||
| Disulfide bond | 84 ↔ 97 | Alternate By similarity | |||||||||
| Disulfide bond | 84 ↔ 86 | By similarity | |||||||||
| Disulfide bond | 90 ↔ 96 | By similarity | |||||||||
| Disulfide bond | 97 ↔ 104 | By similarity | |||||||||
| Disulfide bond | 795 ↔ 1053 | Ref.4 | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 26 – 66 | 41 | Missing in isoform B and isoform D. | VSP_016471 | |||||||
| Alternative sequence | 107 – 194 | 88 | Missing in isoform C, isoform D and isoform E. | VSP_016472 | |||||||
| Alternative sequence | 224 – 766 | 543 | Missing in isoform E. | VSP_016473 | |||||||
Experimental info | |||||||||||
| Mutagenesis | 795 | 1 | C → A: Not cleaved by subtilisin-like proprotein convertase. Not cleaved by subtilisin-like proprotein convertase; when associated with A-1053. Ref.4 | ||||||||
| Mutagenesis | 851 – 853 | 3 | CNC → ANA: Cleaved by subtilisin-like proprotein convertase. Ref.4 | ||||||||
| Mutagenesis | 851 | 1 | C → A: Cleaved by subtilisin-like proprotein convertase. | ||||||||
| Mutagenesis | 930 | 1 | C → A: Cleaved by subtilisin-like proprotein convertase. Ref.4 | ||||||||
| Mutagenesis | 949 – 955 | 7 | RRRRFER → ARARFEA: Not cleaved by subtilisin-like proprotein convertase 4. Ref.4 | ||||||||
| Mutagenesis | 949 – 951 | 3 | RRR → ARA: Cleaved by subtilisin-like proprotein convertase 4. Ref.4 | ||||||||
| Mutagenesis | 955 | 1 | R → A: Not cleaved by subtilisin-like proprotein convertase 4. | ||||||||
| Mutagenesis | 1053 | 1 | C → A: Not cleaved by subtilisin-like proprotein convertase 4. Not cleaved by subtilisin-like proprotein convertase; when associated with A-795. Ref.4 | ||||||||
| Sequence conflict | 65 – 66 | 2 | SP → TT in BAE28900. Ref.2 | ||||||||
| Sequence conflict | 703 | 1 | S → A in BAA92310. Ref.1 | ||||||||
| Sequence conflict | 780 | 1 | Q → R in BAA92310. Ref.1 | ||||||||
| Sequence conflict | 788 | 1 | L → P in BAA92310. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation, characterization and mapping of the mouse and human PRG4 (proteoglycan 4) genes." Ikegawa S., Sano M., Koshizuka Y., Nakamura Y. Cytogenet. Cell Genet. 90:291-297(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, IDENTIFICATION OF ISOFORMS B; C AND D. |
| [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] (ISOFORM E), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-1054. Strain: C57BL/6J. Tissue: Head and Liver. |
| [3] | "The secreted glycoprotein lubricin protects cartilage surfaces and inhibits synovial cell overgrowth." Rhee D.K., Marcelino J., Baker M., Gong Y., Smits P., Lefebvre V., Jay G.D., Stewart M., Wang H., Warman M.L., Carpten J.D. J. Clin. Invest. 115:622-631(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. |
| [4] | "Consequences of disease-causing mutations on lubricin protein synthesis, secretion, and post-translational processing." Rhee D.K., Marcelino J., Al-Mayouf S., Schelling D.K., Bartels C.F., Cui Y., Laxer R., Goldbach-Mansky R., Warman M.L. J. Biol. Chem. 280:31325-31332(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, DISULFIDE BOND, MUTAGENESIS OF 949-ARG--ARG-955; 949-ARG--ARG-951; CYS-795; 851-CYS--CYS-853; CYS-930 AND CYS-1053. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB034730 mRNA. Translation: BAA92310.1. AK132597 mRNA. Translation: BAE21253.1. AK149469 mRNA. Translation: BAE28900.1. |
| IPI | IPI00652394. IPI00656174. IPI00656236. IPI00656272. IPI00656304. |
| RefSeq | NP_001103616.1. NM_001110146.1. |
| UniGene | Mm.174256. Mm.329131. |
3D structure databases | |
| ProteinModelPortal | Q9JM99. |
| SMR | Q9JM99. Positions 26-105, 793-929. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q9JM99. |
Proteomic databases | |
| PaxDb | Q9JM99. |
| PRIDE | Q9JM99. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000006171; ENSMUSP00000006171; ENSMUSG00000006014. ENSMUST00000162367; ENSMUSP00000125551; ENSMUSG00000006014. |
| GeneID | 96875. |
| KEGG | mmu:96875. |
Organism-specific databases | |
| CTD | 10216. |
| MGI | MGI:1891344. Prg4. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| GeneTree | ENSGT00530000063751. |
| HOGENOM | HOG000115691. |
| HOVERGEN | HBG101613. |
| InParanoid | Q9JM99. |
| OrthoDB | EOG4JM7QM. |
Gene expression databases | |
| ArrayExpress | Q9JM99. |
| Bgee | Q9JM99. |
| Genevestigator | Q9JM99. |
| GermOnline | ENSMUSG00000006014. Mus musculus. |
Family and domain databases | |
| Gene3D | 2.110.10.10. 2 hits. |
| InterPro | IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR018486. Hemopexin_CS. IPR020436. Somatomedin_B_chordata. IPR001212. Somatomedin_B_dom. [Graphical view] |
| Pfam | PF00045. Hemopexin. 2 hits. PF01033. Somatomedin_B. 2 hits. [Graphical view] |
| PRINTS | PR00022. SOMATOMEDINB. |
| SMART | SM00120. HX. 2 hits. SM00201. SO. 2 hits. [Graphical view] |
| SUPFAM | SSF50923. Hemopexin. 1 hit. |
| PROSITE | PS00024. HEMOPEXIN. 1 hit. PS00524. SMB_1. 2 hits. PS50958. SMB_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 352339. |
| SOURCE | Search... |
Entry information
| Entry name | PRG4_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9JM99 Secondary accession number(s): Q3UEL1, Q3V198 | ||||||||
| 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
