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Q9JM99 (PRG4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteoglycan 4
Alternative name(s):
Lubricin
Megakaryocyte-stimulating factor
Superficial zone proteoglycan

Cleaved into the following chain:

  1. Proteoglycan 4 C-terminal part
Gene names
Name:Prg4
Synonyms:Msf, Szp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1054 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 repeats.

Contains 2 SMB (somatomedin-B) domains.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 10541030Proteoglycan 4
PRO_0000043234
Chain956 – 105499Proteoglycan 4 C-terminal part
PRO_0000043235

Regions

Domain26 – 6944SMB 1
Domain66 – 10843SMB 2
Repeat317 – 32481; approximate
Repeat325 – 33282; approximate
Repeat333 – 34083; approximate
Repeat349 – 35684; approximate
Repeat357 – 36485
Repeat365 – 37176; approximate
Repeat372 – 37987
Repeat380 – 38788
Repeat388 – 39589
Repeat396 – 403810
Repeat404 – 411811
Repeat412 – 418712; approximate
Repeat419 – 426813
Repeat427 – 434814
Repeat435 – 442815
Repeat443 – 450816; approximate
Repeat451 – 458817
Repeat459 – 466818
Repeat467 – 474819
Repeat475 – 482820
Repeat483 – 490821
Repeat491 – 498822
Repeat499 – 506823
Repeat507 – 514824
Repeat515 – 522825
Repeat523 – 530826
Repeat531 – 538827
Repeat539 – 546828
Repeat547 – 554829
Repeat555 – 562830
Repeat563 – 570831
Repeat571 – 578832
Repeat579 – 586833
Repeat587 – 594834
Repeat595 – 602835
Repeat603 – 610836
Repeat611 – 618837
Repeat797 – 84044Hemopexin 1
Repeat841 – 88848Hemopexin 2
Region317 – 61830237 X 8 AA repeats of K-X-P-X-P-T-T-X
Compositional bias157 – 18428Ser-rich
Compositional bias350 – 606257Glu-rich
Compositional bias659 – 69941Lys-rich

Sites

Site955 – 9562Cleavage; by subtilisin-like proprotein convertase 4

Amino acid modifications

Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation9381N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 46Alternate By similarity
Disulfide bond30 ↔ 34 By similarity
Disulfide bond34 ↔ 64Alternate By similarity
Disulfide bond44 ↔ 57Alternate By similarity
Disulfide bond44 ↔ 46 By similarity
Disulfide bond50 ↔ 56 By similarity
Disulfide bond57 ↔ 64 By similarity
Disulfide bond70 ↔ 86Alternate By similarity
Disulfide bond70 ↔ 74 By similarity
Disulfide bond74 ↔ 104Alternate By similarity
Disulfide bond84 ↔ 97Alternate By similarity
Disulfide bond84 ↔ 86 By similarity
Disulfide bond90 ↔ 96 By similarity
Disulfide bond97 ↔ 104 By similarity
Disulfide bond795 ↔ 1053 Ref.4

Natural variations

Alternative sequence26 – 6641Missing in isoform B and isoform D.
VSP_016471
Alternative sequence107 – 19488Missing in isoform C, isoform D and isoform E.
VSP_016472
Alternative sequence224 – 766543Missing in isoform E.
VSP_016473

Experimental info

Mutagenesis7951C → A: Not cleaved by subtilisin-like proprotein convertase. Not cleaved by subtilisin-like proprotein convertase; when associated with A-1053. Ref.4
Mutagenesis851 – 8533CNC → ANA: Cleaved by subtilisin-like proprotein convertase. Ref.4
Mutagenesis8511C → A: Cleaved by subtilisin-like proprotein convertase.
Mutagenesis9301C → A: Cleaved by subtilisin-like proprotein convertase. Ref.4
Mutagenesis949 – 9557RRRRFER → ARARFEA: Not cleaved by subtilisin-like proprotein convertase 4. Ref.4
Mutagenesis949 – 9513RRR → ARA: Cleaved by subtilisin-like proprotein convertase 4. Ref.4
Mutagenesis9551R → A: Not cleaved by subtilisin-like proprotein convertase 4.
Mutagenesis10531C → A: Not cleaved by subtilisin-like proprotein convertase 4. Not cleaved by subtilisin-like proprotein convertase; when associated with A-795. Ref.4
Sequence conflict65 – 662SP → TT in BAE28900. Ref.2
Sequence conflict7031S → A in BAA92310. Ref.1
Sequence conflict7801Q → R in BAA92310. Ref.1
Sequence conflict7881L → P in BAA92310. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 13312FB7070DF2A4

FASTA1,054115,996
        10         20         30         40         50         60 
MGWKILPVCL SLLLPVVLIQ QVSSQDLSSC AGRCGEGYSR DATCNCDYNC QHYMECCPDF 

        70         80         90        100        110        120 
KRVCSPELSC KGRCFESFAR GRECDCDSQC KQYGKCCADY DSFCEEVHNS TSPSSKTAPT 

       130        140        150        160        170        180 
PAGASDTIKS TTKRSPKSPT TRTIKVVESE ELTEEHSDSE NQESSSSSSS SSSTIRKIKS 

       190        200        210        220        230        240 
SKNSANRELQ KNPNVKDNKK NTPKKKPNPE PPAVDEAGSG LDNGEFKLTP PPPDPPTTPH 

       250        260        270        280        290        300 
SKVATSPKTT AAKPVTPKPS LAPNSETSKE ASLASNKETT VETKETTATN KQSSASKKKT 

       310        320        330        340        350        360 
TSVKETRSAE KTSDKDVEPT STTPKNSAPT TTKKPVTTTK ESKFLPLPQE PEPTTAKEPP 

       370        380        390        400        410        420 
PTTKKPEPTT RKEPEPTTPK EPEPTTPKEP EPTTPKEPEP TTPKEPPPTT KKPEPTTPKE 

       430        440        450        460        470        480 
PGPTTPKEPE PTTTKEPEPT TTKEPESTTR KEPEPTTPKE PEPTTPKEPE PTTLKEPEPT 

       490        500        510        520        530        540 
TPKEPEPTTP KEPEPTTPKE PEPTTPKEPE PTTPKEPEPT TPKEPEPTTP KEPEPTTPKE 

       550        560        570        580        590        600 
PEPTTPKKPE PTTPKEPVPT TPKEPEPTTP KEPEPTTPKE PEPTTRKEPE PTTPKEPEPT 

       610        620        630        640        650        660 
TPKEPEPTTP KKPEPTTTSP KTTTLKATTL APKVTAPAEE IQNKPEETTP ASEDSDDSKT 

       670        680        690        700        710        720 
TLKPQKPTKA PKPTKKPTKA PKKPTSTKKP KTPKTRKPKT TPSPLKTTSA TPELNTTPLE 

       730        740        750        760        770        780 
VMLPTTTIPK QTPNPETAEV NPDHEDADGG EGEKPLIPGP PVLFPTAIPG TDLLAGRLNQ 

       790        800        810        820        830        840 
GININPMLSD ETNLCNGKPV DGLTTLRNGT LVAFRGHYFW MLNPFRPPSP PRRITEVWGI 

       850        860        870        880        890        900 
PSPIDTVFTR CNCEGKTFFF KDSQYWRFTN DVVDPGYPKQ IVKGFGGLTG KIVAALSIAK 

       910        920        930        940        950        960 
YKDRPESVYF FKRGGNIQQY TYKQEPMKKC TGRRPAINYS VYGEAAQVRR RRFERAVGPF 

       970        980        990       1000       1010       1020 
QTHTFRIHYS VPMRVSYQDK GFLHNEVKVS TMWRGFPNVV TSAITLPNIR KPDGYDYYAF 

      1030       1040       1050 
SKDQYYNIDV PTRTARAITT RSGQTLSKIW YNCP 

« Hide

Isoform B [UniParc].

Checksum: 49334633D98BD1E4
Show »

FASTA1,013111,425
Isoform C [UniParc].

Checksum: 123569A1FABFC5BD
Show »

FASTA966106,637
Isoform D [UniParc].

Checksum: 1CD5556F5467CD48
Show »

FASTA925102,066
Isoform E [UniParc].

Checksum: EBC6B86287506E4C
Show »

FASTA42347,989

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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
RefSeqNP_001103616.1. NM_001110146.1.
UniGeneMm.174256.
Mm.329131.

3D structure databases

ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9JM99.

Proteomic databases

PaxDbQ9JM99.
PRIDEQ9JM99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006171; ENSMUSP00000006171; ENSMUSG00000006014.
ENSMUST00000162367; ENSMUSP00000125551; ENSMUSG00000006014.
GeneID96875.
KEGGmmu:96875.

Organism-specific databases

CTD10216.
MGIMGI:1891344. Prg4.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00530000063751.
HOGENOMHOG000115691.
HOVERGENHBG101613.
InParanoidQ9JM99.
OrthoDBEOG7HMS1H.

Gene expression databases

ArrayExpressQ9JM99.
BgeeQ9JM99.
GenevestigatorQ9JM99.

Family and domain databases

Gene3D2.110.10.10. 2 hits.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamPF00045. Hemopexin. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSPR00022. SOMATOMEDINB.
SMARTSM00120. HX. 2 hits.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMSSF50923. SSF50923. 2 hits.
PROSITEPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 2 hits.
PS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio352339.
PROQ9JM99.
SOURCESearch...

Entry information

Entry namePRG4_MOUSE
AccessionPrimary (citable) accession number: Q9JM99
Secondary accession number(s): Q3UEL1, Q3V198
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot