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Q9JM99

- PRG4_MOUSE

UniProt

Q9JM99 - PRG4_MOUSE

Protein

Proteoglycan 4

Gene

Prg4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei955 – 9562Cleavage; by subtilisin-like proprotein convertase 4

    GO - Molecular functioni

    1. polysaccharide binding Source: InterPro
    2. scavenger receptor activity Source: InterPro

    GO - Biological processi

    1. hematopoietic stem cell proliferation Source: MGI
    2. immune response Source: InterPro
    3. negative regulation of interleukin-6 biosynthetic process Source: MGI
    4. regulation of cell proliferation Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteoglycan 4
    Alternative name(s):
    Lubricin
    Megakaryocyte-stimulating factor
    Superficial zone proteoglycan
    Cleaved into the following chain:
    Gene namesi
    Name:Prg4
    Synonyms:Msf, Szp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1891344. Prg4.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular space Source: MGI

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi795 – 7951C → A: Not cleaved by subtilisin-like proprotein convertase. Not cleaved by subtilisin-like proprotein convertase; when associated with A-1053. 1 Publication
    Mutagenesisi851 – 8533CNC → ANA: Cleaved by subtilisin-like proprotein convertase.
    Mutagenesisi851 – 8511C → A: Cleaved by subtilisin-like proprotein convertase.
    Mutagenesisi930 – 9301C → A: Cleaved by subtilisin-like proprotein convertase. 1 Publication
    Mutagenesisi949 – 9557RRRRFER → ARARFEA: Not cleaved by subtilisin-like proprotein convertase 4.
    Mutagenesisi949 – 9513RRR → ARA: Cleaved by subtilisin-like proprotein convertase 4.
    Mutagenesisi955 – 9551R → A: Not cleaved by subtilisin-like proprotein convertase 4.
    Mutagenesisi1053 – 10531C → A: Not cleaved by subtilisin-like proprotein convertase 4. Not cleaved by subtilisin-like proprotein convertase; when associated with A-795. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 10541030Proteoglycan 4PRO_0000043234Add
    BLAST
    Chaini956 – 105499Proteoglycan 4 C-terminal partPRO_0000043235Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 46AlternatePROSITE-ProRule annotation
    Disulfide bondi30 ↔ 34PROSITE-ProRule annotation
    Disulfide bondi34 ↔ 64AlternatePROSITE-ProRule annotation
    Disulfide bondi44 ↔ 57AlternatePROSITE-ProRule annotation
    Disulfide bondi44 ↔ 46PROSITE-ProRule annotation
    Disulfide bondi50 ↔ 56PROSITE-ProRule annotation
    Disulfide bondi57 ↔ 64PROSITE-ProRule annotation
    Disulfide bondi70 ↔ 86AlternatePROSITE-ProRule annotation
    Disulfide bondi70 ↔ 74PROSITE-ProRule annotation
    Disulfide bondi74 ↔ 104AlternatePROSITE-ProRule annotation
    Disulfide bondi84 ↔ 97AlternatePROSITE-ProRule annotation
    Disulfide bondi84 ↔ 86PROSITE-ProRule annotation
    Disulfide bondi90 ↔ 96PROSITE-ProRule annotation
    Disulfide bondi97 ↔ 104PROSITE-ProRule annotation
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi795 ↔ 10531 PublicationPROSITE-ProRule annotation
    Glycosylationi938 – 9381N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan

    Proteomic databases

    PaxDbiQ9JM99.
    PRIDEiQ9JM99.

    PTM databases

    PhosphoSiteiQ9JM99.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Developmental stagei

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ9JM99.
    BgeeiQ9JM99.
    GenevestigatoriQ9JM99.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 Publication

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 6944SMB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini66 – 10843SMB 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati317 – 32481; approximate
    Repeati325 – 33282; approximate
    Repeati333 – 34083; approximate
    Repeati349 – 35684; approximate
    Repeati357 – 36485
    Repeati365 – 37176; approximate
    Repeati372 – 37987
    Repeati380 – 38788
    Repeati388 – 39589
    Repeati396 – 403810
    Repeati404 – 411811
    Repeati412 – 418712; approximate
    Repeati419 – 426813
    Repeati427 – 434814
    Repeati435 – 442815
    Repeati443 – 450816; approximate
    Repeati451 – 458817
    Repeati459 – 466818
    Repeati467 – 474819
    Repeati475 – 482820
    Repeati483 – 490821
    Repeati491 – 498822
    Repeati499 – 506823
    Repeati507 – 514824
    Repeati515 – 522825
    Repeati523 – 530826
    Repeati531 – 538827
    Repeati539 – 546828
    Repeati547 – 554829
    Repeati555 – 562830
    Repeati563 – 570831
    Repeati571 – 578832
    Repeati579 – 586833
    Repeati587 – 594834
    Repeati595 – 602835
    Repeati603 – 610836
    Repeati611 – 618837
    Repeati797 – 84044Hemopexin 1Add
    BLAST
    Repeati841 – 88848Hemopexin 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni317 – 61830237 X 8 AA repeats of K-X-P-X-P-T-T-XAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi157 – 18428Ser-richAdd
    BLAST
    Compositional biasi350 – 606257Glu-richAdd
    BLAST
    Compositional biasi659 – 69941Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 hemopexin repeats.Curated
    Contains 2 SMB (somatomedin-B) domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00530000063751.
    HOGENOMiHOG000115691.
    HOVERGENiHBG101613.
    InParanoidiQ9JM99.
    OrthoDBiEOG7HMS1H.

    Family and domain databases

    Gene3Di2.110.10.10. 2 hits.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view]
    PfamiPF00045. Hemopexin. 1 hit.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view]
    PRINTSiPR00022. SOMATOMEDINB.
    SMARTiSM00120. HX. 2 hits.
    SM00201. SO. 2 hits.
    [Graphical view]
    SUPFAMiSSF50923. SSF50923. 2 hits.
    PROSITEiPS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 2 hits.
    PS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q9JM99-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGWKILPVCL SLLLPVVLIQ QVSSQDLSSC AGRCGEGYSR DATCNCDYNC     50
    QHYMECCPDF KRVCSPELSC KGRCFESFAR GRECDCDSQC KQYGKCCADY 100
    DSFCEEVHNS TSPSSKTAPT PAGASDTIKS TTKRSPKSPT TRTIKVVESE 150
    ELTEEHSDSE NQESSSSSSS SSSTIRKIKS SKNSANRELQ KNPNVKDNKK 200
    NTPKKKPNPE PPAVDEAGSG LDNGEFKLTP PPPDPPTTPH SKVATSPKTT 250
    AAKPVTPKPS LAPNSETSKE ASLASNKETT VETKETTATN KQSSASKKKT 300
    TSVKETRSAE KTSDKDVEPT STTPKNSAPT TTKKPVTTTK ESKFLPLPQE 350
    PEPTTAKEPP PTTKKPEPTT RKEPEPTTPK EPEPTTPKEP EPTTPKEPEP 400
    TTPKEPPPTT KKPEPTTPKE PGPTTPKEPE PTTTKEPEPT TTKEPESTTR 450
    KEPEPTTPKE PEPTTPKEPE PTTLKEPEPT TPKEPEPTTP KEPEPTTPKE 500
    PEPTTPKEPE PTTPKEPEPT TPKEPEPTTP KEPEPTTPKE PEPTTPKKPE 550
    PTTPKEPVPT TPKEPEPTTP KEPEPTTPKE PEPTTRKEPE PTTPKEPEPT 600
    TPKEPEPTTP KKPEPTTTSP KTTTLKATTL APKVTAPAEE IQNKPEETTP 650
    ASEDSDDSKT TLKPQKPTKA PKPTKKPTKA PKKPTSTKKP KTPKTRKPKT 700
    TPSPLKTTSA TPELNTTPLE VMLPTTTIPK QTPNPETAEV NPDHEDADGG 750
    EGEKPLIPGP PVLFPTAIPG TDLLAGRLNQ GININPMLSD ETNLCNGKPV 800
    DGLTTLRNGT LVAFRGHYFW MLNPFRPPSP PRRITEVWGI PSPIDTVFTR 850
    CNCEGKTFFF KDSQYWRFTN DVVDPGYPKQ IVKGFGGLTG KIVAALSIAK 900
    YKDRPESVYF FKRGGNIQQY TYKQEPMKKC TGRRPAINYS VYGEAAQVRR 950
    RRFERAVGPF QTHTFRIHYS VPMRVSYQDK GFLHNEVKVS TMWRGFPNVV 1000
    TSAITLPNIR KPDGYDYYAF SKDQYYNIDV PTRTARAITT RSGQTLSKIW 1050
    YNCP 1054
    Length:1,054
    Mass (Da):115,996
    Last modified:December 6, 2005 - v2
    Checksum:i13312FB7070DF2A4
    GO
    Isoform B (identifier: Q9JM99-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         26-66: Missing.

    Show »
    Length:1,013
    Mass (Da):111,425
    Checksum:i49334633D98BD1E4
    GO
    Isoform C (identifier: Q9JM99-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         107-194: Missing.

    Show »
    Length:966
    Mass (Da):106,637
    Checksum:i123569A1FABFC5BD
    GO
    Isoform D (identifier: Q9JM99-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         26-66: Missing.
         107-194: Missing.

    Show »
    Length:925
    Mass (Da):102,066
    Checksum:i1CD5556F5467CD48
    GO
    Isoform E (identifier: Q9JM99-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         107-194: Missing.
         224-766: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:423
    Mass (Da):47,989
    Checksum:iEBC6B86287506E4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 662SP → TT in BAE28900. (PubMed:16141072)Curated
    Sequence conflicti703 – 7031S → A in BAA92310. (PubMed:11124536)Curated
    Sequence conflicti780 – 7801Q → R in BAA92310. (PubMed:11124536)Curated
    Sequence conflicti788 – 7881L → P in BAA92310. (PubMed:11124536)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei26 – 6641Missing in isoform B and isoform D. CuratedVSP_016471Add
    BLAST
    Alternative sequencei107 – 19488Missing in isoform C, isoform D and isoform E. 1 PublicationVSP_016472Add
    BLAST
    Alternative sequencei224 – 766543Missing in isoform E. 1 PublicationVSP_016473Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB034730 mRNA. Translation: BAA92310.1.
    AK132597 mRNA. Translation: BAE21253.1.
    AK149469 mRNA. Translation: BAE28900.1.
    CCDSiCCDS48391.1. [Q9JM99-5]
    RefSeqiNP_001103616.1. NM_001110146.1.
    UniGeneiMm.174256.
    Mm.329131.

    Genome annotation databases

    EnsembliENSMUST00000006171; ENSMUSP00000006171; ENSMUSG00000006014.
    ENSMUST00000162367; ENSMUSP00000125551; ENSMUSG00000006014.
    GeneIDi96875.
    KEGGimmu:96875.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB034730 mRNA. Translation: BAA92310.1 .
    AK132597 mRNA. Translation: BAE21253.1 .
    AK149469 mRNA. Translation: BAE28900.1 .
    CCDSi CCDS48391.1. [Q9JM99-5 ]
    RefSeqi NP_001103616.1. NM_001110146.1.
    UniGenei Mm.174256.
    Mm.329131.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9JM99.

    Proteomic databases

    PaxDbi Q9JM99.
    PRIDEi Q9JM99.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006171 ; ENSMUSP00000006171 ; ENSMUSG00000006014 .
    ENSMUST00000162367 ; ENSMUSP00000125551 ; ENSMUSG00000006014 .
    GeneIDi 96875.
    KEGGi mmu:96875.

    Organism-specific databases

    CTDi 10216.
    MGIi MGI:1891344. Prg4.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00530000063751.
    HOGENOMi HOG000115691.
    HOVERGENi HBG101613.
    InParanoidi Q9JM99.
    OrthoDBi EOG7HMS1H.

    Miscellaneous databases

    NextBioi 352339.
    PROi Q9JM99.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JM99.
    Bgeei Q9JM99.
    Genevestigatori Q9JM99.

    Family and domain databases

    Gene3Di 2.110.10.10. 2 hits.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view ]
    Pfami PF00045. Hemopexin. 1 hit.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view ]
    PRINTSi PR00022. SOMATOMEDINB.
    SMARTi SM00120. HX. 2 hits.
    SM00201. SO. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50923. SSF50923. 2 hits.
    PROSITEi PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 2 hits.
    PS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiPRG4_MOUSE
    AccessioniPrimary (citable) accession number: Q9JM99
    Secondary accession number(s): Q3UEL1, Q3V198
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Different forms varying in molecular weight have been observed. Such forms are possibly due to different levels of glycosylation and protein cleavage.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3