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P28798 (GRN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Granulins
Alternative name(s):
PC cell-derived growth factor
Short name=PCDGF
Proepithelin
Short name=PEPI

Cleaved into the following 8 chains:

  1. Acrogranin
    Alternative name(s):
    Progranulin
  2. Granulin-1
  3. Granulin-2
  4. Granulin-3
  5. Granulin-4
  6. Granulin-5
  7. Granulin-6
  8. Granulin-7
Gene names
Name:Grn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Acts as an autocrine growth factor for PC cells. Ref.4

Subunit structure

Acrogranin/Progranulin is secreted as a homodimer By similarity.

Subcellular location

Secreted Ref.4.

Tissue specificity

Ubiquitous.

Post-translational modification

Granulins are disulfide bridged.

N-glycosylated. Ref.4

Sequence similarities

Belongs to the granulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.4
Chain18 – 589572Acrogranin
PRO_0000012702
Peptide?58 – ?11356Granulin-1
PRO_0000012703
Peptide?122 – ?17857Granulin-2
PRO_0000012704
Peptide205 – 26056Granulin-3
PRO_0000012705
Peptide280 – 33455Granulin-4
PRO_0000012706
Peptide362 – ?41453Granulin-5
PRO_0000012707
Peptide440 – ?49354Granulin-6
PRO_0000012708
Peptide?517 – ?56852Granulin-7
PRO_0000012709

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation5261N-linked (GlcNAc...) Potential
Disulfide bond125 ↔ 138 By similarity
Disulfide bond132 ↔ 148 By similarity
Disulfide bond295 ↔ 312 By similarity
Disulfide bond305 ↔ 319 By similarity
Disulfide bond313 ↔ 326 By similarity
Disulfide bond320 ↔ 333 By similarity
Disulfide bond364 ↔ 376 By similarity
Disulfide bond370 ↔ 386 By similarity
Disulfide bond395 ↔ 408 By similarity
Disulfide bond402 ↔ 414 By similarity

Experimental info

Sequence conflict2511V → L in AAA37191. Ref.3
Sequence conflict2541L → V in AAA37191. Ref.3
Sequence conflict261 – 2633SKN → YD AA sequence Ref.4
Sequence conflict3501L → R in CAA44197. Ref.2
Sequence conflict402 – 4032CP → SA in AAA37191. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P28798 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 1DE8229C413CB787

FASTA58963,458
        10         20         30         40         50         60 
MWVLMSWLAF AAGLVAGTQC PDGQFCPVAC CLDQGGANYS CCNPLLDTWP RITSHHLDGS 

        70         80         90        100        110        120 
CQTHGHCPAG YSCLLTVSGT SSCCPFSKGV SCGDGYHCCP QGFHCSADGK SCFQMSDNPL 

       130        140        150        160        170        180 
GAVQCPGSQF ECPDSATCCI MVDGSWGCCP MPQASCCEDR VHCCPHGASC DLVHTRCVSP 

       190        200        210        220        230        240 
TGTHTLLKKF PAQKTNRAVS LPFSVVCPDA KTQCPDDSTC CELPTGKYGC CPMPNAICCS 

       250        260        270        280        290        300 
DHLHCCPQDT VCDLIQSKCL SKNYTTDLLT KLPGYPVKEV KCDMEVSCPE GYTCCRLNTG 

       310        320        330        340        350        360 
AWGCCPFAKA VCCEDHIHCC PAGFQCHTEK GTCEMGILQV PWMKKVIAPL RLPDPQILKS 

       370        380        390        400        410        420 
DTPCDDFTRC PTNNTCCKLN SGDWGCCPIP EAVCCSDNQH CCPQGFTCLA QGYCQKGDTM 

       430        440        450        460        470        480 
VAGLEKIPAR QTTPLQIGDI GCDQHTSCPV GQTCCPSLKG SWACCQLPHA VCCEDRQHCC 

       490        500        510        520        530        540 
PAGYTCNVKA RTCEKDVDFI QPPVLLTLGP KVGNVECGEG HFCHDNQTCC KDSAGVWACC 

       550        560        570        580 
PYLKGVCCRD GRHCCPGGFH CSARGTKCLR KKIPRWDMFL RDPVPRPLL 

« Hide

References

[1]"Exon/intron organization of the gene encoding the mouse epithelin/granulin precursor (acrogranin)."
Baba T., Nemoto H., Watanabe K., Arai Y., Gerton G.L.
FEBS Lett. 322:89-94(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The epithelin precursor encodes two proteins with opposing activities on epithelial cell growth."
Plowman G.D., Green J.M., Neubauer M.G., Buckley S.D., McDonald V.L., Todaro G.J., Shoyab M.
J. Biol. Chem. 267:13073-13078(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Kidney.
[3]"Acrogranin, an acrosomal cysteine-rich glycoprotein, is the precursor of the growth-modulating peptides, granulins, and epithelins, and is expressed in somatic as well as male germ cells."
Baba T., Hoff H.B. III, Nemoto H., Lee H., Orth J., Arai Y., Gerton G.L.
Mol. Reprod. Dev. 34:233-243(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Purification of an autocrine growth factor homologous with mouse epithelin precursor from a highly tumorigenic cell line."
Zhou J., Gao G., Crabb J.W., Serrero G.
J. Biol. Chem. 268:10863-10869(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-32; 116-127; 152-164; 198-226; 228-233; 259-280; 297-304 AND 421-430, FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16195 Genomic DNA. Translation: BAA03736.1.
M86736 mRNA. Translation: AAA37191.1.
X62321 mRNA. Translation: CAA44197.1.
PIRC38128.
UniGeneMm.1568.

3D structure databases

ProteinModelPortalP28798.
SMRP28798. Positions 122-153, 209-262, 279-334, 363-416, 439-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28798. 7 interactions.
MINTMINT-4096910.

PTM databases

PhosphoSiteP28798.

Proteomic databases

PaxDbP28798.
PRIDEP28798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:95832. Grn.

Phylogenomic databases

eggNOGNOG270518.
HOVERGENHBG000845.
InParanoidP28798.

Gene expression databases

ArrayExpressP28798.
BgeeP28798.
CleanExMM_GRN.
GenevestigatorP28798.

Family and domain databases

InterProIPR000118. Granulin.
[Graphical view]
PfamPF00396. Granulin. 7 hits.
[Graphical view]
SMARTSM00277. GRAN. 7 hits.
[Graphical view]
PROSITEPS00799. GRANULINS. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGRN. mouse.
PROP28798.
SOURCESearch...

Entry information

Entry nameGRN_MOUSE
AccessionPrimary (citable) accession number: P28798
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 110 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