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P28798

- GRN_MOUSE

UniProt

P28798 - GRN_MOUSE

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Protein

Granulins

Gene

Grn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. blastocyst hatching Source: MGI
  2. embryo implantation Source: MGI
  3. positive regulation of epithelial cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Names & Taxonomyi

Protein namesi
Recommended name:
Granulins
Alternative name(s):
PC cell-derived growth factor
Short name:
PCDGF
Proepithelin
Short name:
PEPI
Cleaved into the following 8 chains:
Gene namesi
Name:Grn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:95832. Grn.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 589572AcrograninPRO_0000012702Add
BLAST
Peptidei?58 – ?11356Granulin-1PRO_0000012703Add
BLAST
Peptidei?122 – ?17857Granulin-2PRO_0000012704Add
BLAST
Peptidei205 – 26056Granulin-3PRO_0000012705Add
BLAST
Peptidei280 – 33455Granulin-4PRO_0000012706Add
BLAST
Peptidei362 – ?41453Granulin-5PRO_0000012707Add
BLAST
Peptidei440 – ?49354Granulin-6PRO_0000012708Add
BLAST
Peptidei?517 – ?56852Granulin-7PRO_0000012709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi125 ↔ 138By similarity
Disulfide bondi132 ↔ 148By similarity
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi295 ↔ 312By similarity
Disulfide bondi305 ↔ 319By similarity
Disulfide bondi313 ↔ 326By similarity
Disulfide bondi320 ↔ 333By similarity
Disulfide bondi364 ↔ 376By similarity
Disulfide bondi370 ↔ 386By similarity
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi395 ↔ 408By similarity
Disulfide bondi402 ↔ 414By similarity
Glycosylationi526 – 5261N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Granulins are disulfide bridged.
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP28798.
PaxDbiP28798.
PRIDEiP28798.

PTM databases

PhosphoSiteiP28798.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP28798.
CleanExiMM_GRN.
ExpressionAtlasiP28798. baseline and differential.
GenevestigatoriP28798.

Interactioni

Subunit structurei

Acrogranin/Progranulin is secreted as a homodimer.By similarity

Protein-protein interaction databases

IntActiP28798. 7 interactions.
MINTiMINT-4096910.

Structurei

3D structure databases

ProteinModelPortaliP28798.
SMRiP28798. Positions 122-153, 209-262, 279-334, 363-416, 439-497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the granulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG270518.
HOVERGENiHBG000845.
InParanoidiP28798.

Family and domain databases

InterProiIPR000118. Granulin.
[Graphical view]
PfamiPF00396. Granulin. 7 hits.
[Graphical view]
SMARTiSM00277. GRAN. 7 hits.
[Graphical view]
PROSITEiPS00799. GRANULINS. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P28798-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWVLMSWLAF AAGLVAGTQC PDGQFCPVAC CLDQGGANYS CCNPLLDTWP
60 70 80 90 100
RITSHHLDGS CQTHGHCPAG YSCLLTVSGT SSCCPFSKGV SCGDGYHCCP
110 120 130 140 150
QGFHCSADGK SCFQMSDNPL GAVQCPGSQF ECPDSATCCI MVDGSWGCCP
160 170 180 190 200
MPQASCCEDR VHCCPHGASC DLVHTRCVSP TGTHTLLKKF PAQKTNRAVS
210 220 230 240 250
LPFSVVCPDA KTQCPDDSTC CELPTGKYGC CPMPNAICCS DHLHCCPQDT
260 270 280 290 300
VCDLIQSKCL SKNYTTDLLT KLPGYPVKEV KCDMEVSCPE GYTCCRLNTG
310 320 330 340 350
AWGCCPFAKA VCCEDHIHCC PAGFQCHTEK GTCEMGILQV PWMKKVIAPL
360 370 380 390 400
RLPDPQILKS DTPCDDFTRC PTNNTCCKLN SGDWGCCPIP EAVCCSDNQH
410 420 430 440 450
CCPQGFTCLA QGYCQKGDTM VAGLEKIPAR QTTPLQIGDI GCDQHTSCPV
460 470 480 490 500
GQTCCPSLKG SWACCQLPHA VCCEDRQHCC PAGYTCNVKA RTCEKDVDFI
510 520 530 540 550
QPPVLLTLGP KVGNVECGEG HFCHDNQTCC KDSAGVWACC PYLKGVCCRD
560 570 580
GRHCCPGGFH CSARGTKCLR KKIPRWDMFL RDPVPRPLL
Length:589
Mass (Da):63,458
Last modified:October 1, 1994 - v2
Checksum:i1DE8229C413CB787
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511V → L in AAA37191. (PubMed:8471244)Curated
Sequence conflicti254 – 2541L → V in AAA37191. (PubMed:8471244)Curated
Sequence conflicti261 – 2633SKN → YD AA sequence (PubMed:8496151)Curated
Sequence conflicti350 – 3501L → R in CAA44197. (PubMed:1618805)Curated
Sequence conflicti402 – 4032CP → SA in AAA37191. (PubMed:8471244)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16195 Genomic DNA. Translation: BAA03736.1.
M86736 mRNA. Translation: AAA37191.1.
X62321 mRNA. Translation: CAA44197.1.
PIRiC38128.
UniGeneiMm.1568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16195 Genomic DNA. Translation: BAA03736.1 .
M86736 mRNA. Translation: AAA37191.1 .
X62321 mRNA. Translation: CAA44197.1 .
PIRi C38128.
UniGenei Mm.1568.

3D structure databases

ProteinModelPortali P28798.
SMRi P28798. Positions 122-153, 209-262, 279-334, 363-416, 439-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P28798. 7 interactions.
MINTi MINT-4096910.

PTM databases

PhosphoSitei P28798.

Proteomic databases

MaxQBi P28798.
PaxDbi P28798.
PRIDEi P28798.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:95832. Grn.

Phylogenomic databases

eggNOGi NOG270518.
HOVERGENi HBG000845.
InParanoidi P28798.

Miscellaneous databases

ChiTaRSi Grn. mouse.
PROi P28798.
SOURCEi Search...

Gene expression databases

Bgeei P28798.
CleanExi MM_GRN.
ExpressionAtlasi P28798. baseline and differential.
Genevestigatori P28798.

Family and domain databases

InterProi IPR000118. Granulin.
[Graphical view ]
Pfami PF00396. Granulin. 7 hits.
[Graphical view ]
SMARTi SM00277. GRAN. 7 hits.
[Graphical view ]
PROSITEi PS00799. GRANULINS. 7 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGRN_MOUSE
AccessioniPrimary (citable) accession number: P28798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1994
Last modified: November 26, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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