SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P28798

- GRN_MOUSE

UniProt

P28798 - GRN_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 - 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. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 Publication
Add
BLAST
Chaini18 – 589572Acrogranin
PRO_0000012702Add
BLAST
Peptidei?58 – ?11356Granulin-1
PRO_0000012703Add
BLAST
Peptidei?122 – ?17857Granulin-2
PRO_0000012704Add
BLAST
Peptidei205 – 26056Granulin-3
PRO_0000012705Add
BLAST
Peptidei280 – 33455Granulin-4
PRO_0000012706Add
BLAST
Peptidei362 – ?41453Granulin-5
PRO_0000012707Add
BLAST
Peptidei440 – ?49354Granulin-6
PRO_0000012708Add
BLAST
Peptidei?517 – ?56852Granulin-7
PRO_0000012709Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Granulins are disulfide bridged.
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP28798.
PRIDEiP28798.

PTM databases

PhosphoSiteiP28798.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP28798.
BgeeiP28798.
CleanExiMM_GRN.
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.

Family & Domainsi

Sequence similaritiesi

Belongs to the granulin family.

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

MWVLMSWLAF AAGLVAGTQC PDGQFCPVAC CLDQGGANYS CCNPLLDTWP    50
RITSHHLDGS CQTHGHCPAG YSCLLTVSGT SSCCPFSKGV SCGDGYHCCP 100
QGFHCSADGK SCFQMSDNPL GAVQCPGSQF ECPDSATCCI MVDGSWGCCP 150
MPQASCCEDR VHCCPHGASC DLVHTRCVSP TGTHTLLKKF PAQKTNRAVS 200
LPFSVVCPDA KTQCPDDSTC CELPTGKYGC CPMPNAICCS DHLHCCPQDT 250
VCDLIQSKCL SKNYTTDLLT KLPGYPVKEV KCDMEVSCPE GYTCCRLNTG 300
AWGCCPFAKA VCCEDHIHCC PAGFQCHTEK GTCEMGILQV PWMKKVIAPL 350
RLPDPQILKS DTPCDDFTRC PTNNTCCKLN SGDWGCCPIP EAVCCSDNQH 400
CCPQGFTCLA QGYCQKGDTM VAGLEKIPAR QTTPLQIGDI GCDQHTSCPV 450
GQTCCPSLKG SWACCQLPHA VCCEDRQHCC PAGYTCNVKA RTCEKDVDFI 500
QPPVLLTLGP KVGNVECGEG HFCHDNQTCC KDSAGVWACC PYLKGVCCRD 550
GRHCCPGGFH CSARGTKCLR KKIPRWDMFL RDPVPRPLL 589
Length:589
Mass (Da):63,458
Last modified:October 1, 1994 - v2
Checksum:i1DE8229C413CB787
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511V → L in AAA37191. 1 Publication
Sequence conflicti254 – 2541L → V in AAA37191. 1 Publication
Sequence conflicti261 – 2633SKN → YD AA sequence 1 Publication
Sequence conflicti350 – 3501L → R in CAA44197. 1 Publication
Sequence conflicti402 – 4032CP → SA in AAA37191. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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

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

ArrayExpressi P28798.
Bgeei P28798.
CleanExi MM_GRN.
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: June 11, 2014
This is version 110 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

Similar proteinsi