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Protein

Granulins

Gene

Grn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.

GO - Biological processi

  • chondrocyte proliferation Source: RGD
  • male mating behavior Source: RGD
  • neural precursor cell proliferation Source: RGD
  • positive regulation of dendritic spine development Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • response to estradiol Source: RGD
  • synaptic vesicle endocytosis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Names & Taxonomyi

Protein namesi
Recommended name:
Granulins
Cleaved into the following 8 chains:
Alternative name(s):
Progranulin
Alternative name(s):
Granulin G
Alternative name(s):
Granulin F
Alternative name(s):
Epithelin-2
Granulin B
Alternative name(s):
Epithelin-1
Granulin A
Alternative name(s):
Granulin C
Alternative name(s):
Granulin D
Alternative name(s):
Granulin E
Gene namesi
Name:Grn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61983. Grn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 588571AcrograninPRO_0000012710Add
BLAST
Peptidei58 – 11356Granulin-1PRO_0000012711Add
BLAST
Peptidei122 – 17857Granulin-2PRO_0000012712Add
BLAST
Peptidei204 – 25956Granulin-3PRO_0000012713Add
BLAST
Peptidei278 – 33457Granulin-4PRO_0000012714Add
BLAST
Peptidei361 – 41353Granulin-5PRO_0000012715Add
BLAST
Peptidei438 – 49255Granulin-6PRO_0000012716Add
BLAST
Peptidei512 – 56756Granulin-7PRO_0000012717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi125 ↔ 138By similarity
Disulfide bondi132 ↔ 148By similarity
Disulfide bondi294 ↔ 311By similarity
Disulfide bondi304 ↔ 318By similarity
Disulfide bondi312 ↔ 325By similarity
Disulfide bondi319 ↔ 332By similarity
Disulfide bondi363 ↔ 375By similarity
Disulfide bondi369 ↔ 385By similarity
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence analysis
Disulfide bondi394 ↔ 407By similarity
Disulfide bondi401 ↔ 413By similarity
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Granulins are disulfide bridged.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP23785.
PRIDEiP23785.

Expressioni

Tissue specificityi

Ubiquitous; most abundant in the spleen and several tissues of endocrine significance.

Interactioni

Subunit structurei

Acrogranin/Progranulin is secreted as a homodimer.By similarity

Protein-protein interaction databases

BioGridi247826. 2 interactions.
IntActiP23785. 1 interaction.
STRINGi10116.ENSRNOP00000028557.

Structurei

3D structure databases

ProteinModelPortaliP23785.
SMRiP23785. Positions 122-153, 204-234, 278-333, 361-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the granulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG4296. Eukaryota.
ENOG410XR6S. LUCA.
HOGENOMiHOG000067856.
HOVERGENiHBG000845.
InParanoidiP23785.
PhylomeDBiP23785.

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.

P23785-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWILVSWLAL VARLVAGTQC PDGQFCPVAC CLDQGGANYS CCNPLLDTWP
60 70 80 90 100
IITSRRLDGS CQIRDHCPDG YSCLLTVSGT SSCCPFSEGV SCDDGQHCCP
110 120 130 140 150
RGFHCSADGK SCSQISDSLL GAVQCPGSQF ECPDSATCCI MIDGSWGCCP
160 170 180 190 200
MPQASCCEDR VHCCPHGASC DLVHTRCISP TGTHPLLKKF PAQRTNRAVA
210 220 230 240 250
SFSVVCPDAK TQCPDDSTCC ELPTGKYGCC PMPNAICCSD HLHCCPQDTV
260 270 280 290 300
CDLIQSKCIS KDYTTDLMTK LPGYPVNEVK CDLEVSCPDG YTCCRLNTGA
310 320 330 340 350
WGCCPFTKAV CCEDHIHCCP AGFQCHTETG TCELGVLQVP WMKKVTASLS
360 370 380 390 400
LPDPQILKND VPCDDFSSCP SNNTCCRLSS GDWGCCPMPE AVCCLDHQHC
410 420 430 440 450
CPQGFKCMDE GYCQKGDRMV AGLEKMPVRQ TTLLQHGDIG CDQHTSCPVG
460 470 480 490 500
QTCCPSLKGS WACCQLPHAV CCEDRQHCCP AGYTCNVKAR TCEKDAGSVQ
510 520 530 540 550
PSMDLTFGSK VGNVECGAGH FCHDNQSCCK DSQGGWACCP YVKGVCCRDG
560 570 580
RHCCPIGFHC SAKGTKCLRK KTPRWDILLR DPAPRPLL
Length:588
Mass (Da):63,370
Last modified:December 1, 1992 - v3
Checksum:i113D434F7E099B31
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011S → FP in CAA44198 (PubMed:1618805).Curated
Sequence conflicti307 – 3082TK → SB AA sequence (PubMed:2268320).Curated
Sequence conflicti324 – 3241Q → T AA sequence (PubMed:2268320).Curated
Sequence conflicti388 – 3881M → I in CAA44198 (PubMed:1618805).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97750 mRNA. Translation: AAA16903.1.
X62322 mRNA. Translation: CAA44198.1.
PIRiB38128.
RefSeqiNP_058809.2. NM_017113.2.
UniGeneiRn.5820.

Genome annotation databases

GeneIDi29143.
KEGGirno:29143.
UCSCiRGD:61983. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97750 mRNA. Translation: AAA16903.1.
X62322 mRNA. Translation: CAA44198.1.
PIRiB38128.
RefSeqiNP_058809.2. NM_017113.2.
UniGeneiRn.5820.

3D structure databases

ProteinModelPortaliP23785.
SMRiP23785. Positions 122-153, 204-234, 278-333, 361-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247826. 2 interactions.
IntActiP23785. 1 interaction.
STRINGi10116.ENSRNOP00000028557.

Proteomic databases

PaxDbiP23785.
PRIDEiP23785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29143.
KEGGirno:29143.
UCSCiRGD:61983. rat.

Organism-specific databases

CTDi2896.
RGDi61983. Grn.

Phylogenomic databases

eggNOGiKOG4296. Eukaryota.
ENOG410XR6S. LUCA.
HOGENOMiHOG000067856.
HOVERGENiHBG000845.
InParanoidiP23785.
PhylomeDBiP23785.

Miscellaneous databases

PROiP23785.

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]
ProtoNetiSearch...

Publicationsi

  1. "The complementary deoxyribonucleic acid sequence, tissue distribution, and cellular localization of the rat granulin precursor."
    Bhandari V., Giaid A., Bateman A.
    Endocrinology 133:2682-2689(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  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 [MRNA], PROTEIN SEQUENCE OF 204-259 AND 278-334.
    Tissue: Kidney.
  3. "Epithelins 1 and 2: isolation and characterization of two cysteine-rich growth-modulating proteins."
    Shoyab M., McDonald V.L., Byles C., Todaro G.J., Plowman G.D.
    Proc. Natl. Acad. Sci. U.S.A. 87:7912-7916(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 204-225 AND 279-299.
  4. Cited for: PROTEIN SEQUENCE OF 278-328.
    Tissue: Bone marrow.

Entry informationi

Entry nameiGRN_RAT
AccessioniPrimary (citable) accession number: P23785
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: December 1, 1992
Last modified: July 6, 2016
This is version 107 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.