GRN_MOUSE
ID GRN_MOUSE Reviewed; 589 AA.
AC P28798;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Progranulin {ECO:0000303|PubMed:12524533};
DE Short=PGRN {ECO:0000250|UniProtKB:P28799};
DE AltName: Full=Acrogranin {ECO:0000303|PubMed:8482392};
DE AltName: Full=Epithelin/granulin precursor {ECO:0000303|PubMed:8482392};
DE AltName: Full=Glycoprotein of 88 Kda {ECO:0000305|PubMed:8496151};
DE Short=GP88;
DE Short=Glycoprotein 88;
DE AltName: Full=PC cell-derived growth factor {ECO:0000303|PubMed:8496151};
DE Short=PCDGF {ECO:0000303|PubMed:8496151};
DE AltName: Full=Proepithelin {ECO:0000303|PubMed:12526812};
DE Short=PEPI {ECO:0000250|UniProtKB:P28799};
DE Contains:
DE RecName: Full=Paragranulin;
DE Contains:
DE RecName: Full=Granulin-1;
DE Contains:
DE RecName: Full=Granulin-2;
DE Contains:
DE RecName: Full=Granulin-3;
DE Contains:
DE RecName: Full=Granulin-4;
DE Contains:
DE RecName: Full=Granulin-5;
DE Contains:
DE RecName: Full=Granulin-6;
DE Contains:
DE RecName: Full=Granulin-7;
DE Flags: Precursor;
GN Name=Grn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8482392; DOI=10.1016/0014-5793(93)81544-a;
RA Baba T., Nemoto H., Watanabe K., Arai Y., Gerton G.L.;
RT "Exon/intron organization of the gene encoding the mouse epithelin/granulin
RT precursor (acrogranin).";
RL FEBS Lett. 322:89-94(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Kidney;
RX PubMed=1618805; DOI=10.1016/s0021-9258(18)42382-4;
RA Plowman G.D., Green J.M., Neubauer M.G., Buckley S.D., McDonald V.L.,
RA Todaro G.J., Shoyab M.;
RT "The epithelin precursor encodes two proteins with opposing activities on
RT epithelial cell growth.";
RL J. Biol. Chem. 267:13073-13078(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8471244; DOI=10.1002/mrd.1080340302;
RA Baba T., Hoff H.B. III, Nemoto H., Lee H., Orth J., Arai Y., Gerton G.L.;
RT "Acrogranin, an acrosomal cysteine-rich glycoprotein, is the precursor of
RT the growth-modulating peptides, granulins, and epithelins, and is expressed
RT in somatic as well as male germ cells.";
RL Mol. Reprod. Dev. 34:233-243(1993).
RN [4]
RP PROTEIN SEQUENCE OF 18-32; 116-127; 152-164; 198-226; 228-233; 259-280;
RP 297-304 AND 421-430, FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=8496151; DOI=10.1016/s0021-9258(18)82064-6;
RA Zhou J., Gao G., Crabb J.W., Serrero G.;
RT "Purification of an autocrine growth factor homologous with mouse epithelin
RT precursor from a highly tumorigenic cell line.";
RL J. Biol. Chem. 268:10863-10869(1993).
RN [5]
RP INTERACTION WITH SLPI.
RX PubMed=12526812; DOI=10.1016/s0092-8674(02)01141-8;
RA Zhu J., Nathan C., Jin W., Sim D., Ashcroft G.S., Wahl S.M., Lacomis L.,
RA Erdjument-Bromage H., Tempst P., Wright C.D., Ding A.;
RT "Conversion of proepithelin to epithelins: roles of SLPI and elastase in
RT host defense and wound repair.";
RL Cell 111:867-878(2002).
RN [6]
RP INDUCTION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12524533; DOI=10.1038/nm816;
RA He Z., Ong C.H., Halper J., Bateman A.;
RT "Progranulin is a mediator of the wound response.";
RL Nat. Med. 9:225-229(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20026663; DOI=10.1084/jem.20091568;
RA Yin F., Banerjee R., Thomas B., Zhou P., Qian L., Jia T., Ma X., Ma Y.,
RA Iadecola C., Beal M.F., Nathan C., Ding A.;
RT "Exaggerated inflammation, impaired host defense, and neuropathology in
RT progranulin-deficient mice.";
RL J. Exp. Med. 207:117-128(2010).
RN [9]
RP INDUCTION.
RX PubMed=21092856; DOI=10.1016/j.neuron.2010.09.034;
RA Hu F., Padukkavidana T., Vaegter C.B., Brady O.A., Zheng Y.,
RA Mackenzie I.R., Feldman H.H., Nykjaer A., Strittmatter S.M.;
RT "Sortilin-mediated endocytosis determines levels of the frontotemporal
RT dementia protein, progranulin.";
RL Neuron 68:654-667(2010).
RN [10]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23041626; DOI=10.1172/jci63113;
RA Martens L.H., Zhang J., Barmada S.J., Zhou P., Kamiya S., Sun B., Min S.W.,
RA Gan L., Finkbeiner S., Huang E.J., Farese R.V. Jr.;
RT "Progranulin deficiency promotes neuroinflammation and neuron loss
RT following toxin-induced injury.";
RL J. Clin. Invest. 122:3955-3959(2012).
RN [11]
RP INTERACTION WITH PSAP.
RX PubMed=26370502; DOI=10.1083/jcb.201502029;
RA Zhou X., Sun L., Bastos de Oliveira F., Qi X., Brown W.J., Smolka M.B.,
RA Sun Y., Hu F.;
RT "Prosaposin facilitates sortilin-independent lysosomal trafficking of
RT progranulin.";
RL J. Cell Biol. 210:991-1002(2015).
RN [12]
RP INDUCTION, TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH GBA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27789271; DOI=10.1016/j.ebiom.2016.10.010;
RA Jian J., Tian Q.Y., Hettinghouse A., Zhao S., Liu H., Wei J., Grunig G.,
RA Zhang W., Setchell K.D.R., Sun Y., Overkleeft H.S., Chan G.L., Liu C.J.;
RT "Progranulin Recruits HSP70 to beta-Glucocerebrosidase and Is Therapeutic
RT Against Gaucher Disease.";
RL EBioMedicine 13:212-224(2016).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28073925; DOI=10.1093/hmg/ddx011;
RA Tanaka Y., Suzuki G., Matsuwaki T., Hosokawa M., Serrano G., Beach T.G.,
RA Yamanouchi K., Hasegawa M., Nishihara M.;
RT "Progranulin regulates lysosomal function and biogenesis through
RT acidification of lysosomes.";
RL Hum. Mol. Genet. 26:969-988(2017).
RN [14]
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=28453791; DOI=10.1093/hmg/ddx162;
RA Beel S., Moisse M., Damme M., De Muynck L., Robberecht W.,
RA Van Den Bosch L., Saftig P., Van Damme P.;
RT "Progranulin functions as a cathepsin D chaperone to stimulate axonal
RT outgrowth in vivo.";
RL Hum. Mol. Genet. 26:2850-2863(2017).
RN [15]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=28835281; DOI=10.1186/s13024-017-0205-9;
RA Zhou X., Paushter D.H., Feng T., Sun L., Reinheckel T., Hu F.;
RT "Lysosomal processing of progranulin.";
RL Mol. Neurodegener. 12:62-62(2017).
RN [16]
RP TISSUE SPECIFICITY, INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28541286; DOI=10.1038/ncomms15277;
RA Zhou X., Sun L., Bracko O., Choi J.W., Jia Y., Nana A.L., Brady O.A.,
RA Hernandez J.C.C., Nishimura N., Seeley W.W., Hu F.;
RT "Impaired prosaposin lysosomal trafficking in frontotemporal lobar
RT degeneration due to progranulin mutations.";
RL Nat. Commun. 8:15277-15277(2017).
CC -!- FUNCTION: Secreted protein that acts as a key regulator of lysosomal
CC function and as a growth factor involved in inflammation, wound healing
CC and cell proliferation (PubMed:28073925, PubMed:8496151,
CC PubMed:28541286, PubMed:28453791, PubMed:20026663, PubMed:23041626,
CC PubMed:27789271, PubMed:12524533). Regulates protein trafficking to
CC lysosomes and, also the activity of lysosomal enzymes (PubMed:28453791,
CC PubMed:28541286, PubMed:27789271). Facilitates also the acidification
CC of lysosomes, causing degradation of mature CTSD by CTSB
CC (PubMed:28073925). In addition, functions as wound-related growth
CC factor that acts directly on dermal fibroblasts and endothelial cells
CC to promote division, migration and the formation of capillary-like
CC tubule structures (PubMed:12524533). Also promotes epithelial cell
CC proliferation by blocking TNF-mediated neutrophil activation preventing
CC release of oxidants and proteases (PubMed:8496151). Moreover, modulates
CC inflammation in neurons by preserving neurons survival, axonal
CC outgrowth and neuronal integrity (PubMed:23041626, PubMed:20026663).
CC {ECO:0000269|PubMed:12524533, ECO:0000269|PubMed:20026663,
CC ECO:0000269|PubMed:23041626, ECO:0000269|PubMed:27789271,
CC ECO:0000269|PubMed:28073925, ECO:0000269|PubMed:28453791,
CC ECO:0000269|PubMed:28541286, ECO:0000269|PubMed:8496151}.
CC -!- FUNCTION: [Granulin-3]: Inhibits epithelial cell proliferation and
CC induces epithelial cells to secrete IL-8.
CC {ECO:0000250|UniProtKB:P28799}.
CC -!- FUNCTION: [Granulin-7]: Stabilizes CTSD through interaction with CTSD
CC leading to maintain its aspartic-type peptidase activity.
CC {ECO:0000250|UniProtKB:P28799}.
CC -!- SUBUNIT: Progranulin is secreted as a homodimer (By similarity).
CC Interacts with SLPI; interaction protects progranulin from proteolysis
CC (PubMed:12526812). Interacts (via region corresponding to granulin-7
CC peptide) with CTSD; stabilizes CTSD and increases its proteolytic
CC activity. Interacts (via region corresponding to granulin-7 peptide)
CC with SORT1; this interaction mediates endocytosis and lysosome delivery
CC of progranulin; interaction occurs at the neuronal cell surface in a
CC stressed nervous system (By similarity). Interacts with PSAP;
CC facilitates lysosomal delivery of progranulin from the extracellular
CC space and the biosynthetic pathway (PubMed:26370502). Forms a complex
CC with PSAP and M6PR; PSAP bridges the binding between progranulin and
CC M6PR. Forms a complex with PSAP and SORT1; progranulin bridges the
CC interaction between PSAP and SORT1; facilitates lysosomal targeting of
CC PSAP via SORT1; interaction enhances PSAP uptake in primary cortical
CC neurons (By similarity). Interacts (via regions corresponding to
CC granulin-2 and granulin-7 peptides) with GBA; this interaction prevents
CC aggregation of GBA-SCARB2 complex via interaction with HSPA1A upon
CC stress (PubMed:27789271). Interacts (via region corresponding to
CC granulin-7 peptide) with HSPA1A; mediates recruitment of HSPA1A to GBA
CC and prevents GBA aggregation in response to stress (By similarity).
CC {ECO:0000250|UniProtKB:P28799, ECO:0000269|PubMed:12526812,
CC ECO:0000269|PubMed:26370502, ECO:0000269|PubMed:27789271}.
CC -!- INTERACTION:
CC P28798; Q61207: Psap; NbExp=4; IntAct=EBI-2365205, EBI-645756;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28073925,
CC ECO:0000269|PubMed:28541286, ECO:0000269|PubMed:8496151}. Lysosome
CC {ECO:0000269|PubMed:27789271, ECO:0000269|PubMed:28073925}.
CC Note=Endocytosed by SORT1 and delivred to lysosomes. Targeted to
CC lysosome by PSAP via M6PR and LRP1, in both biosynthetic and endocytic
CC pathways (By similarity). Co-localized with GBA in the intracellular
CC trafficking compartments until to lysosome (PubMed:27789271).
CC {ECO:0000250|UniProtKB:P28799, ECO:0000269|PubMed:27789271}.
CC -!- TISSUE SPECIFICITY: Highly expressed at the wound site and diminishes
CC away from the wound. Not expressed in fibroblasts and endothelial cells
CC in intact skin (PubMed:12524533). In adult brain, expressed primarily
CC in neurons and in resting and reactive microglia (PubMed:23041626).
CC Expressed in both neurons and microglia. Highly expressed in activated
CC microglia in response to injury (PubMed:28541286). Expressed in
CC macrophage (PubMed:27789271). {ECO:0000269|PubMed:12524533,
CC ECO:0000269|PubMed:23041626, ECO:0000269|PubMed:27789271,
CC ECO:0000269|PubMed:28541286}.
CC -!- INDUCTION: Injury-stimulated induction in the fibroblasts and
CC endothelial cells and by inflammatory cells entering the wound
CC (PubMed:12524533). Injury-stimulated induction in neurons
CC (PubMed:28453791). Strongly induced in activated microglial cells that
CC surround motor neurons after peripheral axonal injury, but not by
CC astrocytes (PubMed:21092856). Up-regulated in response to a cortical
CC injury. Up-regulated in activated glia during normal aging
CC (PubMed:28541286). Induced in response to inflammation
CC (PubMed:27789271). {ECO:0000269|PubMed:12524533,
CC ECO:0000269|PubMed:21092856, ECO:0000269|PubMed:27789271,
CC ECO:0000269|PubMed:28453791, ECO:0000269|PubMed:28541286}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8496151}.
CC -!- PTM: Cleaved by ELANE; proteolysis is blocked by SLPI and is
CC concentration- and time-dependent and induces CXCL8/IL-8 production;
CC granulin-3 and granulin-4 are resistant to ELANE (By similarity).
CC Cleaved by CTSL in lysosome thus regulating the maturation and turnover
CC of progranulin within the lysosome (PubMed:28835281).
CC {ECO:0000250|UniProtKB:P28799, ECO:0000269|PubMed:28835281}.
CC -!- DISRUPTION PHENOTYPE: Young-adult Grn knockout mice are healthy and
CC fertile, grow normally and show no abnormalities in hematogram or serum
CC chemistries. However mice show an exaggerated inflammation, impaired
CC host defense, and neuropathology (PubMed:20026663). Grn knockout mice
CC displays a neuronal outgrowth deficit. Conditional knockout Grn mice in
CC neuron show a significant delay in axonal regrowth and functional
CC recovery after crush (PubMed:28453791). Grn knockout mice show an
CC increase neuron death and microglial activation upon central nervous
CC system injury (CNS). Conditional knockout Grn mice exhibit a reduction
CC in dopaminergic neurons and increased microgliosis after CNS injury
CC (PubMed:23041626). {ECO:0000269|PubMed:20026663,
CC ECO:0000269|PubMed:23041626, ECO:0000269|PubMed:28453791}.
CC -!- SIMILARITY: Belongs to the granulin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D16195; BAA03736.1; -; Genomic_DNA.
DR EMBL; M86736; AAA37191.1; -; mRNA.
DR EMBL; X62321; CAA44197.1; -; mRNA.
DR PIR; C38128; C38128.
DR RefSeq; NP_032201.2; NM_008175.4.
DR AlphaFoldDB; P28798; -.
DR SMR; P28798; -.
DR IntAct; P28798; 7.
DR MINT; P28798; -.
DR STRING; 10090.ENSMUSP00000046340; -.
DR GlyGen; P28798; 4 sites.
DR iPTMnet; P28798; -.
DR PhosphoSitePlus; P28798; -.
DR CPTAC; non-CPTAC-3399; -.
DR CPTAC; non-CPTAC-3917; -.
DR EPD; P28798; -.
DR jPOST; P28798; -.
DR PaxDb; P28798; -.
DR PeptideAtlas; P28798; -.
DR PRIDE; P28798; -.
DR ProteomicsDB; 269840; -.
DR Antibodypedia; 1406; 668 antibodies from 38 providers.
DR DNASU; 14824; -.
DR Ensembl; ENSMUST00000239431; ENSMUSP00000159379; ENSMUSG00000034708.
DR GeneID; 14824; -.
DR KEGG; mmu:14824; -.
DR CTD; 2896; -.
DR MGI; MGI:95832; Grn.
DR VEuPathDB; HostDB:ENSMUSG00000034708; -.
DR eggNOG; KOG4296; Eukaryota.
DR GeneTree; ENSGT00470000042293; -.
DR InParanoid; P28798; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR ChiTaRS; Grn; mouse.
DR PRO; PR:P28798; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P28798; protein.
DR Bgee; ENSMUSG00000034708; Expressed in stroma of bone marrow and 272 other tissues.
DR ExpressionAtlas; P28798; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0002265; P:astrocyte activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0001835; P:blastocyst hatching; IDA:MGI.
DR GO; GO:0035988; P:chondrocyte proliferation; ISO:MGI.
DR GO; GO:0007566; P:embryo implantation; IDA:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IMP:MGI.
DR GO; GO:0007041; P:lysosomal transport; IMP:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:UniProtKB.
DR GO; GO:0060179; P:male mating behavior; ISO:MGI.
DR GO; GO:0002282; P:microglial cell activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:1903979; P:negative regulation of microglial cell activation; IMP:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1902564; P:negative regulation of neutrophil activation; ISS:UniProtKB.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0061351; P:neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:1905247; P:positive regulation of aspartic-type peptidase activity; IMP:UniProtKB.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:MGI.
DR GO; GO:0106016; P:positive regulation of inflammatory response to wounding; IDA:UniProtKB.
DR GO; GO:1905673; P:positive regulation of lysosome organization; IDA:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1903334; P:positive regulation of protein folding; IMP:UniProtKB.
DR GO; GO:1904075; P:positive regulation of trophectodermal cell proliferation; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:1905671; P:regulation of lysosome organization; IMP:MGI.
DR GO; GO:0032355; P:response to estradiol; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0001834; P:trophectodermal cell proliferation; IDA:MGI.
DR Gene3D; 2.10.25.160; -; 7.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR039036; Granulin_fam.
DR InterPro; IPR037277; Granulin_sf.
DR PANTHER; PTHR12274; PTHR12274; 1.
DR Pfam; PF00396; Granulin; 7.
DR SMART; SM00277; GRAN; 7.
DR PROSITE; PS00799; GRANULINS; 7.
PE 1: Evidence at protein level;
KW Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lysosome; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:8496151"
FT CHAIN 18..589
FT /note="Paragranulin"
FT /id="PRO_0000012702"
FT PEPTIDE 18..47
FT /note="Paragranulin"
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT /id="PRO_0000446331"
FT PEPTIDE ?58..?113
FT /note="Granulin-1"
FT /id="PRO_0000012703"
FT PEPTIDE ?122..?178
FT /note="Granulin-2"
FT /id="PRO_0000012704"
FT PEPTIDE 205..260
FT /note="Granulin-3"
FT /id="PRO_0000012705"
FT PEPTIDE 280..334
FT /note="Granulin-4"
FT /id="PRO_0000012706"
FT PEPTIDE 362..?414
FT /note="Granulin-5"
FT /id="PRO_0000012707"
FT PEPTIDE 440..?493
FT /note="Granulin-6"
FT /id="PRO_0000012708"
FT PEPTIDE ?517..?568
FT /note="Granulin-7"
FT /id="PRO_0000012709"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..138
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 132..148
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 282..294
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 288..304
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 295..312
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 305..319
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 313..326
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 320..333
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 364..376
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 370..386
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 395..408
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT DISULFID 402..414
FT /evidence="ECO:0000250|UniProtKB:P28799"
FT CONFLICT 251
FT /note="V -> L (in Ref. 3; AAA37191)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="L -> V (in Ref. 3; AAA37191)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..263
FT /note="SKN -> YD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="L -> R (in Ref. 2; CAA44197)"
FT /evidence="ECO:0000305"
FT CONFLICT 402..403
FT /note="CP -> SA (in Ref. 3; AAA37191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 63458 MW; 1DE8229C413CB787 CRC64;
MWVLMSWLAF AAGLVAGTQC PDGQFCPVAC CLDQGGANYS CCNPLLDTWP RITSHHLDGS
CQTHGHCPAG YSCLLTVSGT SSCCPFSKGV SCGDGYHCCP QGFHCSADGK SCFQMSDNPL
GAVQCPGSQF ECPDSATCCI MVDGSWGCCP MPQASCCEDR VHCCPHGASC DLVHTRCVSP
TGTHTLLKKF PAQKTNRAVS LPFSVVCPDA KTQCPDDSTC CELPTGKYGC CPMPNAICCS
DHLHCCPQDT VCDLIQSKCL SKNYTTDLLT KLPGYPVKEV KCDMEVSCPE GYTCCRLNTG
AWGCCPFAKA VCCEDHIHCC PAGFQCHTEK GTCEMGILQV PWMKKVIAPL RLPDPQILKS
DTPCDDFTRC PTNNTCCKLN SGDWGCCPIP EAVCCSDNQH CCPQGFTCLA QGYCQKGDTM
VAGLEKIPAR QTTPLQIGDI GCDQHTSCPV GQTCCPSLKG SWACCQLPHA VCCEDRQHCC
PAGYTCNVKA RTCEKDVDFI QPPVLLTLGP KVGNVECGEG HFCHDNQTCC KDSAGVWACC
PYLKGVCCRD GRHCCPGGFH CSARGTKCLR KKIPRWDMFL RDPVPRPLL
