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-NOV-2009, entry version 76. DE RecName: Full=Granulins; DE AltName: Full=Proepithelin; DE Short=PEPI; DE AltName: Full=PC cell-derived growth factor; DE Short=PCDGF; DE Contains: DE RecName: Full=Acrogranin; 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=93245991; 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 RT epithelin/granulin precursor (acrogranin)."; RL FEBS Lett. 322:89-94(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Kidney; RX MEDLINE=92317004; PubMed=1618805; 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 RT on epithelial cell growth."; RL J. Biol. Chem. 267:13073-13078(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93228994; PubMed=8471244; DOI=10.1002/mrd.1080340302; RA Baba T., Hoff H.B. III, Nemoto H., Lee H., Orth J., Arai Y., RA Gerton G.L.; RT "Acrogranin, an acrosomal cysteine-rich glycoprotein, is the precursor RT of the growth-modulating peptides, granulins, and epithelins, and is RT expressed 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; RP 259-280; 297-304 AND 421-430, FUNCTION, GLYCOSYLATION, AND SUBCELLULAR RP LOCATION. RX PubMed=8496151; RA Zhou J., Gao G., Crabb J.W., Serrero G.; RT "Purification of an autocrine growth factor homologous with mouse RT epithelin precursor from a highly tumorigenic cell line."; RL J. Biol. Chem. 268:10863-10869(1993). CC -!- FUNCTION: Granulins have possible cytokine-like activity. They may CC play a role in inflammation, wound repair, and tissue remodeling. CC Acts as an autocrine growth factor for PC cells. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: Granulins are disulfide bridged. CC -!- PTM: N-glycosylated. CC -!- SIMILARITY: Belongs to the granulin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D16195; BAA03736.1; -; Genomic_DNA. DR EMBL; M86736; AAA37191.1; -; mRNA. DR EMBL; X62321; CAA44197.1; -; mRNA. DR IPI; IPI00124640; -. DR PIR; C38128; C38128. DR UniGene; Mm.1568; -. DR HSSP; P28799; 1G26. DR IntAct; P28798; 1. DR STRING; P28798; -. DR PRIDE; P28798; -. DR Ensembl; ENSMUST00000049460; ENSMUSP00000046340; ENSMUSG00000034708; Mus musculus. DR UCSC; uc007lrv.1; mouse. DR MGI; MGI:95832; Grn. DR HOVERGEN; P28798; -. DR NextBio; 287027; -. DR ArrayExpress; P28798; -. DR Bgee; P28798; -. DR CleanEx; MM_GRN; -. DR Genevestigator; P28798; -. DR GermOnline; ENSMUSG00000034708; Mus musculus. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW. DR GO; GO:0001835; P:blastocyst hatching; IDA:MGI. DR GO; GO:0007566; P:embryo implantation; IDA:MGI. DR GO; GO:0050679; P:positive regulation of epithelial cell prol...; IDA:MGI. DR InterPro; IPR000118; Granulin. 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 Repeat; Secreted; Signal. FT SIGNAL 1 17 FT CHAIN 18 589 Acrogranin. FT /FTId=PRO_0000012702. FT PEPTIDE ?58 ?113 Granulin-1. FT /FTId=PRO_0000012703. FT PEPTIDE ?122 ?178 Granulin-2. FT /FTId=PRO_0000012704. FT PEPTIDE 205 260 Granulin-3. FT /FTId=PRO_0000012705. FT PEPTIDE 280 334 Granulin-4. FT /FTId=PRO_0000012706. FT PEPTIDE 362 ?414 Granulin-5. FT /FTId=PRO_0000012707. FT PEPTIDE 440 ?493 Granulin-6. FT /FTId=PRO_0000012708. FT PEPTIDE ?517 ?568 Granulin-7. FT /FTId=PRO_0000012709. FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 263 263 N-linked (GlcNAc...) (Potential). FT CARBOHYD 373 373 N-linked (GlcNAc...) (Potential). FT CARBOHYD 526 526 N-linked (GlcNAc...) (Potential). FT CONFLICT 251 251 V -> L (in Ref. 3; AAA37191). FT CONFLICT 254 254 L -> V (in Ref. 3; AAA37191). FT CONFLICT 261 263 SKN -> YD (in Ref. 4; AA sequence). FT CONFLICT 350 350 L -> R (in Ref. 2; CAA44197). FT CONFLICT 402 403 CP -> SA (in Ref. 3; AAA37191). 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 //