ID PEDF_MOUSE Reviewed; 417 AA. AC P97298; O70629; O88691; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2004, sequence version 2. DT 24-JAN-2024, entry version 169. DE RecName: Full=Pigment epithelium-derived factor; DE Short=PEDF; DE AltName: Full=Caspin; DE AltName: Full=Serpin F1; DE AltName: Full=Stromal cell-derived factor 3; DE Short=SDF-3; DE Flags: Precursor; GN Name=Serpinf1; Synonyms=Pedf, Sdf3; 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 [MRNA]. RX PubMed=8938438; DOI=10.1006/geno.1996.0560; RA Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M., RA Hamada T., Sato T., Nakano T., Honjo T.; RT "Characterization of novel secreted and membrane proteins isolated by the RT signal sequence trap method."; RL Genomics 37:273-280(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-66; 252-261; 333-344 AND RP 359-372, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=BALB/cJ; TISSUE=Liver; RX PubMed=9614124; DOI=10.1074/jbc.273.24.15125; RA Kozaki K., Miyaishi O., Koiwai O., Yasui Y., Kashiwai A., Nishikawa Y., RA Shimizu S., Saga S.; RT "Isolation, purification and characterization of a collagen-associated RT serpin, caspin, produced by murine colon adenocarcinoma cells."; RL J. Biol. Chem. 273:15125-15130(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=9565647; RA Singh V.K., Chader G.J., Rodriguez I.R.; RT "Structural and comparative analysis of the mouse gene for pigment RT epithelium-derived factor (PEDF)."; RL Mol. Vis. 4:7-7(1998). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BALB/cJ; RA Tombran-Tink J.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION. RX PubMed=12632345; DOI=10.1053/jpsu.2003.50104; RA Abramson L.P., Stellmach V., Doll J.A., Cornwell M., Arensman R.M., RA Crawford S.E.; RT "Wilms' tumor growth is suppressed by antiangiogenic pigment epithelium- RT derived factor in a xenograft model."; RL J. Pediatr. Surg. 38:336-342(2003). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, 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). CC -!- FUNCTION: Neurotrophic protein; induces extensive neuronal CC differentiation in retinoblastoma cells. Potent inhibitor of CC angiogenesis. As it does not undergo the S (stressed) to R (relaxed) CC conformational transition characteristic of active serpins, it exhibits CC no serine protease inhibitory activity. {ECO:0000269|PubMed:12632345}. CC -!- SUBUNIT: Interacts with PNPLA2; this interaction stimulates the CC phospholipase A2 activity of PNPLA2. {ECO:0000250|UniProtKB:P36955}. CC -!- SUBCELLULAR LOCATION: Secreted. Melanosome {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, gastric glandular CC mucosa and renal tubules. It is also expressed in the brain, heart, CC lung retina and testes. {ECO:0000269|PubMed:9565647, CC ECO:0000269|PubMed:9614124}. CC -!- DEVELOPMENTAL STAGE: First detected at 12.5 dpc in cartilage CC primordium, it is present in the osseous matrix of developing limbs, CC vertebrae, ribs and skull. At 16.5 dpc it is detected in bone matrix CC and smooth muscle, and at lower levels in connective tissue, bronchial CC epithelial cells, metanephron microtubules, and skin. CC {ECO:0000269|PubMed:9614124}. CC -!- SIMILARITY: Belongs to the serpin 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; D50460; BAA09051.1; -; mRNA. DR EMBL; AF036164; AAC69271.1; -; mRNA. DR EMBL; D87975; BAA31978.1; -; mRNA. DR EMBL; AF017055; AAC05733.1; -; Genomic_DNA. DR EMBL; AF017051; AAC05733.1; JOINED; Genomic_DNA. DR EMBL; AF017052; AAC05733.1; JOINED; Genomic_DNA. DR EMBL; AF017053; AAC05733.1; JOINED; Genomic_DNA. DR EMBL; AF017054; AAC05733.1; JOINED; Genomic_DNA. DR EMBL; AF017057; AAC05731.1; -; mRNA. DR EMBL; BC019852; AAH19852.1; -; mRNA. DR CCDS; CCDS25045.1; -. DR RefSeq; NP_035470.3; NM_011340.3. DR PDB; 6LOS; X-ray; 2.48 A; A=37-416. DR PDBsum; 6LOS; -. DR AlphaFoldDB; P97298; -. DR SMR; P97298; -. DR BioGRID; 203140; 12. DR IntAct; P97298; 1. DR MINT; P97298; -. DR STRING; 10090.ENSMUSP00000000769; -. DR MEROPS; I04.979; -. DR GlyCosmos; P97298; 1 site, No reported glycans. DR GlyGen; P97298; 1 site. DR PhosphoSitePlus; P97298; -. DR CPTAC; non-CPTAC-3389; -. DR CPTAC; non-CPTAC-3390; -. DR PaxDb; 10090-ENSMUSP00000000769; -. DR PeptideAtlas; P97298; -. DR ProteomicsDB; 287671; -. DR Pumba; P97298; -. DR Antibodypedia; 865; 766 antibodies from 38 providers. DR DNASU; 20317; -. DR Ensembl; ENSMUST00000000769.14; ENSMUSP00000000769.8; ENSMUSG00000000753.16. DR GeneID; 20317; -. DR KEGG; mmu:20317; -. DR UCSC; uc007kdp.1; mouse. DR AGR; MGI:108080; -. DR CTD; 5176; -. DR MGI; MGI:108080; Serpinf1. DR VEuPathDB; HostDB:ENSMUSG00000000753; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000158112; -. DR HOGENOM; CLU_023330_3_1_1; -. DR InParanoid; P97298; -. DR OMA; QEVNNWV; -. DR OrthoDB; 5316968at2759; -. DR PhylomeDB; P97298; -. DR TreeFam; TF317350; -. DR BioGRID-ORCS; 20317; 4 hits in 78 CRISPR screens. DR ChiTaRS; Serpinf1; mouse. DR PRO; PR:P97298; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P97298; Protein. DR Bgee; ENSMUSG00000000753; Expressed in vault of skull and 249 other cell types or tissues. DR ExpressionAtlas; P97298; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0043203; C:axon hillock; ISO:MGI. DR GO; GO:0005604; C:basement membrane; ISO:MGI. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:MGI. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central. DR GO; GO:0071279; P:cellular response to cobalt ion; IEA:Ensembl. DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl. DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IMP:MGI. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB. DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI. DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl. DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:0010447; P:response to acidic pH; IEA:Ensembl. DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI. DR GO; GO:1901652; P:response to peptide; ISO:MGI. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR GO; GO:0007614; P:short-term memory; ISO:MGI. DR CDD; cd02052; serpinF1_PEDF; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1. DR InterPro; IPR033832; PEDF_serpin_dom. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR InterPro; IPR036186; Serpin_sf. DR InterPro; IPR042178; Serpin_sf_1. DR InterPro; IPR042185; Serpin_sf_2. DR PANTHER; PTHR11461:SF84; PIGMENT EPITHELIUM-DERIVED FACTOR; 1. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00284; SERPIN; 1. DR Genevisible; P97298; MM. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycoprotein; Phosphoprotein; KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000250" FT CHAIN 20..417 FT /note="Pigment epithelium-derived factor" FT /id="PRO_0000032509" FT REGION 17..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..32 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 20 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000250|UniProtKB:P36955" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36955" FT CARBOHYD 284 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 70 FT /note="S -> G (in Ref. 4; AAC69271)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="K -> N (in Ref. 2; BAA31978)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="S -> R (in Ref. 4; AAC69271)" FT /evidence="ECO:0000305" FT CONFLICT 280 FT /note="T -> A (in Ref. 1; BAA09051)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="Q -> L (in Ref. 4; AAC69271)" FT /evidence="ECO:0000305" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 49..70 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 81..91 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 97..106 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 117..128 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 135..143 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 151..161 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 172..186 FT /evidence="ECO:0007829|PDB:6LOS" FT TURN 187..189 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 203..213 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 226..230 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 232..235 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 238..255 FT /evidence="ECO:0007829|PDB:6LOS" FT TURN 256..259 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 260..267 FT /evidence="ECO:0007829|PDB:6LOS" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 271..280 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 286..289 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 305..314 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 316..323 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 325..329 FT /evidence="ECO:0007829|PDB:6LOS" FT TURN 330..333 FT /evidence="ECO:0007829|PDB:6LOS" FT HELIX 334..337 FT /evidence="ECO:0007829|PDB:6LOS" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 352..363 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 385..388 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 393..399 FT /evidence="ECO:0007829|PDB:6LOS" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:6LOS" FT STRAND 405..412 FT /evidence="ECO:0007829|PDB:6LOS" SQ SEQUENCE 417 AA; 46234 MW; ECD360FE6AA74D25 CRC64; MQALVLLLWT GALLGHGSSQ NVPSSSEGSP VPDSTGEPVE EEDPFFKVPV NKLAAAVSNF GYDLYRLRSS ASPTGNVLLS PLSVATALSA LSLGAEHRTE SVIHRALYYD LITNPDIHST YKELLASVTA PEKNLKSASR IVFERKLRVK SSFVAPLEKS YGTRPRILTG NPRVDLQEIN NWVQAQMKGK IARSTREMPS ALSILLLGVA YFKGQWVTKF DSRKTTLQDF HLDEDRTVRV PMMSDPKAIL RYGLDSDLNC KIAQLPLTGS MSIIFFLPLT VTQNLTMIEE SLTSEFIHDI DRELKTIQAV LTVPKLKLSF EGELTKSLQD MKLQSLFESP DFSKITGKPV KLTQVEHRAA FEWNEEGAGS SPSPGLQPVR LTFPLDYHLN QPFLFVLRDT DTGALLFIGR ILDPSST //