ID PEDF_HUMAN Reviewed; 418 AA. AC P36955; F1T092; Q13236; Q2TU83; Q96CT1; Q96R01; Q9BWA4; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 4. DT 27-MAR-2024, entry version 223. DE RecName: Full=Pigment epithelium-derived factor; DE Short=PEDF; DE AltName: Full=Cell proliferation-inducing gene 35 protein; DE AltName: Full=EPC-1; DE AltName: Full=Serpin F1; DE Flags: Precursor; GN Name=SERPINF1; Synonyms=PEDF; ORFNames=PIG35; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT MET-72. RC TISSUE=Fetal eye; RX PubMed=8434014; DOI=10.1073/pnas.90.4.1526; RA Steele F.R., Chader G.J., Johnson L.V., Tombran-Tink J.; RT "Pigment epithelium-derived factor: neurotrophic activity and RT identification as a member of the serine protease inhibitor gene family."; RL Proc. Natl. Acad. Sci. U.S.A. 90:1526-1530(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-72. RX PubMed=9238088; RA Tombran-Tink J., Mazuruk K., Rodriguez I.R., Chung D., Linker T., RA Englander E., Chader G.J.; RT "Organization, evolutionary conservation, expression and unusual Alu RT density of the human gene for pigment epithelium-derived factor, a unique RT neurotrophic serpin."; RL Mol. Vis. 2:11-11(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MET-72. RA Yin B., Peng X., Yuan J., Qiang B.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-72. RC TISSUE=Liver cancer; RA Kim J.W.; RT "Identification of a human cell proliferation inducing gene."; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=21697133; DOI=10.1167/iovs.11-7479; RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., RA Usami R., Ohtoko K., Kato S.; RT "Full-length transcriptome analysis of human retina-derived cell lines RT ARPE-19 and Y79 using the vector-capping method."; RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-72. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-72 AND ARG-132. RC TISSUE=Muscle; 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 [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-332, AND VARIANT MET-72. RC TISSUE=Fetal lung fibroblast; RA Coljee V.W.; RL Thesis (1996), Medical College of Pennsylvania, United States. RN [11] RP PROTEIN SEQUENCE OF 21-29; 253-262 AND 282-303, TISSUE SPECIFICITY, AND RP PYROGLUTAMATE FORMATION AT GLN-20. RC TISSUE=Plasma; RX PubMed=12737624; DOI=10.1042/bj20030313; RA Petersen S.V., Valnickova Z., Enghild J.J.; RT "Pigment-epithelium-derived factor (PEDF) occurs at a physiologically RT relevant concentration in human blood: purification and characterization."; RL Biochem. J. 374:199-206(2003). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-418, AND VARIANT MET-72. RC TISSUE=Fetal lung fibroblast; RX PubMed=8473338; DOI=10.1016/s0021-9258(18)52964-1; RA Pignolo R.J., Cristofalo V.J., Rotenberg M.O.; RT "Senescent WI-38 cells fail to express EPC-1, a gene induced in young cells RT upon entry into the G0 state."; RL J. Biol. Chem. 268:8949-8957(1993). RN [13] RP FUNCTION. RX PubMed=8226833; DOI=10.1016/s0021-9258(19)49439-8; RA Becerra S.P., Palmer I., Kumar A., Steele F.R., Shiloach J., Notario V., RA Chader G.J.; RT "Overexpression of fetal human pigment epithelium-derived factor in RT Escherichia coli. A functionally active neurotrophic factor."; RL J. Biol. Chem. 268:23148-23156(1993). RN [14] RP FUNCTION. RX PubMed=7592790; DOI=10.1074/jbc.270.43.25992; RA Becerra S.P., Sagasti A., Spinella P., Notario V.; RT "Pigment epithelium-derived factor behaves like a noninhibitory serpin. RT Neurotrophic activity does not require the serpin reactive loop."; RL J. Biol. Chem. 270:25992-25999(1995). RN [15] RP PHOSPHORYLATION AT SER-24; SER-114 AND SER-227. RX PubMed=15374885; DOI=10.1182/blood-2004-04-1569; RA Maik-Rachline G., Shaltiel S., Seger R.; RT "Extracellular phosphorylation converts pigment epithelium-derived factor RT from a neurotrophic to an antiangiogenic factor."; RL Blood 105:670-678(2005). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-285. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [17] RP INTERACTION WITH PNPLA2. RX PubMed=17032652; DOI=10.1074/jbc.m600353200; RA Notari L., Baladron V., Aroca-Aguilar J.D., Balko N., Heredia R., Meyer C., RA Notario P.M., Saravanamuthu S., Nueda M.-L., Sanchez-Sanchez F., RA Escribano J., Laborda J., Becerra S.P.; RT "Identification of a lipase-linked cell membrane receptor for pigment RT epithelium-derived factor."; RL J. Biol. Chem. 281:38022-38037(2006). RN [18] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-285. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [20] RP GLYCOSYLATION AT ASN-285. RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., RA Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core fucosylated RT glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS], AND STRUCTURE OF CARBOHYDRATES. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., RA Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [22] RP INVOLVEMENT IN OI6. RX PubMed=21353196; DOI=10.1016/j.ajhg.2011.01.015; RA Becker J., Semler O., Gilissen C., Li Y., Bolz H.J., Giunta C., RA Bergmann C., Rohrbach M., Koerber F., Zimmermann K., de Vries P., Wirth B., RA Schoenau E., Wollnik B., Veltman J.A., Hoischen A., Netzer C.; RT "Exome sequencing identifies truncating mutations in human SERPINF1 in RT autosomal-recessive osteogenesis imperfecta."; RL Am. J. Hum. Genet. 88:362-371(2011). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 21-418, AND GLYCOSYLATION AT RP ASN-285. RX PubMed=11562499; DOI=10.1073/pnas.211268598; RA Simonovic M., Gettins P.G.W., Volz K.; RT "Crystal structure of human PEDF, a potent anti-angiogenic and neurite RT growth-promoting factor."; RL Proc. Natl. Acad. Sci. U.S.A. 98:11131-11135(2001). RN [26] RP VARIANT MET-72. RX PubMed=10398730; RA Koenekoop R., Pina A.L., Loyer M., Davidson J., Robitaille J., Maumenee I., RA Tombran-Tink J.; RT "Four polymorphic variations in the PEDF gene identified during the RT mutation screening of patients with Leber congenital amaurosis."; RL Mol. Vis. 5:10-10(1999). RN [27] RP VARIANT MET-72, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22028381; DOI=10.1093/jmcb/mjr024; RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., RA Zeng R., Wu J.R.; RT "Quantitative detection of single amino acid polymorphisms by targeted RT proteomics."; RL J. Mol. Cell Biol. 3:309-315(2011). 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:7592790, CC ECO:0000269|PubMed:8226833}. CC -!- SUBUNIT: Interacts with PNPLA2; this interaction stimulates the CC phospholipase A2 activity of PNPLA2. {ECO:0000269|PubMed:17032652}. CC -!- INTERACTION: CC P36955; Q7L775: EPM2AIP1; NbExp=11; IntAct=EBI-2932733, EBI-6255981; CC P36955; Q9P2X3: IMPACT; NbExp=3; IntAct=EBI-2932733, EBI-2857352; CC P36955; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2932733, EBI-744081; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17081065}. CC Melanosome {ECO:0000269|PubMed:17081065}. Note=Enriched in stage I CC melanosomes. CC -!- TISSUE SPECIFICITY: Retinal pigment epithelial cells and blood plasma. CC {ECO:0000269|PubMed:12737624}. CC -!- DEVELOPMENTAL STAGE: Expressed in quiescent cells. CC -!- DOMAIN: The N-terminal (AA 44-121) exhibits neurite outgrowth-inducing CC activity. The C-terminal exposed loop (AA 382-418) is essential for CC serpin activity. CC -!- PTM: The N-terminus is blocked. Extracellular phosphorylation enhances CC antiangiogenic activity. {ECO:0000269|PubMed:15374885}. CC -!- PTM: N- and O-glycosylated. O-glycosylated with a core 1 or possibly CC core 8 glycan. {ECO:0000269|PubMed:11562499, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169}. CC -!- DISEASE: Osteogenesis imperfecta 6 (OI6) [MIM:613982]: A form of CC osteogenesis imperfecta, a connective tissue disorder characterized by CC low bone mass, bone fragility and susceptibility to fractures after CC minimal trauma. Disease severity ranges from very mild forms without CC fractures to intrauterine fractures and perinatal lethality. CC Extraskeletal manifestations, which affect a variable number of CC patients, are dentinogenesis imperfecta, hearing loss, and blue CC sclerae. OI6 is a severe, autosomal recessive form compatible with OI CC type III in the Sillence classification. {ECO:0000269|PubMed:21353196}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA84914.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAA93524.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; M76979; AAA60058.1; -; mRNA. DR EMBL; U29953; AAA84914.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF400442; AAK92491.1; -; mRNA. DR EMBL; BT007222; AAP35886.1; -; mRNA. DR EMBL; AY513280; AAT08033.1; -; mRNA. DR EMBL; AB593011; BAJ83966.1; -; mRNA. DR EMBL; AB593012; BAJ83967.1; -; mRNA. DR EMBL; AB593013; BAJ83968.1; -; mRNA. DR EMBL; AC130343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC130689; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471108; EAW90577.1; -; Genomic_DNA. DR EMBL; BC000522; AAH00522.1; -; mRNA. DR EMBL; BC013984; AAH13984.1; -; mRNA. DR EMBL; AH004879; AAB38685.1; -; Genomic_DNA. DR EMBL; M90439; AAA93524.1; ALT_INIT; mRNA. DR CCDS; CCDS11012.1; -. DR PIR; A46046; A46046. DR PIR; A47281; A47281. DR RefSeq; NP_001316832.1; NM_001329903.1. DR RefSeq; NP_002606.3; NM_002615.6. DR PDB; 1IMV; X-ray; 2.85 A; A=21-418. DR PDBsum; 1IMV; -. DR AlphaFoldDB; P36955; -. DR SMR; P36955; -. DR BioGRID; 111202; 39. DR IntAct; P36955; 17. DR MINT; P36955; -. DR STRING; 9606.ENSP00000254722; -. DR ChEMBL; CHEMBL4295753; -. DR DrugBank; DB09130; Copper. DR MEROPS; I04.979; -. DR GlyConnect; 645; 7 N-Linked glycans (1 site). DR GlyCosmos; P36955; 6 sites, 8 glycans. DR GlyGen; P36955; 7 sites, 11 N-linked glycans (1 site), 3 O-linked glycans (6 sites). DR iPTMnet; P36955; -. DR PhosphoSitePlus; P36955; -. DR BioMuta; SERPINF1; -. DR DMDM; 313104314; -. DR REPRODUCTION-2DPAGE; IPI00006114; -. DR CPTAC; non-CPTAC-1146; -. DR EPD; P36955; -. DR jPOST; P36955; -. DR MassIVE; P36955; -. DR MaxQB; P36955; -. DR PaxDb; 9606-ENSP00000254722; -. DR PeptideAtlas; P36955; -. DR ProteomicsDB; 55243; -. DR Pumba; P36955; -. DR Antibodypedia; 865; 766 antibodies from 38 providers. DR DNASU; 5176; -. DR Ensembl; ENST00000254722.9; ENSP00000254722.4; ENSG00000132386.11. DR GeneID; 5176; -. DR KEGG; hsa:5176; -. DR MANE-Select; ENST00000254722.9; ENSP00000254722.4; NM_002615.7; NP_002606.3. DR UCSC; uc002ftl.4; human. DR AGR; HGNC:8824; -. DR CTD; 5176; -. DR DisGeNET; 5176; -. DR GeneCards; SERPINF1; -. DR HGNC; HGNC:8824; SERPINF1. DR HPA; ENSG00000132386; Tissue enriched (choroid). DR MalaCards; SERPINF1; -. DR MIM; 172860; gene. DR MIM; 613982; phenotype. DR neXtProt; NX_P36955; -. DR OpenTargets; ENSG00000132386; -. DR Orphanet; 216812; Osteogenesis imperfecta type 3. DR Orphanet; 216820; Osteogenesis imperfecta type 4. DR PharmGKB; PA35508; -. DR VEuPathDB; HostDB:ENSG00000132386; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000158112; -. DR HOGENOM; CLU_023330_3_1_1; -. DR InParanoid; P36955; -. DR OMA; QEVNNWV; -. DR OrthoDB; 5316968at2759; -. DR PhylomeDB; P36955; -. DR TreeFam; TF317350; -. DR PathwayCommons; P36955; -. DR SignaLink; P36955; -. DR SIGNOR; P36955; -. DR BioGRID-ORCS; 5176; 10 hits in 1157 CRISPR screens. DR ChiTaRS; SERPINF1; human. DR EvolutionaryTrace; P36955; -. DR GeneWiki; PEDF; -. DR GenomeRNAi; 5176; -. DR Pharos; P36955; Tbio. DR PRO; PR:P36955; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P36955; Protein. DR Bgee; ENSG00000132386; Expressed in pigmented layer of retina and 201 other cell types or tissues. DR ExpressionAtlas; P36955; baseline and differential. DR GO; GO:0043203; C:axon hillock; IEA:Ensembl. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. 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; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl. DR GO; GO:0050769; P:positive regulation of neurogenesis; IDA:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. 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:1901652; P:response to peptide; IEA:Ensembl. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR GO; GO:0007614; P:short-term memory; IEA:Ensembl. 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; P36955; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Dwarfism; Glycoprotein; KW Osteogenesis imperfecta; Phosphoprotein; Pyrrolidone carboxylic acid; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..19 FT CHAIN 20..418 FT /note="Pigment epithelium-derived factor" FT /id="PRO_0000032508" FT REGION 20..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 371..383 FT /note="O-glycosylated at one site" FT MOD_RES 20 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:12737624" FT MOD_RES 24 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15374885" FT MOD_RES 114 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15374885" FT MOD_RES 227 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:15374885" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:11562499, FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218" FT VARIANT 72 FT /note="T -> M (confirmed at protein level; FT dbSNP:rs1136287)" FT /evidence="ECO:0000269|PubMed:10398730, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:8434014, ECO:0000269|PubMed:8473338, FT ECO:0000269|PubMed:9238088, ECO:0000269|Ref.10, FT ECO:0000269|Ref.3, ECO:0000269|Ref.5, ECO:0000269|Ref.8" FT /id="VAR_009126" FT VARIANT 132 FT /note="P -> R (in dbSNP:rs1804145)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_025500" FT CONFLICT 97..98 FT /note="EQ -> DE (in Ref. 1; AAA60058 and 10; AAB38685)" FT /evidence="ECO:0000305" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 50..72 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 82..92 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 118..129 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 136..144 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 152..162 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 173..187 FT /evidence="ECO:0007829|PDB:1IMV" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 204..214 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 227..236 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 238..256 FT /evidence="ECO:0007829|PDB:1IMV" FT TURN 257..260 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 261..268 FT /evidence="ECO:0007829|PDB:1IMV" FT TURN 269..271 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 272..281 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 287..290 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 295..304 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 306..315 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 317..324 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 326..330 FT /evidence="ECO:0007829|PDB:1IMV" FT TURN 331..335 FT /evidence="ECO:0007829|PDB:1IMV" FT HELIX 336..339 FT /evidence="ECO:0007829|PDB:1IMV" FT TURN 344..346 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 353..364 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 368..370 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 394..400 FT /evidence="ECO:0007829|PDB:1IMV" FT TURN 401..403 FT /evidence="ECO:0007829|PDB:1IMV" FT STRAND 406..413 FT /evidence="ECO:0007829|PDB:1IMV" SQ SEQUENCE 418 AA; 46312 MW; 7630DD2B4026A0D3 CRC64; MQALVLLLCI GALLGHSSCQ NPASPPEEGS PDPDSTGALV EEEDPFFKVP VNKLAAAVSN FGYDLYRVRS STSPTTNVLL SPLSVATALS ALSLGAEQRT ESIIHRALYY DLISSPDIHG TYKELLDTVT APQKNLKSAS RIVFEKKLRI KSSFVAPLEK SYGTRPRVLT GNPRLDLQEI NNWVQAQMKG KLARSTKEIP DEISILLLGV AHFKGQWVTK FDSRKTSLED FYLDEERTVR VPMMSDPKAV LRYGLDSDLS CKIAQLPLTG SMSIIFFLPL KVTQNLTLIE ESLTSEFIHD IDRELKTVQA VLTVPKLKLS YEGEVTKSLQ EMKLQSLFDS PDFSKITGKP IKLTQVEHRA GFEWNEDGAG TTPSPGLQPA HLTFPLDYHL NQPFIFVLRD TDTGALLFIG KILDPRGP //