PEDF_HUMAN
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 03-AUG-2022, entry version 214.
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};
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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; 36.
DR IntAct; P36955; 15.
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 GlyGen; P36955; 6 sites, 10 N-linked glycans (1 site), 2 O-linked glycans (5 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; P36955; -.
DR PeptideAtlas; P36955; -.
DR PRIDE; P36955; -.
DR ProteomicsDB; 55243; -.
DR Antibodypedia; 865; 686 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 CTD; 5176; -.
DR DisGeNET; 5176; -.
DR GeneCards; SERPINF1; -.
DR HGNC; HGNC:8824; SERPINF1.
DR HPA; ENSG00000132386; Tissue enhanced (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; KVPMMSD; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P36955; -.
DR TreeFam; TF317350; -.
DR PathwayCommons; P36955; -.
DR SignaLink; P36955; -.
DR SIGNOR; P36955; -.
DR BioGRID-ORCS; 5176; 10 hits in 1077 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 199 other tissues.
DR ExpressionAtlas; P36955; baseline and differential.
DR Genevisible; P36955; HS.
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:0007568; P:aging; IEA:Ensembl.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; 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; -; 1.
DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
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
