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 09-DEC-2015, entry version 165. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT RP 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 RT 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 RT unique 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 RT 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., RA Toyama S., 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., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA 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 RT the 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RP 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 RT project: 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, RP AND 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 RT 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; 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 RT cells upon entry into the G0 state."; RL J. Biol. Chem. 268:8949-8957(1993). RN [13] RP FUNCTION. RX PubMed=8226833; RA Becerra S.P., Palmer I., Kumar A., Steele F.R., Shiloach J., RA Notario V., 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 RT serpin. Neurotrophic activity does not require the serpin reactive RT 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 RT factor 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., RA Moore R.J., 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 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., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA 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 [18] 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] 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., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [20] 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., RA Brinkmalm G., Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [21] 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., RA Wirth B., Schoenau E., Wollnik B., Veltman J.A., Hoischen A., RA 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 [22] 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., RA Buerckstuemmer T., 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 [23] 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., RA Fischer-Posovszky P., Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion RT profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [24] 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 [25] RP VARIANT MET-72. RX PubMed=10398730; RA Koenekoop R., Pina A.L., Loyer M., Davidson J., Robitaille J., RA Maumenee I., 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 [26] 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., RA Lin X., 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 CC (relaxed) conformational transition characteristic of active CC serpins, it exhibits no serine protease inhibitory activity. CC {ECO:0000269|PubMed:7592790, ECO:0000269|PubMed:8226833}. CC -!- INTERACTION: CC Q7L775:EPM2AIP1; NbExp=3; IntAct=EBI-2932733, EBI-6255981; 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 CC plasma. {ECO:0000269|PubMed:12737624}. CC -!- DEVELOPMENTAL STAGE: Expressed in quiescent cells. CC -!- DOMAIN: The N-terminal (AA 44-121) exhibits neurite outgrowth- CC inducing activity. The C-terminal exposed loop (AA 382-418) is CC essential for serpin activity. CC -!- PTM: The N-terminus is blocked. Extracellular phosphorylation CC enhances antiangiogenic activity. {ECO:0000269|PubMed:15374885}. CC -!- PTM: N- and O-glycosylated. O-glycosylated with a core 1 or CC possibly 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 CC characterized by low bone mass, bone fragility and susceptibility CC to fractures after minimal trauma. Disease severity ranges from CC very mild forms without fractures to intrauterine fractures and CC perinatal lethality. Extraskeletal manifestations, which affect a CC variable number of patients, are dentinogenesis imperfecta, CC hearing loss, and blue sclerae. OI6 is a severe, autosomal CC recessive form compatible with OI type III in the Sillence CC classification. {ECO:0000269|PubMed:21353196}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA84914.1; Type=Frameshift; Positions=356; Evidence={ECO:0000305}; CC Sequence=AAA93524.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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_002606.3; NM_002615.5. DR UniGene; Hs.532768; -. DR PDB; 1IMV; X-ray; 2.85 A; A=21-418. DR PDBsum; 1IMV; -. DR ProteinModelPortal; P36955; -. DR SMR; P36955; 36-418. DR BioGrid; 111202; 12. DR IntAct; P36955; 7. DR MINT; MINT-7711036; -. DR STRING; 9606.ENSP00000254722; -. DR MEROPS; I04.979; -. DR PhosphoSite; P36955; -. DR BioMuta; SERPINF1; -. DR DMDM; 313104314; -. DR REPRODUCTION-2DPAGE; IPI00006114; -. DR MaxQB; P36955; -. DR PaxDb; P36955; -. DR PeptideAtlas; P36955; -. DR PRIDE; P36955; -. DR DNASU; 5176; -. DR Ensembl; ENST00000254722; ENSP00000254722; ENSG00000132386. DR GeneID; 5176; -. DR KEGG; hsa:5176; -. DR UCSC; uc002ftl.3; human. DR CTD; 5176; -. DR GeneCards; SERPINF1; -. DR H-InvDB; HIX0013408; -. DR HGNC; HGNC:8824; SERPINF1. DR HPA; CAB004785; -. DR HPA; HPA005825; -. DR MalaCards; SERPINF1; -. DR MIM; 172860; gene. DR MIM; 613982; phenotype. DR neXtProt; NX_P36955; -. DR Orphanet; 216812; Osteogenesis imperfecta type 3. DR PharmGKB; PA35508; -. DR eggNOG; KOG2392; Eukaryota. DR eggNOG; COG4826; LUCA. DR GeneTree; ENSGT00760000118839; -. DR HOGENOM; HOG000115489; -. DR HOVERGEN; HBG106911; -. DR InParanoid; P36955; -. DR KO; K19614; -. DR OMA; LNCKIAQ; -. DR OrthoDB; EOG7K3TMD; -. DR PhylomeDB; P36955; -. DR TreeFam; TF317350; -. DR ChiTaRS; SERPINF1; human. DR EvolutionaryTrace; P36955; -. DR GeneWiki; PEDF; -. DR GenomeRNAi; 5176; -. DR NextBio; 20036; -. DR PRO; PR:P36955; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; P36955; -. DR CleanEx; HS_SERPINF1; -. 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:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA: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; TAS:ProtInc. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc. 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:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc. 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:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR GO; GO:0007614; P:short-term memory; IEA:Ensembl. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. 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; Complete proteome; Direct protein sequencing; Dwarfism; KW Glycoprotein; Osteogenesis imperfecta; Phosphoprotein; Polymorphism; KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal. FT SIGNAL 1 19 FT CHAIN 20 418 Pigment epithelium-derived factor. FT /FTId=PRO_0000032508. FT REGION 371 383 O-glycosylated at one site. FT MOD_RES 20 20 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:12737624}. FT MOD_RES 24 24 Phosphoserine; by CK2. FT {ECO:0000269|PubMed:15374885}. FT MOD_RES 114 114 Phosphoserine; by CK2. FT {ECO:0000269|PubMed:15374885}. FT MOD_RES 227 227 Phosphoserine; by PKA. FT {ECO:0000269|PubMed:15374885}. FT CARBOHYD 285 285 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:11562499, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218}. FT VARIANT 72 72 T -> M (polymorphism; confirmed at FT protein level; dbSNP:rs1136287). FT {ECO:0000269|PubMed:10398730, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:22028381, FT ECO:0000269|PubMed:8434014, FT ECO:0000269|PubMed:8473338, FT ECO:0000269|PubMed:9238088, FT ECO:0000269|Ref.10, ECO:0000269|Ref.3, FT ECO:0000269|Ref.5, ECO:0000269|Ref.8}. FT /FTId=VAR_009126. FT VARIANT 132 132 P -> R (in dbSNP:rs1804145). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_025500. FT CONFLICT 97 98 EQ -> DE (in Ref. 1; AAA60058 and 10; FT AAB38685). {ECO:0000305}. FT HELIX 45 48 {ECO:0000244|PDB:1IMV}. FT HELIX 50 72 {ECO:0000244|PDB:1IMV}. FT STRAND 78 80 {ECO:0000244|PDB:1IMV}. FT HELIX 82 92 {ECO:0000244|PDB:1IMV}. FT HELIX 93 95 {ECO:0000244|PDB:1IMV}. FT HELIX 98 107 {ECO:0000244|PDB:1IMV}. FT HELIX 110 112 {ECO:0000244|PDB:1IMV}. FT HELIX 118 129 {ECO:0000244|PDB:1IMV}. FT STRAND 136 144 {ECO:0000244|PDB:1IMV}. FT HELIX 152 162 {ECO:0000244|PDB:1IMV}. FT HELIX 173 187 {ECO:0000244|PDB:1IMV}. FT TURN 188 190 {ECO:0000244|PDB:1IMV}. FT STRAND 204 214 {ECO:0000244|PDB:1IMV}. FT STRAND 217 219 {ECO:0000244|PDB:1IMV}. FT HELIX 223 225 {ECO:0000244|PDB:1IMV}. FT STRAND 227 236 {ECO:0000244|PDB:1IMV}. FT STRAND 238 256 {ECO:0000244|PDB:1IMV}. FT TURN 257 260 {ECO:0000244|PDB:1IMV}. FT STRAND 261 268 {ECO:0000244|PDB:1IMV}. FT TURN 269 271 {ECO:0000244|PDB:1IMV}. FT STRAND 272 281 {ECO:0000244|PDB:1IMV}. FT HELIX 287 290 {ECO:0000244|PDB:1IMV}. FT HELIX 295 304 {ECO:0000244|PDB:1IMV}. FT STRAND 306 315 {ECO:0000244|PDB:1IMV}. FT STRAND 317 324 {ECO:0000244|PDB:1IMV}. FT HELIX 326 330 {ECO:0000244|PDB:1IMV}. FT TURN 331 335 {ECO:0000244|PDB:1IMV}. FT HELIX 336 339 {ECO:0000244|PDB:1IMV}. FT TURN 344 346 {ECO:0000244|PDB:1IMV}. FT STRAND 353 364 {ECO:0000244|PDB:1IMV}. FT STRAND 368 370 {ECO:0000244|PDB:1IMV}. FT STRAND 387 389 {ECO:0000244|PDB:1IMV}. FT STRAND 394 400 {ECO:0000244|PDB:1IMV}. FT TURN 401 403 {ECO:0000244|PDB:1IMV}. FT STRAND 406 413 {ECO:0000244|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 //