PEDF_MOUSE
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 03-AUG-2022, entry version 161.
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}.
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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 GlyGen; P97298; 1 site.
DR PhosphoSitePlus; P97298; -.
DR CPTAC; non-CPTAC-3389; -.
DR CPTAC; non-CPTAC-3390; -.
DR PaxDb; P97298; -.
DR PeptideAtlas; P97298; -.
DR PRIDE; P97298; -.
DR ProteomicsDB; 287671; -.
DR Antibodypedia; 865; 686 antibodies from 38 providers.
DR DNASU; 20317; -.
DR Ensembl; ENSMUST00000000769; ENSMUSP00000000769; ENSMUSG00000000753.
DR GeneID; 20317; -.
DR KEGG; mmu:20317; -.
DR UCSC; uc007kdp.1; mouse.
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; KVPMMSD; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P97298; -.
DR TreeFam; TF317350; -.
DR BioGRID-ORCS; 20317; 3 hits in 73 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 246 other tissues.
DR ExpressionAtlas; P97298; baseline and differential.
DR Genevisible; P97298; MM.
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: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; 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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; 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; -; 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; 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
