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P97298 (PEDF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pigment epithelium-derived factor

Short name=PEDF
Alternative name(s):
Caspin
Serpin F1
Stromal cell-derived factor 3
Short name=SDF-3
Gene names
Name:Serpinf1
Synonyms:Pedf, Sdf3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. Ref.6

Subcellular location

Secreted. Melanosome By similarity.

Tissue specificity

Highly expressed in the liver, gastric glandular mucosa and renal tubules. It is also expressed in the brain, heart, lung retina and testes. Ref.2 Ref.3

Developmental stage

First detected at 12.5 dpc in cartilage primordium, it is present in the osseous matrix of developing limbs, vertebrae, ribs and skull. At 16.5 dpc it is detected in bone matrix and smooth muscle, and at lower levels in connective tissue, bronchial epithelial cells, metanephron microtubules, and skin. Ref.2

Sequence similarities

Belongs to the serpin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   PTMGlycoprotein
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

negative regulation of angiogenesis

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of epithelial cell proliferation involved in prostate gland development

Inferred from mutant phenotype PubMed 12740569. Source: MGI

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

short-term memory

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular matrix

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay Ref.2. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 15020256. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 417398Pigment epithelium-derived factor
PRO_0000032509

Amino acid modifications

Modified residue201Pyrrolidone carboxylic acid By similarity
Modified residue241Phosphoserine By similarity
Glycosylation2841N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict701S → G in AAC69271. Ref.4
Sequence conflict1361K → N in BAA31978. Ref.2
Sequence conflict1371S → R in AAC69271. Ref.4
Sequence conflict2801T → A in BAA09051. Ref.1
Sequence conflict3771Q → L in AAC69271. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P97298 [UniParc].

Last modified March 29, 2004. Version 2.
Checksum: ECD360FE6AA74D25

FASTA41746,234
        10         20         30         40         50         60 
MQALVLLLWT GALLGHGSSQ NVPSSSEGSP VPDSTGEPVE EEDPFFKVPV NKLAAAVSNF 

        70         80         90        100        110        120 
GYDLYRLRSS ASPTGNVLLS PLSVATALSA LSLGAEHRTE SVIHRALYYD LITNPDIHST 

       130        140        150        160        170        180 
YKELLASVTA PEKNLKSASR IVFERKLRVK SSFVAPLEKS YGTRPRILTG NPRVDLQEIN 

       190        200        210        220        230        240 
NWVQAQMKGK IARSTREMPS ALSILLLGVA YFKGQWVTKF DSRKTTLQDF HLDEDRTVRV 

       250        260        270        280        290        300 
PMMSDPKAIL RYGLDSDLNC KIAQLPLTGS MSIIFFLPLT VTQNLTMIEE SLTSEFIHDI 

       310        320        330        340        350        360 
DRELKTIQAV LTVPKLKLSF EGELTKSLQD MKLQSLFESP DFSKITGKPV KLTQVEHRAA 

       370        380        390        400        410 
FEWNEEGAGS SPSPGLQPVR LTFPLDYHLN QPFLFVLRDT DTGALLFIGR ILDPSST 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of novel secreted and membrane proteins isolated by the signal sequence trap method."
Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M., Hamada T., Sato T., Nakano T., Honjo T.
Genomics 37:273-280(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation, purification and characterization of a collagen-associated serpin, caspin, produced by murine colon adenocarcinoma cells."
Kozaki K., Miyaishi O., Koiwai O., Yasui Y., Kashiwai A., Nishikawa Y., Shimizu S., Saga S.
J. Biol. Chem. 273:15125-15130(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-66; 252-261; 333-344 AND 359-372, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: BALB/c.
Tissue: Liver.
[3]"Structural and comparative analysis of the mouse gene for pigment epithelium-derived factor (PEDF)."
Singh V.K., Chader G.J., Rodriguez I.R.
Mol. Vis. 4:7-7(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: FVB/N.
Tissue: Liver.
[4]Tombran-Tink J.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BALB/c.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[6]"Wilms' tumor growth is suppressed by antiangiogenic pigment epithelium-derived factor in a xenograft model."
Abramson L.P., Stellmach V., Doll J.A., Cornwell M., Arensman R.M., Crawford S.E.
J. Pediatr. Surg. 38:336-342(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50460 mRNA. Translation: BAA09051.1.
AF036164 mRNA. Translation: AAC69271.1.
D87975 mRNA. Translation: BAA31978.1.
AF017055 expand/collapse EMBL AC list , AF017051, AF017052, AF017053, AF017054 Genomic DNA. Translation: AAC05733.1.
AF017057 mRNA. Translation: AAC05731.1.
BC019852 mRNA. Translation: AAH19852.1.
CCDSCCDS25045.1.
RefSeqNP_035470.3. NM_011340.3.
UniGeneMm.2044.

3D structure databases

ProteinModelPortalP97298.
SMRP97298. Positions 35-414.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI04.979.

PTM databases

PhosphoSiteP97298.

Proteomic databases

MaxQBP97298.
PaxDbP97298.
PRIDEP97298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000769; ENSMUSP00000000769; ENSMUSG00000000753.
GeneID20317.
KEGGmmu:20317.
UCSCuc007kdp.1. mouse.

Organism-specific databases

CTD5176.
MGIMGI:108080. Serpinf1.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00750000117478.
HOGENOMHOG000115489.
HOVERGENHBG106911.
InParanoidP97298.
OMALNCKIAQ.
OrthoDBEOG7K3TMD.
PhylomeDBP97298.
TreeFamTF317350.

Gene expression databases

ArrayExpressP97298.
BgeeP97298.
GenevestigatorP97298.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSERPINF1. mouse.
NextBio298103.
PROP97298.
SOURCESearch...

Entry information

Entry namePEDF_MOUSE
AccessionPrimary (citable) accession number: P97298
Secondary accession number(s): O70629, O88691
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 29, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot