PEDF_BOVIN
ID PEDF_BOVIN Reviewed; 416 AA.
AC Q95121; Q2KIF6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Pigment epithelium-derived factor;
DE Short=PEDF;
DE AltName: Full=Serpin F1;
DE Flags: Precursor;
GN Name=SERPINF1; Synonyms=PEDF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retinal pigment epithelium;
RA Perez-Mediavilla L., Chew C., Campochiaro P., Zack D.J., Becerra S.P.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Singh V.K., Chader G.J., Rodriguez I.R.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 21-47 AND 380-399.
RC TISSUE=Eye;
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).
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.
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: Retinal pigment epithelial cells. Located in the
CC interphotoreceptor matrix (IPM) which is between the retinal pigment
CC epithelium and the neural retina.
CC -!- DOMAIN: The N-terminal (AA 42-139) exhibits neurite outgrowth-inducing
CC activity. The C-terminal exposed loop (AA 380-416) is essential for
CC serpin activity.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; U48229; AAC48856.1; -; mRNA.
DR EMBL; AF017058; AAC05732.1; -; mRNA.
DR EMBL; BC112656; AAI12657.1; -; mRNA.
DR RefSeq; NP_776565.1; NM_174140.3.
DR AlphaFoldDB; Q95121; -.
DR SMR; Q95121; -.
DR STRING; 9913.ENSBTAP00000012804; -.
DR MEROPS; I04.979; -.
DR PaxDb; Q95121; -.
DR PeptideAtlas; Q95121; -.
DR PRIDE; Q95121; -.
DR Ensembl; ENSBTAT00000012804; ENSBTAP00000012804; ENSBTAG00000009705.
DR GeneID; 281386; -.
DR KEGG; bta:281386; -.
DR CTD; 5176; -.
DR VEuPathDB; HostDB:ENSBTAG00000009705; -.
DR VGNC; VGNC:34478; SERPINF1.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158112; -.
DR HOGENOM; CLU_023330_3_1_1; -.
DR InParanoid; Q95121; -.
DR OMA; KVPMMSD; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF317350; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000009705; Expressed in liver and 104 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
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 Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7592790"
FT CHAIN 21..416
FT /note="Pigment epithelium-derived factor"
FT /id="PRO_0000032507"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36955"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36955"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 21
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="K -> R (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46229 MW; F6C76B6A4C9A4ECA CRC64;
MQALVLLLWT GALLGFGRCQ NAGQEAGSLT PESTGAPVEE EDPFFKVPVN KLAAAVSNFG
YDLYRVRSGE SPTANVLLSP LSVATALSAL SLGAEQRTES NIHRALYYDL ISNPDIHGTY
KDLLASVTAP QKNLKSASRI IFERKLRIKA SFIPPLEKSY GTRPRILTGN SRVDLQEINN
WVQAQMKGKV ARSTREMPSE ISIFLLGVAY FKGQWVTKFD SRKTSLEDFY LDEERTVKVP
MMSDPQAVLR YGLDSDLNCK IAQLPLTGST SIIFFLPQKV TQNLTLIEES LTSEFIHDID
RELKTVQAVL TIPKLKLSYE GELTKSVQEL KLQSLFDAPD FSKITGKPIK LTQVEHRVGF
EWNEDGAGTN SSPGVQPARL TFPLDYHLNQ PFIFVLRDTD TGALLFIGKI LDPRGT
