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Pigment epithelium-derived factor (PEDF) (Cell proliferation-inducing gene 35 protein) (EPC-1) (Serpin F1)

 PEDF_HUMAN              Reviewed;         418 AA.
P36955; F1T092; Q13236; Q2TU83; Q96CT1; Q96R01; Q9BWA4;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
18-JUL-2018, entry version 188.
RecName: Full=Pigment epithelium-derived factor;
Short=PEDF;
AltName: Full=Cell proliferation-inducing gene 35 protein;
AltName: Full=EPC-1;
AltName: Full=Serpin F1;
Flags: Precursor;
Name=SERPINF1; Synonyms=PEDF; ORFNames=PIG35;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
MET-72.
TISSUE=Fetal eye;
PubMed=8434014; DOI=10.1073/pnas.90.4.1526;
Steele F.R., Chader G.J., Johnson L.V., Tombran-Tink J.;
"Pigment epithelium-derived factor: neurotrophic activity and
identification as a member of the serine protease inhibitor gene
family.";
Proc. Natl. Acad. Sci. U.S.A. 90:1526-1530(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-72.
PubMed=9238088;
Tombran-Tink J., Mazuruk K., Rodriguez I.R., Chung D., Linker T.,
Englander E., Chader G.J.;
"Organization, evolutionary conservation, expression and unusual Alu
density of the human gene for pigment epithelium-derived factor, a
unique neurotrophic serpin.";
Mol. Vis. 2:11-11(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MET-72.
Yin B., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-72.
TISSUE=Liver cancer;
Kim J.W.;
"Identification of a human cell proliferation inducing gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=21697133; DOI=10.1167/iovs.11-7479;
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M.,
Toyama S., Usami R., Ohtoko K., Kato S.;
"Full-length transcriptome analysis of human retina-derived cell lines
ARPE-19 and Y79 using the vector-capping method.";
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-72.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-72 AND
ARG-132.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-332, AND VARIANT MET-72.
TISSUE=Fetal lung fibroblast;
Coljee V.W.;
Thesis (1996), Medical College of Pennsylvania, United States.
[11]
PROTEIN SEQUENCE OF 21-29; 253-262 AND 282-303, TISSUE SPECIFICITY,
AND PYROGLUTAMATE FORMATION AT GLN-20.
TISSUE=Plasma;
PubMed=12737624; DOI=10.1042/BJ20030313;
Petersen S.V., Valnickova Z., Enghild J.J.;
"Pigment-epithelium-derived factor (PEDF) occurs at a physiologically
relevant concentration in human blood: purification and
characterization.";
Biochem. J. 374:199-206(2003).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 60-418, AND VARIANT MET-72.
TISSUE=Fetal lung fibroblast;
PubMed=8473338;
Pignolo R.J., Cristofalo V.J., Rotenberg M.O.;
"Senescent WI-38 cells fail to express EPC-1, a gene induced in young
cells upon entry into the G0 state.";
J. Biol. Chem. 268:8949-8957(1993).
[13]
FUNCTION.
PubMed=8226833;
Becerra S.P., Palmer I., Kumar A., Steele F.R., Shiloach J.,
Notario V., Chader G.J.;
"Overexpression of fetal human pigment epithelium-derived factor in
Escherichia coli. A functionally active neurotrophic factor.";
J. Biol. Chem. 268:23148-23156(1993).
[14]
FUNCTION.
PubMed=7592790; DOI=10.1074/jbc.270.43.25992;
Becerra S.P., Sagasti A., Spinella P., Notario V.;
"Pigment epithelium-derived factor behaves like a noninhibitory
serpin. Neurotrophic activity does not require the serpin reactive
loop.";
J. Biol. Chem. 270:25992-25999(1995).
[15]
PHOSPHORYLATION AT SER-24; SER-114 AND SER-227.
PubMed=15374885; DOI=10.1182/blood-2004-04-1569;
Maik-Rachline G., Shaltiel S., Seger R.;
"Extracellular phosphorylation converts pigment epithelium-derived
factor from a neurotrophic to an antiangiogenic factor.";
Blood 105:670-678(2005).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-285.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[17]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-285.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[19]
GLYCOSYLATION AT ASN-285.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS], AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[21]
INVOLVEMENT IN OI6.
PubMed=21353196; DOI=10.1016/j.ajhg.2011.01.015;
Becker J., Semler O., Gilissen C., Li Y., Bolz H.J., Giunta C.,
Bergmann C., Rohrbach M., Koerber F., Zimmermann K., de Vries P.,
Wirth B., Schoenau E., Wollnik B., Veltman J.A., Hoischen A.,
Netzer C.;
"Exome sequencing identifies truncating mutations in human SERPINF1 in
autosomal-recessive osteogenesis imperfecta.";
Am. J. Hum. Genet. 88:362-371(2011).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[24]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 21-418, AND GLYCOSYLATION AT
ASN-285.
PubMed=11562499; DOI=10.1073/pnas.211268598;
Simonovic M., Gettins P.G.W., Volz K.;
"Crystal structure of human PEDF, a potent anti-angiogenic and neurite
growth-promoting factor.";
Proc. Natl. Acad. Sci. U.S.A. 98:11131-11135(2001).
[25]
VARIANT MET-72.
PubMed=10398730;
Koenekoop R., Pina A.L., Loyer M., Davidson J., Robitaille J.,
Maumenee I., Tombran-Tink J.;
"Four polymorphic variations in the PEDF gene identified during the
mutation screening of patients with Leber congenital amaurosis.";
Mol. Vis. 5:10-10(1999).
[26]
VARIANT MET-72, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
Lin X., Zeng R., Wu J.R.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
-!- 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.
{ECO:0000269|PubMed:7592790, ECO:0000269|PubMed:8226833}.
-!- INTERACTION:
Q7L775:EPM2AIP1; NbExp=8; IntAct=EBI-2932733, EBI-6255981;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17081065}.
Melanosome {ECO:0000269|PubMed:17081065}. Note=Enriched in stage I
melanosomes.
-!- TISSUE SPECIFICITY: Retinal pigment epithelial cells and blood
plasma. {ECO:0000269|PubMed:12737624}.
-!- DEVELOPMENTAL STAGE: Expressed in quiescent cells.
-!- DOMAIN: The N-terminal (AA 44-121) exhibits neurite outgrowth-
inducing activity. The C-terminal exposed loop (AA 382-418) is
essential for serpin activity.
-!- PTM: The N-terminus is blocked. Extracellular phosphorylation
enhances antiangiogenic activity. {ECO:0000269|PubMed:15374885}.
-!- PTM: N- and O-glycosylated. O-glycosylated with a core 1 or
possibly core 8 glycan. {ECO:0000269|PubMed:11562499,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169}.
-!- DISEASE: Osteogenesis imperfecta 6 (OI6) [MIM:613982]: A form of
osteogenesis imperfecta, a connective tissue disorder
characterized by low bone mass, bone fragility and susceptibility
to fractures after minimal trauma. Disease severity ranges from
very mild forms without fractures to intrauterine fractures and
perinatal lethality. Extraskeletal manifestations, which affect a
variable number of patients, are dentinogenesis imperfecta,
hearing loss, and blue sclerae. OI6 is a severe, autosomal
recessive form compatible with OI type III in the Sillence
classification. {ECO:0000269|PubMed:21353196}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA84914.1; Type=Frameshift; Positions=356; Evidence={ECO:0000305};
Sequence=AAA93524.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; M76979; AAA60058.1; -; mRNA.
EMBL; U29953; AAA84914.1; ALT_FRAME; Genomic_DNA.
EMBL; AF400442; AAK92491.1; -; mRNA.
EMBL; BT007222; AAP35886.1; -; mRNA.
EMBL; AY513280; AAT08033.1; -; mRNA.
EMBL; AB593011; BAJ83966.1; -; mRNA.
EMBL; AB593012; BAJ83967.1; -; mRNA.
EMBL; AB593013; BAJ83968.1; -; mRNA.
EMBL; AC130343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC130689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW90577.1; -; Genomic_DNA.
EMBL; BC000522; AAH00522.1; -; mRNA.
EMBL; BC013984; AAH13984.1; -; mRNA.
EMBL; AH004879; AAB38685.1; -; Genomic_DNA.
EMBL; M90439; AAA93524.1; ALT_INIT; mRNA.
CCDS; CCDS11012.1; -.
PIR; A46046; A46046.
PIR; A47281; A47281.
RefSeq; NP_001316832.1; NM_001329903.1.
RefSeq; NP_002606.3; NM_002615.6.
UniGene; Hs.532768; -.
PDB; 1IMV; X-ray; 2.85 A; A=21-418.
PDBsum; 1IMV; -.
ProteinModelPortal; P36955; -.
SMR; P36955; -.
BioGrid; 111202; 18.
IntAct; P36955; 8.
MINT; P36955; -.
STRING; 9606.ENSP00000254722; -.
MEROPS; I04.979; -.
GlyConnect; 645; -.
iPTMnet; P36955; -.
PhosphoSitePlus; P36955; -.
BioMuta; SERPINF1; -.
DMDM; 313104314; -.
REPRODUCTION-2DPAGE; IPI00006114; -.
EPD; P36955; -.
MaxQB; P36955; -.
PaxDb; P36955; -.
PeptideAtlas; P36955; -.
PRIDE; P36955; -.
ProteomicsDB; 55243; -.
DNASU; 5176; -.
Ensembl; ENST00000254722; ENSP00000254722; ENSG00000132386.
GeneID; 5176; -.
KEGG; hsa:5176; -.
UCSC; uc002ftl.4; human.
CTD; 5176; -.
DisGeNET; 5176; -.
EuPathDB; HostDB:ENSG00000132386.10; -.
GeneCards; SERPINF1; -.
H-InvDB; HIX0013408; -.
HGNC; HGNC:8824; SERPINF1.
HPA; HPA005825; -.
MalaCards; SERPINF1; -.
MIM; 172860; gene.
MIM; 613982; phenotype.
neXtProt; NX_P36955; -.
OpenTargets; ENSG00000132386; -.
Orphanet; 216812; Osteogenesis imperfecta type 3.
PharmGKB; PA35508; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00920000149046; -.
HOGENOM; HOG000115489; -.
HOVERGEN; HBG106911; -.
InParanoid; P36955; -.
KO; K19614; -.
OMA; LNCKIAQ; -.
OrthoDB; EOG091G09UU; -.
PhylomeDB; P36955; -.
TreeFam; TF317350; -.
SIGNOR; P36955; -.
ChiTaRS; SERPINF1; human.
EvolutionaryTrace; P36955; -.
GeneWiki; PEDF; -.
GenomeRNAi; 5176; -.
PRO; PR:P36955; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000132386; -.
CleanEx; HS_SERPINF1; -.
ExpressionAtlas; P36955; baseline and differential.
Genevisible; P36955; HS.
GO; GO:0043203; C:axon hillock; IEA:Ensembl.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0071279; P:cellular response to cobalt ion; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
GO; GO:0050769; P:positive regulation of neurogenesis; IDA:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0007614; P:short-term memory; IEA:Ensembl.
CDD; cd02052; PEDF; 1.
InterPro; IPR033832; PEDF.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Dwarfism;
Glycoprotein; Osteogenesis imperfecta; Phosphoprotein; Polymorphism;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
SIGNAL 1 19
CHAIN 20 418 Pigment epithelium-derived factor.
/FTId=PRO_0000032508.
REGION 371 383 O-glycosylated at one site.
MOD_RES 20 20 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:12737624}.
MOD_RES 24 24 Phosphoserine; by CK2.
{ECO:0000269|PubMed:15374885}.
MOD_RES 114 114 Phosphoserine; by CK2.
{ECO:0000269|PubMed:15374885}.
MOD_RES 227 227 Phosphoserine; by PKA.
{ECO:0000269|PubMed:15374885}.
CARBOHYD 285 285 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:11562499,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
VARIANT 72 72 T -> M (polymorphism; confirmed at
protein level; dbSNP:rs1136287).
{ECO:0000269|PubMed:10398730,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:8434014,
ECO:0000269|PubMed:8473338,
ECO:0000269|PubMed:9238088,
ECO:0000269|Ref.10, ECO:0000269|Ref.3,
ECO:0000269|Ref.5, ECO:0000269|Ref.8}.
/FTId=VAR_009126.
VARIANT 132 132 P -> R (in dbSNP:rs1804145).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025500.
CONFLICT 97 98 EQ -> DE (in Ref. 1; AAA60058 and 10;
AAB38685). {ECO:0000305}.
HELIX 45 48 {ECO:0000244|PDB:1IMV}.
HELIX 50 72 {ECO:0000244|PDB:1IMV}.
STRAND 78 80 {ECO:0000244|PDB:1IMV}.
HELIX 82 92 {ECO:0000244|PDB:1IMV}.
HELIX 93 95 {ECO:0000244|PDB:1IMV}.
HELIX 98 107 {ECO:0000244|PDB:1IMV}.
HELIX 110 112 {ECO:0000244|PDB:1IMV}.
HELIX 118 129 {ECO:0000244|PDB:1IMV}.
STRAND 136 144 {ECO:0000244|PDB:1IMV}.
HELIX 152 162 {ECO:0000244|PDB:1IMV}.
HELIX 173 187 {ECO:0000244|PDB:1IMV}.
TURN 188 190 {ECO:0000244|PDB:1IMV}.
STRAND 204 214 {ECO:0000244|PDB:1IMV}.
STRAND 217 219 {ECO:0000244|PDB:1IMV}.
HELIX 223 225 {ECO:0000244|PDB:1IMV}.
STRAND 227 236 {ECO:0000244|PDB:1IMV}.
STRAND 238 256 {ECO:0000244|PDB:1IMV}.
TURN 257 260 {ECO:0000244|PDB:1IMV}.
STRAND 261 268 {ECO:0000244|PDB:1IMV}.
TURN 269 271 {ECO:0000244|PDB:1IMV}.
STRAND 272 281 {ECO:0000244|PDB:1IMV}.
HELIX 287 290 {ECO:0000244|PDB:1IMV}.
HELIX 295 304 {ECO:0000244|PDB:1IMV}.
STRAND 306 315 {ECO:0000244|PDB:1IMV}.
STRAND 317 324 {ECO:0000244|PDB:1IMV}.
HELIX 326 330 {ECO:0000244|PDB:1IMV}.
TURN 331 335 {ECO:0000244|PDB:1IMV}.
HELIX 336 339 {ECO:0000244|PDB:1IMV}.
TURN 344 346 {ECO:0000244|PDB:1IMV}.
STRAND 353 364 {ECO:0000244|PDB:1IMV}.
STRAND 368 370 {ECO:0000244|PDB:1IMV}.
STRAND 387 389 {ECO:0000244|PDB:1IMV}.
STRAND 394 400 {ECO:0000244|PDB:1IMV}.
TURN 401 403 {ECO:0000244|PDB:1IMV}.
STRAND 406 413 {ECO:0000244|PDB:1IMV}.
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


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