Full text data of NPTN
NPTN
(SDFR1, SDR1)
[Confidence: high (present in two of the MS resources)]
Neuroplastin (Stromal cell-derived receptor 1; SDR-1; Flags: Precursor)
Neuroplastin (Stromal cell-derived receptor 1; SDR-1; Flags: Precursor)
hRBCD
IPI00011578
IPI00011578 Stromal cell-derived receptor-1 alpha Stromal cell-derived receptor-1 alpha membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a extracellular n/a found at its expected molecular weight found at molecular weight
IPI00011578 Stromal cell-derived receptor-1 alpha Stromal cell-derived receptor-1 alpha membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a extracellular n/a found at its expected molecular weight found at molecular weight
Comments
Isoform Q9Y639-1 was detected.
Isoform Q9Y639-1 was detected.
UniProt
Q9Y639
ID NPTN_HUMAN Reviewed; 398 AA.
AC Q9Y639; B2RAL7; B7Z4D3; B7ZLL2; Q17R52; Q59EJ9; Q6NVX7; Q9Y640;
read moreDT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Neuroplastin;
DE AltName: Full=Stromal cell-derived receptor 1;
DE Short=SDR-1;
DE Flags: Precursor;
GN Name=NPTN; Synonyms=SDFR1, SDR1;
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] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP SPECIFICITY.
RA Lopez N.D., Kinoshita A., Taniwaki M., Tada H., Shirozu M., Nakano T.,
RA Tashiro K., Honjo T.;
RT "Isoform specific expression of the SDR-1 protein, alpha and beta in
RT subregions of adult rodent brain.";
RL Biomed. Res. 20:43-49(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain, and Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 29-43 (ISOFORM 1).
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17196182; DOI=10.1016/j.brainres.2006.11.090;
RA Bernstein H.G., Smalla K.H., Bogerts B., Gordon-Weeks P.R.,
RA Beesley P.W., Gundelfinger E.D., Kreutz M.R.;
RT "The immunolocalization of the synaptic glycoprotein neuroplastin
RT differs substantially between the human and the rodent brain.";
RL Brain Res. 1134:107-112(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-284 AND ASN-296, AND MASS
RP SPECTROMETRY.
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-229, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
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).
CC -!- FUNCTION: Probable homophilic and heterophilic cell adhesion
CC molecule involved in long term potentiation at hippocampal
CC excitatory synapses through activation of p38MAPK. May also
CC regulate neurite outgrowth by activating the FGFR1 signaling
CC pathway. May play a role in synaptic plasticity (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential). Note=Enriched at postsynaptic density (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2; Synonyms=SDR-1-beta;
CC IsoId=Q9Y639-2; Sequence=Displayed;
CC Name=1; Synonyms=SDR-1-alpha;
CC IsoId=Q9Y639-1; Sequence=VSP_039251;
CC Name=3;
CC IsoId=Q9Y639-3; Sequence=VSP_039251, VSP_039253;
CC Name=4;
CC IsoId=Q9Y639-4; Sequence=VSP_039252;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9Y639-5; Sequence=VSP_039253;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2
CC is expressed in brain cortex and cerebellum (at protein level).
CC -!- DOMAIN: Some isoforms lack the first Ig-like domain which may
CC confer homophilic adhesion activity. However, they can bind and
CC activate FGFR1 (By similarity).
CC -!- SIMILARITY: Contains 3 Ig-like (immunoglobulin-like) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93049.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF109126; AAD43217.1; -; mRNA.
DR EMBL; AF109127; AAD43218.1; -; mRNA.
DR EMBL; AK297184; BAH12519.1; -; mRNA.
DR EMBL; AK314248; BAG36914.1; -; mRNA.
DR EMBL; AB209812; BAD93049.1; ALT_INIT; mRNA.
DR EMBL; CH471082; EAW77931.1; -; Genomic_DNA.
DR EMBL; BC105979; AAI05980.1; -; mRNA.
DR EMBL; BC117462; AAI17463.1; -; mRNA.
DR EMBL; BC143880; AAI43881.1; -; mRNA.
DR EMBL; BC143881; AAI43882.1; -; mRNA.
DR PIR; T17219; T17219.
DR RefSeq; NP_001154835.1; NM_001161363.1.
DR RefSeq; NP_001154836.1; NM_001161364.1.
DR RefSeq; NP_036560.1; NM_012428.3.
DR RefSeq; NP_059429.1; NM_017455.3.
DR UniGene; Hs.744867; -.
DR ProteinModelPortal; Q9Y639; -.
DR SMR; Q9Y639; 31-335.
DR IntAct; Q9Y639; 2.
DR MINT; MINT-4542281; -.
DR STRING; 9606.ENSP00000290401; -.
DR PhosphoSite; Q9Y639; -.
DR DMDM; 298286871; -.
DR PaxDb; Q9Y639; -.
DR PRIDE; Q9Y639; -.
DR DNASU; 27020; -.
DR Ensembl; ENST00000345330; ENSP00000290401; ENSG00000156642.
DR Ensembl; ENST00000351217; ENSP00000342958; ENSG00000156642.
DR Ensembl; ENST00000562924; ENSP00000456349; ENSG00000156642.
DR Ensembl; ENST00000563691; ENSP00000457028; ENSG00000156642.
DR GeneID; 27020; -.
DR KEGG; hsa:27020; -.
DR UCSC; uc002avs.3; human.
DR CTD; 27020; -.
DR GeneCards; GC15M073852; -.
DR HGNC; HGNC:17867; NPTN.
DR HPA; HPA051497; -.
DR MIM; 612820; gene.
DR neXtProt; NX_Q9Y639; -.
DR PharmGKB; PA134927704; -.
DR eggNOG; NOG149118; -.
DR HOVERGEN; HBG008120; -.
DR OMA; AITWIRA; -.
DR OrthoDB; EOG7V1FQN; -.
DR ChiTaRS; NPTN; human.
DR GeneWiki; NPTN; -.
DR GenomeRNAi; 27020; -.
DR NextBio; 49544; -.
DR PRO; PR:Q9Y639; -.
DR ArrayExpress; Q9Y639; -.
DR Bgee; Q9Y639; -.
DR CleanEx; HS_NPTN; -.
DR Genevestigator; Q9Y639; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; ISS:HGNC.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:HGNC.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; ISS:HGNC.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISS:HGNC.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR027112; Neuroplastin.
DR PANTHER; PTHR10075:SF5; PTHR10075:SF5; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 2.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 28
FT CHAIN 29 398 Neuroplastin.
FT /FTId=PRO_0000394470.
FT TOPO_DOM 29 339 Extracellular (Potential).
FT TRANSMEM 340 360 Helical; (Potential).
FT TOPO_DOM 361 398 Cytoplasmic (Potential).
FT DOMAIN 29 134 Ig-like 1.
FT DOMAIN 148 235 Ig-like 2.
FT DOMAIN 238 329 Ig-like 3.
FT REGION 149 161 Narpin; mediates binding with FGFR1 and
FT has antidepressant-like activity (By
FT similarity).
FT CARBOHYD 171 171 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 229 229 N-linked (GlcNAc...).
FT CARBOHYD 284 284 N-linked (GlcNAc...).
FT CARBOHYD 296 296 N-linked (GlcNAc...).
FT CARBOHYD 317 317 N-linked (GlcNAc...) (Potential).
FT DISULFID 52 116 By similarity.
FT DISULFID 170 218 By similarity.
FT DISULFID 259 316 By similarity.
FT VAR_SEQ 31 147 AGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNR
FT AESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSG
FT TYECRASNDPKRNDLRQNPSITWIRAQATISVLQK -> E
FT (in isoform 1 and isoform 3).
FT /FTId=VSP_039251.
FT VAR_SEQ 320 398 NAIGSASVVTVLRVRSHLAPLWPFLGILAEIIILVVIIVVY
FT EKRKRPDEVPDDDEPAGPMKTNSTNNHKDKNLRQRNTN ->
FT WPHSGLSWEFWLKLSSLW (in isoform 4).
FT /FTId=VSP_039252.
FT VAR_SEQ 372 375 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_039253.
FT CONFLICT 299 299 E -> K (in Ref. 2; BAH12519).
SQ SEQUENCE 398 AA; 44387 MW; 5109E3C03B4967EA CRC64;
MSGSSLPSAL ALSLLLVSGS LLPGPGAAQN AGFVKSPMSE TKLTGDAFEL YCDVVGSPTP
EIQWWYAEVN RAESFRQLWD GARKRRVTVN TAYGSNGVSV LRITRLTLED SGTYECRASN
DPKRNDLRQN PSITWIRAQA TISVLQKPRI VTSEEVIIRD SPVLPVTLQC NLTSSSHTLT
YSYWTKNGVE LSATRKNASN MEYRINKPRA EDSGEYHCVY HFVSAPKANA TIEVKAAPDI
TGHKRSENKN EGQDATMYCK SVGYPHPDWI WRKKENGMPM DIVNTSGRFF IINKENYTEL
NIVNLQITED PGEYECNATN AIGSASVVTV LRVRSHLAPL WPFLGILAEI IILVVIIVVY
EKRKRPDEVP DDDEPAGPMK TNSTNNHKDK NLRQRNTN
//
ID NPTN_HUMAN Reviewed; 398 AA.
AC Q9Y639; B2RAL7; B7Z4D3; B7ZLL2; Q17R52; Q59EJ9; Q6NVX7; Q9Y640;
read moreDT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Neuroplastin;
DE AltName: Full=Stromal cell-derived receptor 1;
DE Short=SDR-1;
DE Flags: Precursor;
GN Name=NPTN; Synonyms=SDFR1, SDR1;
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] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP SPECIFICITY.
RA Lopez N.D., Kinoshita A., Taniwaki M., Tada H., Shirozu M., Nakano T.,
RA Tashiro K., Honjo T.;
RT "Isoform specific expression of the SDR-1 protein, alpha and beta in
RT subregions of adult rodent brain.";
RL Biomed. Res. 20:43-49(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain, and Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 29-43 (ISOFORM 1).
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17196182; DOI=10.1016/j.brainres.2006.11.090;
RA Bernstein H.G., Smalla K.H., Bogerts B., Gordon-Weeks P.R.,
RA Beesley P.W., Gundelfinger E.D., Kreutz M.R.;
RT "The immunolocalization of the synaptic glycoprotein neuroplastin
RT differs substantially between the human and the rodent brain.";
RL Brain Res. 1134:107-112(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-284 AND ASN-296, AND MASS
RP SPECTROMETRY.
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-229, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
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).
CC -!- FUNCTION: Probable homophilic and heterophilic cell adhesion
CC molecule involved in long term potentiation at hippocampal
CC excitatory synapses through activation of p38MAPK. May also
CC regulate neurite outgrowth by activating the FGFR1 signaling
CC pathway. May play a role in synaptic plasticity (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential). Note=Enriched at postsynaptic density (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2; Synonyms=SDR-1-beta;
CC IsoId=Q9Y639-2; Sequence=Displayed;
CC Name=1; Synonyms=SDR-1-alpha;
CC IsoId=Q9Y639-1; Sequence=VSP_039251;
CC Name=3;
CC IsoId=Q9Y639-3; Sequence=VSP_039251, VSP_039253;
CC Name=4;
CC IsoId=Q9Y639-4; Sequence=VSP_039252;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9Y639-5; Sequence=VSP_039253;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2
CC is expressed in brain cortex and cerebellum (at protein level).
CC -!- DOMAIN: Some isoforms lack the first Ig-like domain which may
CC confer homophilic adhesion activity. However, they can bind and
CC activate FGFR1 (By similarity).
CC -!- SIMILARITY: Contains 3 Ig-like (immunoglobulin-like) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93049.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF109126; AAD43217.1; -; mRNA.
DR EMBL; AF109127; AAD43218.1; -; mRNA.
DR EMBL; AK297184; BAH12519.1; -; mRNA.
DR EMBL; AK314248; BAG36914.1; -; mRNA.
DR EMBL; AB209812; BAD93049.1; ALT_INIT; mRNA.
DR EMBL; CH471082; EAW77931.1; -; Genomic_DNA.
DR EMBL; BC105979; AAI05980.1; -; mRNA.
DR EMBL; BC117462; AAI17463.1; -; mRNA.
DR EMBL; BC143880; AAI43881.1; -; mRNA.
DR EMBL; BC143881; AAI43882.1; -; mRNA.
DR PIR; T17219; T17219.
DR RefSeq; NP_001154835.1; NM_001161363.1.
DR RefSeq; NP_001154836.1; NM_001161364.1.
DR RefSeq; NP_036560.1; NM_012428.3.
DR RefSeq; NP_059429.1; NM_017455.3.
DR UniGene; Hs.744867; -.
DR ProteinModelPortal; Q9Y639; -.
DR SMR; Q9Y639; 31-335.
DR IntAct; Q9Y639; 2.
DR MINT; MINT-4542281; -.
DR STRING; 9606.ENSP00000290401; -.
DR PhosphoSite; Q9Y639; -.
DR DMDM; 298286871; -.
DR PaxDb; Q9Y639; -.
DR PRIDE; Q9Y639; -.
DR DNASU; 27020; -.
DR Ensembl; ENST00000345330; ENSP00000290401; ENSG00000156642.
DR Ensembl; ENST00000351217; ENSP00000342958; ENSG00000156642.
DR Ensembl; ENST00000562924; ENSP00000456349; ENSG00000156642.
DR Ensembl; ENST00000563691; ENSP00000457028; ENSG00000156642.
DR GeneID; 27020; -.
DR KEGG; hsa:27020; -.
DR UCSC; uc002avs.3; human.
DR CTD; 27020; -.
DR GeneCards; GC15M073852; -.
DR HGNC; HGNC:17867; NPTN.
DR HPA; HPA051497; -.
DR MIM; 612820; gene.
DR neXtProt; NX_Q9Y639; -.
DR PharmGKB; PA134927704; -.
DR eggNOG; NOG149118; -.
DR HOVERGEN; HBG008120; -.
DR OMA; AITWIRA; -.
DR OrthoDB; EOG7V1FQN; -.
DR ChiTaRS; NPTN; human.
DR GeneWiki; NPTN; -.
DR GenomeRNAi; 27020; -.
DR NextBio; 49544; -.
DR PRO; PR:Q9Y639; -.
DR ArrayExpress; Q9Y639; -.
DR Bgee; Q9Y639; -.
DR CleanEx; HS_NPTN; -.
DR Genevestigator; Q9Y639; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; ISS:HGNC.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:HGNC.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; ISS:HGNC.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISS:HGNC.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR027112; Neuroplastin.
DR PANTHER; PTHR10075:SF5; PTHR10075:SF5; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 2.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 28
FT CHAIN 29 398 Neuroplastin.
FT /FTId=PRO_0000394470.
FT TOPO_DOM 29 339 Extracellular (Potential).
FT TRANSMEM 340 360 Helical; (Potential).
FT TOPO_DOM 361 398 Cytoplasmic (Potential).
FT DOMAIN 29 134 Ig-like 1.
FT DOMAIN 148 235 Ig-like 2.
FT DOMAIN 238 329 Ig-like 3.
FT REGION 149 161 Narpin; mediates binding with FGFR1 and
FT has antidepressant-like activity (By
FT similarity).
FT CARBOHYD 171 171 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 229 229 N-linked (GlcNAc...).
FT CARBOHYD 284 284 N-linked (GlcNAc...).
FT CARBOHYD 296 296 N-linked (GlcNAc...).
FT CARBOHYD 317 317 N-linked (GlcNAc...) (Potential).
FT DISULFID 52 116 By similarity.
FT DISULFID 170 218 By similarity.
FT DISULFID 259 316 By similarity.
FT VAR_SEQ 31 147 AGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNR
FT AESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSG
FT TYECRASNDPKRNDLRQNPSITWIRAQATISVLQK -> E
FT (in isoform 1 and isoform 3).
FT /FTId=VSP_039251.
FT VAR_SEQ 320 398 NAIGSASVVTVLRVRSHLAPLWPFLGILAEIIILVVIIVVY
FT EKRKRPDEVPDDDEPAGPMKTNSTNNHKDKNLRQRNTN ->
FT WPHSGLSWEFWLKLSSLW (in isoform 4).
FT /FTId=VSP_039252.
FT VAR_SEQ 372 375 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_039253.
FT CONFLICT 299 299 E -> K (in Ref. 2; BAH12519).
SQ SEQUENCE 398 AA; 44387 MW; 5109E3C03B4967EA CRC64;
MSGSSLPSAL ALSLLLVSGS LLPGPGAAQN AGFVKSPMSE TKLTGDAFEL YCDVVGSPTP
EIQWWYAEVN RAESFRQLWD GARKRRVTVN TAYGSNGVSV LRITRLTLED SGTYECRASN
DPKRNDLRQN PSITWIRAQA TISVLQKPRI VTSEEVIIRD SPVLPVTLQC NLTSSSHTLT
YSYWTKNGVE LSATRKNASN MEYRINKPRA EDSGEYHCVY HFVSAPKANA TIEVKAAPDI
TGHKRSENKN EGQDATMYCK SVGYPHPDWI WRKKENGMPM DIVNTSGRFF IINKENYTEL
NIVNLQITED PGEYECNATN AIGSASVVTV LRVRSHLAPL WPFLGILAEI IILVVIIVVY
EKRKRPDEVP DDDEPAGPMK TNSTNNHKDK NLRQRNTN
//
MIM
612820
*RECORD*
*FIELD* NO
612820
*FIELD* TI
*612820 NEUROPLASTIN; NPTN
;;STROMAL CELL-DERIVED FACTOR RECEPTOR 1; SDFR1
GLYCOPROTEIN, 55-KD, INCLUDED; GP55, INCLUDED;;
read moreNEUROPLASTIN 55, INCLUDED; NP55, INCLUDED;;
GLYCOPROTEIN, 65-KD, INCLUDED; GP65, INCLUDED;;
NEUROPLASTIN 65, INCLUDED; NP65, INCLUDED
*FIELD* TX
DESCRIPTION
Neuroplastin is a cell adhesion molecule of the immunoglobulin (Ig)
superfamily and plays a role in synaptic plasticity processes (Bernstein
et al., 2007).
CLONING
By screening a rat brain cDNA expression library using monoclonal
antibody SMgp65, followed by additional cDNA library screening,
Langnaese et al. (1997) cloned rat Nptn. They identified 2 splice
variants: a deduced 281-amino acid protein corresponding to the 55-kD
glycoprotein (Gp55) species and a deduced 397-amino acid protein
containing a 116-amino acid insertion that corresponds to the 65-kD
glycoprotein (Gp65) species. Both deduced proteins contain a predicted
28-amino acid signal peptide, and the Gp55 species contains 4 C-terminal
residues (DDEP) lacking in the Gp65 species. The deduced mature Gp55 and
Gp65 proteins contain 253 and 365 amino acid residues with calculated
molecular masses of 28.8 and 41.4 kD, respectively. Both species contain
a single putative membrane spanning domain, and Gp55 has 2 extracellular
Ig domains whereas Gp65 has 3 extracellular Ig domains. Gp55 shares
similarity with basigin (109480) Ig domain proteins. Immunocytochemical
studies localized Gp55 and Gp65 to the cell membrane in HEK293 cells.
Northern blot analysis of rat tissues detected a 2.5-kb Gp65 transcript
and 2.2-kb Gp55 transcript in several brain regions; however, the 2.5-kb
transcript showed a brain-specific distribution, whereas the 2.2-kb
transcript was detected in other tissues including kidney, spleen,
thymus, skeletal muscle, heart, and liver. In situ hybridization
detected both transcripts in rat brain, with a more restricted
distribution noted for the 2.5-kb transcript. Langnaese et al. (1997)
stated that Gp65 is most enriched in the postsynaptic density (PSD)
fraction. Expression analysis in postnatal rat brain showed that Gp55
was detected at all stages, whereas Gp65 was low initially, increased
steadily to postnatal day 20 to 25, and then declined to an intermediate
level.
Bernstein et al. (2007) noted that human NPTN contains 2 isoforms termed
NP65 and NP55, similar to the Nptn isoforms detected in rat.
Immunohistochemical studies localized the 2 NPTN isoforms in brain
tissue. Bernstein et al. (2007) noted that unlike the rat ortholog, the
human NP65 isoform was not detected in the hippocampus. Human brain NP65
displayed a predominant localization to the cerebellum, in contrast to
earlier observation of rat Np55 as the predominant isoform in mouse and
rat cerebellum.
GENE FUNCTION
Using immunoaffinity chromatography and mass spectrometry, followed by
coprecipitation and FRET analysis, Sarto-Jackson et al. (2012) found
that rat Np, predominantly the brain-specific Np65 isoform, interacted
with subunits of the rat GABA(A) receptor (see GABRA1; 137160). In
cultured embryonic rat hippocampal neurons and in adult hippocampal
sections, a portion of GABA(A) receptors colocalized with Np in clusters
at both synaptic and extrasynaptic sites. Knockdown of Np in primary
hippocampal neurons via short hairpin RNA led to diffuse staining for
the alpha-2 GABA(A) receptor subunit (GABRA2; 137140) at GABAergic
synapses. Sarto-Jackson et al. (2012) proposed that NP may contribute to
GABA(A) receptor anchoring at specific sites and affect synaptic
strength.
MAPPING
Hartz (2013) mapped the NPTN gene to chromosome 15q24.1 based on an
alignment of the NPTN sequence (GenBank GENBANK AF035287) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Bernstein, H.-G.; Smalla, K.-H.; Bogerts, B.; Gordon-Weeks, P.
R.; Beesley, P. W.; Gundelfinger, E. D.; Kreutz, M. R.: The immunolocalization
of the synaptic glycoprotein neuroplastin differs substantially between
the human and the rodent brain. Brain Res. 1134: 107-112, 2007.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/23/2013.
3. Langnaese, K.; Beesley, P. W.; Gundelfinger, E. D.: Synaptic membrane
glycoprotein gp65 and gp55 are new members of the immunoglobulin superfamily. J.
Biol. Chem. 272: 821-827, 1997.
4. Sarto-Jackson, I.; Milenkovic, I.; Smalla, K.-H.; Gundelfinger,
E. D.; Kaehne, T.; Herrera-Molina, R.; Thomas, S.; Kiebler, M. A.;
Sieghart, W.: The cell adhesion molecule neuroplastin-65 is a novel
interaction partner of gamma-aminobutyric acid type A receptors. J.
Biol. Chem. 287: 14201-14214, 2012.
*FIELD* CN
Patricia A. Hartz - updated: 1/23/2013
*FIELD* CD
Dorothy S. Reilly: 5/27/2009
*FIELD* ED
mgross: 01/24/2013
mgross: 1/24/2013
terry: 1/23/2013
terry: 6/16/2009
wwang: 5/27/2009
*RECORD*
*FIELD* NO
612820
*FIELD* TI
*612820 NEUROPLASTIN; NPTN
;;STROMAL CELL-DERIVED FACTOR RECEPTOR 1; SDFR1
GLYCOPROTEIN, 55-KD, INCLUDED; GP55, INCLUDED;;
read moreNEUROPLASTIN 55, INCLUDED; NP55, INCLUDED;;
GLYCOPROTEIN, 65-KD, INCLUDED; GP65, INCLUDED;;
NEUROPLASTIN 65, INCLUDED; NP65, INCLUDED
*FIELD* TX
DESCRIPTION
Neuroplastin is a cell adhesion molecule of the immunoglobulin (Ig)
superfamily and plays a role in synaptic plasticity processes (Bernstein
et al., 2007).
CLONING
By screening a rat brain cDNA expression library using monoclonal
antibody SMgp65, followed by additional cDNA library screening,
Langnaese et al. (1997) cloned rat Nptn. They identified 2 splice
variants: a deduced 281-amino acid protein corresponding to the 55-kD
glycoprotein (Gp55) species and a deduced 397-amino acid protein
containing a 116-amino acid insertion that corresponds to the 65-kD
glycoprotein (Gp65) species. Both deduced proteins contain a predicted
28-amino acid signal peptide, and the Gp55 species contains 4 C-terminal
residues (DDEP) lacking in the Gp65 species. The deduced mature Gp55 and
Gp65 proteins contain 253 and 365 amino acid residues with calculated
molecular masses of 28.8 and 41.4 kD, respectively. Both species contain
a single putative membrane spanning domain, and Gp55 has 2 extracellular
Ig domains whereas Gp65 has 3 extracellular Ig domains. Gp55 shares
similarity with basigin (109480) Ig domain proteins. Immunocytochemical
studies localized Gp55 and Gp65 to the cell membrane in HEK293 cells.
Northern blot analysis of rat tissues detected a 2.5-kb Gp65 transcript
and 2.2-kb Gp55 transcript in several brain regions; however, the 2.5-kb
transcript showed a brain-specific distribution, whereas the 2.2-kb
transcript was detected in other tissues including kidney, spleen,
thymus, skeletal muscle, heart, and liver. In situ hybridization
detected both transcripts in rat brain, with a more restricted
distribution noted for the 2.5-kb transcript. Langnaese et al. (1997)
stated that Gp65 is most enriched in the postsynaptic density (PSD)
fraction. Expression analysis in postnatal rat brain showed that Gp55
was detected at all stages, whereas Gp65 was low initially, increased
steadily to postnatal day 20 to 25, and then declined to an intermediate
level.
Bernstein et al. (2007) noted that human NPTN contains 2 isoforms termed
NP65 and NP55, similar to the Nptn isoforms detected in rat.
Immunohistochemical studies localized the 2 NPTN isoforms in brain
tissue. Bernstein et al. (2007) noted that unlike the rat ortholog, the
human NP65 isoform was not detected in the hippocampus. Human brain NP65
displayed a predominant localization to the cerebellum, in contrast to
earlier observation of rat Np55 as the predominant isoform in mouse and
rat cerebellum.
GENE FUNCTION
Using immunoaffinity chromatography and mass spectrometry, followed by
coprecipitation and FRET analysis, Sarto-Jackson et al. (2012) found
that rat Np, predominantly the brain-specific Np65 isoform, interacted
with subunits of the rat GABA(A) receptor (see GABRA1; 137160). In
cultured embryonic rat hippocampal neurons and in adult hippocampal
sections, a portion of GABA(A) receptors colocalized with Np in clusters
at both synaptic and extrasynaptic sites. Knockdown of Np in primary
hippocampal neurons via short hairpin RNA led to diffuse staining for
the alpha-2 GABA(A) receptor subunit (GABRA2; 137140) at GABAergic
synapses. Sarto-Jackson et al. (2012) proposed that NP may contribute to
GABA(A) receptor anchoring at specific sites and affect synaptic
strength.
MAPPING
Hartz (2013) mapped the NPTN gene to chromosome 15q24.1 based on an
alignment of the NPTN sequence (GenBank GENBANK AF035287) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Bernstein, H.-G.; Smalla, K.-H.; Bogerts, B.; Gordon-Weeks, P.
R.; Beesley, P. W.; Gundelfinger, E. D.; Kreutz, M. R.: The immunolocalization
of the synaptic glycoprotein neuroplastin differs substantially between
the human and the rodent brain. Brain Res. 1134: 107-112, 2007.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/23/2013.
3. Langnaese, K.; Beesley, P. W.; Gundelfinger, E. D.: Synaptic membrane
glycoprotein gp65 and gp55 are new members of the immunoglobulin superfamily. J.
Biol. Chem. 272: 821-827, 1997.
4. Sarto-Jackson, I.; Milenkovic, I.; Smalla, K.-H.; Gundelfinger,
E. D.; Kaehne, T.; Herrera-Molina, R.; Thomas, S.; Kiebler, M. A.;
Sieghart, W.: The cell adhesion molecule neuroplastin-65 is a novel
interaction partner of gamma-aminobutyric acid type A receptors. J.
Biol. Chem. 287: 14201-14214, 2012.
*FIELD* CN
Patricia A. Hartz - updated: 1/23/2013
*FIELD* CD
Dorothy S. Reilly: 5/27/2009
*FIELD* ED
mgross: 01/24/2013
mgross: 1/24/2013
terry: 1/23/2013
terry: 6/16/2009
wwang: 5/27/2009