Full text data of TAGLN3
TAGLN3
(NP25)
[Confidence: low (only semi-automatic identification from reviews)]
Transgelin-3 (Neuronal protein 22; NP22; Neuronal protein NP25)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transgelin-3 (Neuronal protein 22; NP22; Neuronal protein NP25)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UI15
ID TAGL3_HUMAN Reviewed; 199 AA.
AC Q9UI15; D3DN64; Q96A74;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Transgelin-3;
DE AltName: Full=Neuronal protein 22;
DE Short=NP22;
DE AltName: Full=Neuronal protein NP25;
GN Name=TAGLN3; Synonyms=NP25;
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].
RC TISSUE=Brain;
RX PubMed=11238712; DOI=10.1046/j.1471-4159.2001.00176.x;
RA Fan L., Jaquet V., Dodd P.R., Chen W., Wilce P.A.;
RT "Molecular cloning and characterization of hNP22: a gene up-regulated
RT in human alcoholic brain.";
RL J. Neurochem. 76:1275-1281(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 5-12; 22-49; 55-79; 89-120; 128-139; 146-153 AND
RP 160-196, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
CC -!- TISSUE SPECIFICITY: Widely expressed in the brain. Expression is
CC increased in the superior frontal cortex of alcoholics, but not in
CC the motor cortex or cerebellum.
CC -!- SIMILARITY: Belongs to the calponin family.
CC -!- SIMILARITY: Contains 1 calponin-like repeat.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17189.1; Type=Frameshift; Positions=199;
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; AF303058; AAL09330.1; -; mRNA.
DR EMBL; AF112201; AAF17189.1; ALT_FRAME; mRNA.
DR EMBL; BT007408; AAP36076.1; -; mRNA.
DR EMBL; CH471052; EAW79685.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79686.1; -; Genomic_DNA.
DR EMBL; BC015329; AAH15329.1; -; mRNA.
DR RefSeq; NP_001008273.1; NM_001008272.1.
DR RefSeq; NP_001008274.1; NM_001008273.1.
DR RefSeq; NP_037391.2; NM_013259.2.
DR UniGene; Hs.169330; -.
DR ProteinModelPortal; Q9UI15; -.
DR SMR; Q9UI15; 25-153.
DR STRING; 9606.ENSP00000273368; -.
DR PhosphoSite; Q9UI15; -.
DR DMDM; 33860182; -.
DR UCD-2DPAGE; Q9UI15; -.
DR PaxDb; Q9UI15; -.
DR PRIDE; Q9UI15; -.
DR DNASU; 29114; -.
DR Ensembl; ENST00000273368; ENSP00000273368; ENSG00000144834.
DR Ensembl; ENST00000393917; ENSP00000377494; ENSG00000144834.
DR Ensembl; ENST00000455401; ENSP00000391160; ENSG00000144834.
DR Ensembl; ENST00000478951; ENSP00000419105; ENSG00000144834.
DR GeneID; 29114; -.
DR KEGG; hsa:29114; -.
DR UCSC; uc003dyl.3; human.
DR CTD; 29114; -.
DR GeneCards; GC03P111717; -.
DR HGNC; HGNC:29868; TAGLN3.
DR MIM; 607953; gene.
DR neXtProt; NX_Q9UI15; -.
DR PharmGKB; PA134896732; -.
DR eggNOG; COG5199; -.
DR HOVERGEN; HBG005186; -.
DR InParanoid; Q9UI15; -.
DR OMA; QMAFKQM; -.
DR OrthoDB; EOG718KD9; -.
DR GeneWiki; TAGLN3; -.
DR GenomeRNAi; 29114; -.
DR NextBio; 52187; -.
DR PRO; PR:Q9UI15; -.
DR ArrayExpress; Q9UI15; -.
DR Bgee; Q9UI15; -.
DR CleanEx; HS_TAGLN3; -.
DR Genevestigator; Q9UI15; -.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR000557; Calponin_repeat.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR001061; TAGLN.
DR PANTHER; PTHR18959:SF5; PTHR18959:SF5; 1.
DR Pfam; PF00402; Calponin; 1.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS01052; CALPONIN_1; 1.
DR PROSITE; PS51122; CALPONIN_2; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Reference proteome.
FT CHAIN 1 199 Transgelin-3.
FT /FTId=PRO_0000204788.
FT DOMAIN 24 136 CH.
FT REPEAT 174 199 Calponin-like.
SQ SEQUENCE 199 AA; 22473 MW; 09837A0CC2A0E157 CRC64;
MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT
VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK
DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS
NKGASQAGMT GYGMPRQIM
//
ID TAGL3_HUMAN Reviewed; 199 AA.
AC Q9UI15; D3DN64; Q96A74;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Transgelin-3;
DE AltName: Full=Neuronal protein 22;
DE Short=NP22;
DE AltName: Full=Neuronal protein NP25;
GN Name=TAGLN3; Synonyms=NP25;
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].
RC TISSUE=Brain;
RX PubMed=11238712; DOI=10.1046/j.1471-4159.2001.00176.x;
RA Fan L., Jaquet V., Dodd P.R., Chen W., Wilce P.A.;
RT "Molecular cloning and characterization of hNP22: a gene up-regulated
RT in human alcoholic brain.";
RL J. Neurochem. 76:1275-1281(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 5-12; 22-49; 55-79; 89-120; 128-139; 146-153 AND
RP 160-196, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
CC -!- TISSUE SPECIFICITY: Widely expressed in the brain. Expression is
CC increased in the superior frontal cortex of alcoholics, but not in
CC the motor cortex or cerebellum.
CC -!- SIMILARITY: Belongs to the calponin family.
CC -!- SIMILARITY: Contains 1 calponin-like repeat.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17189.1; Type=Frameshift; Positions=199;
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; AF303058; AAL09330.1; -; mRNA.
DR EMBL; AF112201; AAF17189.1; ALT_FRAME; mRNA.
DR EMBL; BT007408; AAP36076.1; -; mRNA.
DR EMBL; CH471052; EAW79685.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79686.1; -; Genomic_DNA.
DR EMBL; BC015329; AAH15329.1; -; mRNA.
DR RefSeq; NP_001008273.1; NM_001008272.1.
DR RefSeq; NP_001008274.1; NM_001008273.1.
DR RefSeq; NP_037391.2; NM_013259.2.
DR UniGene; Hs.169330; -.
DR ProteinModelPortal; Q9UI15; -.
DR SMR; Q9UI15; 25-153.
DR STRING; 9606.ENSP00000273368; -.
DR PhosphoSite; Q9UI15; -.
DR DMDM; 33860182; -.
DR UCD-2DPAGE; Q9UI15; -.
DR PaxDb; Q9UI15; -.
DR PRIDE; Q9UI15; -.
DR DNASU; 29114; -.
DR Ensembl; ENST00000273368; ENSP00000273368; ENSG00000144834.
DR Ensembl; ENST00000393917; ENSP00000377494; ENSG00000144834.
DR Ensembl; ENST00000455401; ENSP00000391160; ENSG00000144834.
DR Ensembl; ENST00000478951; ENSP00000419105; ENSG00000144834.
DR GeneID; 29114; -.
DR KEGG; hsa:29114; -.
DR UCSC; uc003dyl.3; human.
DR CTD; 29114; -.
DR GeneCards; GC03P111717; -.
DR HGNC; HGNC:29868; TAGLN3.
DR MIM; 607953; gene.
DR neXtProt; NX_Q9UI15; -.
DR PharmGKB; PA134896732; -.
DR eggNOG; COG5199; -.
DR HOVERGEN; HBG005186; -.
DR InParanoid; Q9UI15; -.
DR OMA; QMAFKQM; -.
DR OrthoDB; EOG718KD9; -.
DR GeneWiki; TAGLN3; -.
DR GenomeRNAi; 29114; -.
DR NextBio; 52187; -.
DR PRO; PR:Q9UI15; -.
DR ArrayExpress; Q9UI15; -.
DR Bgee; Q9UI15; -.
DR CleanEx; HS_TAGLN3; -.
DR Genevestigator; Q9UI15; -.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR000557; Calponin_repeat.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR001061; TAGLN.
DR PANTHER; PTHR18959:SF5; PTHR18959:SF5; 1.
DR Pfam; PF00402; Calponin; 1.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS01052; CALPONIN_1; 1.
DR PROSITE; PS51122; CALPONIN_2; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Reference proteome.
FT CHAIN 1 199 Transgelin-3.
FT /FTId=PRO_0000204788.
FT DOMAIN 24 136 CH.
FT REPEAT 174 199 Calponin-like.
SQ SEQUENCE 199 AA; 22473 MW; 09837A0CC2A0E157 CRC64;
MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT
VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK
DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS
NKGASQAGMT GYGMPRQIM
//
MIM
607953
*RECORD*
*FIELD* NO
607953
*FIELD* TI
*607953 NEURONAL PROTEIN, 25-KD, RAT, HOMOLOG OF
;;NP25;;
NEURONAL PROTEIN, 22-KD; NP22
read more*FIELD* TX
CLONING
Ren et al. (1994) cloned Np25 from a rat brain cDNA library. The deduced
219-amino acid protein contains an EF-hand-like motif, a C-terminal
ATP-binding sequence, and several putative phosphorylation sites. Np25
shares significant homology with rat SM22-alpha (600818), Mp20, and
calponin (see 600806). Northern blot analysis detected a single 1.0-kb
transcript in rat brain and spinal cord, in most specific rat brain
regions examined, and in human cortex and cerebellum. In situ
hybridization of rat brain detected highest expression in central
amygdaloid nuclei and glomeruli in the granule layer of the cerebellum.
By pH gradient electrophoresis, Ren et al. (1994) identified at least 2
isoforms of Np25 with similar molecular masses.
By differential display analysis, Fan et al. (2001) found heightened
expression of NP25, which they designated NP22, in brains of alcoholic
individuals. They obtained the full-length clone by screening a brain
cDNA library. The deduced 199-amino acid protein has a calculated
molecular mass of about 22.5 kD. NP25 contains 2 putative EF-hand
calcium-binding sites and several putative phosphorylation sites, but no
ATP-binding site or glycosylation site. Northern blot analysis detected
a 1.35-kb transcript in all brain regions examined. NP25 shares about
97% homology with rat Np25.
GENE FUNCTION
Fan et al. (2001) found increased expression of NP25 in the superior
frontal cortex of alcoholic brains compared with nonalcoholic controls.
There was no enhanced expression in the primary motor cortex or
cerebellum.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NP25
gene to chromosome 3 (TMAP sts-H20135).
*FIELD* RF
1. Fan, L.; Jaquet, V.; Dodd, P. R.; Chen, W.; Wilce, P. A.: Molecular
cloning and characterization of hNP22: a gene up-regulated in human
alcoholic brain. J. Neurochem. 76: 1275-1281, 2001.
2. Ren, W.-Z.; Ng, G. Y. K.; Wang, R.-X.; Wu, P. H.; O'Dowd, B. F.;
Osmond, D. H.; George, S. R.; Liew, C.-C.: The identification of
NP25: a novel protein that is differentially expressed by neuronal
subpopulations. Molec. Brain Res. 22: 173-185, 1994.
*FIELD* CD
Patricia A. Hartz: 7/17/2003
*FIELD* ED
terry: 05/10/2006
mgross: 7/17/2003
*RECORD*
*FIELD* NO
607953
*FIELD* TI
*607953 NEURONAL PROTEIN, 25-KD, RAT, HOMOLOG OF
;;NP25;;
NEURONAL PROTEIN, 22-KD; NP22
read more*FIELD* TX
CLONING
Ren et al. (1994) cloned Np25 from a rat brain cDNA library. The deduced
219-amino acid protein contains an EF-hand-like motif, a C-terminal
ATP-binding sequence, and several putative phosphorylation sites. Np25
shares significant homology with rat SM22-alpha (600818), Mp20, and
calponin (see 600806). Northern blot analysis detected a single 1.0-kb
transcript in rat brain and spinal cord, in most specific rat brain
regions examined, and in human cortex and cerebellum. In situ
hybridization of rat brain detected highest expression in central
amygdaloid nuclei and glomeruli in the granule layer of the cerebellum.
By pH gradient electrophoresis, Ren et al. (1994) identified at least 2
isoforms of Np25 with similar molecular masses.
By differential display analysis, Fan et al. (2001) found heightened
expression of NP25, which they designated NP22, in brains of alcoholic
individuals. They obtained the full-length clone by screening a brain
cDNA library. The deduced 199-amino acid protein has a calculated
molecular mass of about 22.5 kD. NP25 contains 2 putative EF-hand
calcium-binding sites and several putative phosphorylation sites, but no
ATP-binding site or glycosylation site. Northern blot analysis detected
a 1.35-kb transcript in all brain regions examined. NP25 shares about
97% homology with rat Np25.
GENE FUNCTION
Fan et al. (2001) found increased expression of NP25 in the superior
frontal cortex of alcoholic brains compared with nonalcoholic controls.
There was no enhanced expression in the primary motor cortex or
cerebellum.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NP25
gene to chromosome 3 (TMAP sts-H20135).
*FIELD* RF
1. Fan, L.; Jaquet, V.; Dodd, P. R.; Chen, W.; Wilce, P. A.: Molecular
cloning and characterization of hNP22: a gene up-regulated in human
alcoholic brain. J. Neurochem. 76: 1275-1281, 2001.
2. Ren, W.-Z.; Ng, G. Y. K.; Wang, R.-X.; Wu, P. H.; O'Dowd, B. F.;
Osmond, D. H.; George, S. R.; Liew, C.-C.: The identification of
NP25: a novel protein that is differentially expressed by neuronal
subpopulations. Molec. Brain Res. 22: 173-185, 1994.
*FIELD* CD
Patricia A. Hartz: 7/17/2003
*FIELD* ED
terry: 05/10/2006
mgross: 7/17/2003