Full text data of PLAA
PLAA
(PLAP)
[Confidence: low (only semi-automatic identification from reviews)]
Phospholipase A-2-activating protein; PLA2P; PLAP
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phospholipase A-2-activating protein; PLA2P; PLAP
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y263
ID PLAP_HUMAN Reviewed; 795 AA.
AC Q9Y263; Q53EU5; Q5VY33; Q9NUL8; Q9NVE9; Q9UF53; Q9Y5L1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-JUN-2006, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Phospholipase A-2-activating protein;
DE Short=PLA2P;
DE Short=PLAP;
GN Name=PLAA; Synonyms=PLAP;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-795.
RX PubMed=10644453; DOI=10.1006/geno.1999.5999;
RA Beatty B., Qi S., Pienkowska M., Scherer S.W., Testa J.R., Cheng J.Q.,
RA Herbrick J.-A., Scheidl T., Zhang Z., Kola I., Seth A.;
RT "Chromosomal localization of phospholipase A2 activating protein, an
RT ets2 target gene, to 9p21.";
RL Genomics 62:529-532(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-795.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-795.
RC TISSUE=Fetal brain;
RX PubMed=10571045; DOI=10.1016/S0378-1119(99)00354-6;
RA Ruiz A., Nadal M., Puig S., Estivill X.;
RT "Cloning of the human phospholipase A2 activating protein (hPLAP) gene
RT on the chromosome 9p21 melanoma deleted region.";
RL Gene 239:155-161(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-795.
RX PubMed=9931468; DOI=10.1016/S0167-4781(98)00249-8;
RA Chopra A.K., Ribardo D.A., Wood T.G., Prusak D.J., Xu X.-J.,
RA Peterson J.W.;
RT "Molecular characterization of cDNA for phospholipase A2-activating
RT protein.";
RL Biochim. Biophys. Acta 1444:125-130(1999).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-529, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(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).
RN [11]
RP STRUCTURE BY NMR OF 386-465, AND INTERACTION WITH UBIQUITIN.
RX PubMed=19423704; DOI=10.1074/jbc.M109.009126;
RA Fu Q.-S., Zhou C.-J., Gao H.-C., Jiang Y.-J., Zhou Z.-R., Hong J.,
RA Yao W.-M., Song A.-X., Lin D.-H., Hu H.-Y.;
RT "Structural basis for ubiquitin recognition by a novel domain from
RT human phospholipase A2-activating protein.";
RL J. Biol. Chem. 284:19043-19052(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 511-795 IN COMPLEX WITH VCP,
RP AND DOMAIN ARM REPEATS.
RX PubMed=19887378; DOI=10.1074/jbc.M109.044685;
RA Qiu L., Pashkova N., Walker J.R., Winistorfer S., Allali-Hassani A.,
RA Akutsu M., Piper R., Dhe-Paganon S.;
RT "Structure and function of the PLAA/Ufd3-p97/Cdc48 complex.";
RL J. Biol. Chem. 285:365-372(2010).
CC -!- FUNCTION: Involved in the maintenance of ubiquitin levels (By
CC similarity).
CC -!- SUBUNIT: Interacts with ubiquitin. Interacts with VCP.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=3; IntAct=EBI-1994037, EBI-6248077;
CC -!- DOMAIN: The PUL domain is composed of 6 armadillo-like repeats and
CC mediates the interaction with VCP C-terminus.
CC -!- DOMAIN: The PFU domain mediates interaction with ubiquitin.
CC -!- SIMILARITY: Belongs to the WD repeat PLAP family.
CC -!- SIMILARITY: Contains 6 ARM repeats.
CC -!- SIMILARITY: Contains 1 PFU domain.
CC -!- SIMILARITY: Contains 1 PUL domain.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03030.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD42075.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD42075.1; Type=Frameshift; Positions=698;
CC Sequence=BAA92105.1; Type=Erroneous termination; Positions=545; Note=Translated as Gln;
CC Sequence=BAD97264.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB42881.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAH72641.1; Type=Erroneous gene model prediction;
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DR EMBL; AK001642; BAA91803.1; -; mRNA.
DR EMBL; AK002143; BAA92105.1; ALT_SEQ; mRNA.
DR EMBL; AL133608; CAB63739.1; -; mRNA.
DR EMBL; AL356133; CAH72641.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC032551; AAH32551.1; -; mRNA.
DR EMBL; AF145020; AAD42075.1; ALT_SEQ; mRNA.
DR EMBL; AK223544; BAD97264.1; ALT_INIT; mRNA.
DR EMBL; AJ238243; CAB42881.1; ALT_INIT; mRNA.
DR EMBL; AF083395; AAD03030.1; ALT_INIT; mRNA.
DR PIR; T43447; T43447.
DR RefSeq; NP_001026859.1; NM_001031689.2.
DR UniGene; Hs.27182; -.
DR PDB; 2K89; NMR; -; A=386-465.
DR PDB; 2K8A; NMR; -; A=386-465.
DR PDB; 2K8B; NMR; -; B=386-465.
DR PDB; 2K8C; NMR; -; B=386-465.
DR PDB; 3EBB; X-ray; 1.90 A; A/B/C/D=511-795.
DR PDBsum; 2K89; -.
DR PDBsum; 2K8A; -.
DR PDBsum; 2K8B; -.
DR PDBsum; 2K8C; -.
DR PDBsum; 3EBB; -.
DR ProteinModelPortal; Q9Y263; -.
DR SMR; Q9Y263; 13-378, 386-465, 531-795.
DR IntAct; Q9Y263; 13.
DR MINT; MINT-3084225; -.
DR STRING; 9606.ENSP00000380460; -.
DR BindingDB; Q9Y263; -.
DR ChEMBL; CHEMBL6114; -.
DR PhosphoSite; Q9Y263; -.
DR DMDM; 108935868; -.
DR PaxDb; Q9Y263; -.
DR PRIDE; Q9Y263; -.
DR DNASU; 9373; -.
DR Ensembl; ENST00000397292; ENSP00000380460; ENSG00000137055.
DR GeneID; 9373; -.
DR KEGG; hsa:9373; -.
DR UCSC; uc003zqd.3; human.
DR CTD; 9373; -.
DR GeneCards; GC09M026903; -.
DR HGNC; HGNC:9043; PLAA.
DR HPA; CAB005035; -.
DR HPA; HPA020994; -.
DR HPA; HPA020996; -.
DR MIM; 603873; gene.
DR neXtProt; NX_Q9Y263; -.
DR PharmGKB; PA33370; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000174247; -.
DR HOVERGEN; HBG008204; -.
DR InParanoid; Q9Y263; -.
DR KO; K14018; -.
DR OMA; AQSVWCC; -.
DR OrthoDB; EOG7D2FCZ; -.
DR SignaLink; Q9Y263; -.
DR ChiTaRS; PLAA; human.
DR EvolutionaryTrace; Q9Y263; -.
DR GeneWiki; PLAA_(gene); -.
DR GenomeRNAi; 9373; -.
DR NextBio; 35110; -.
DR PRO; PR:Q9Y263; -.
DR ArrayExpress; Q9Y263; -.
DR Bgee; Q9Y263; -.
DR CleanEx; HS_PLAA; -.
DR Genevestigator; Q9Y263; -.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0016005; F:phospholipase A2 activator activity; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015155; PLAA_fam_Ub-bd_PFU.
DR InterPro; IPR013535; PUL.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF09070; PFU; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
DR PROSITE; PS51394; PFU; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1 795 Phospholipase A-2-activating protein.
FT /FTId=PRO_0000051130.
FT REPEAT 17 56 WD 1.
FT REPEAT 63 107 WD 2.
FT REPEAT 110 148 WD 3.
FT REPEAT 149 188 WD 4.
FT REPEAT 190 227 WD 5.
FT REPEAT 229 268 WD 6.
FT REPEAT 270 307 WD 7.
FT DOMAIN 366 465 PFU.
FT DOMAIN 533 794 PUL.
FT REPEAT 546 588 ARM 1.
FT REPEAT 589 620 ARM 2.
FT REPEAT 621 669 ARM 3.
FT REPEAT 670 715 ARM 4.
FT REPEAT 716 755 ARM 5.
FT REPEAT 756 795 ARM 6.
FT MOD_RES 529 529 N6-acetyllysine.
FT CONFLICT 14 14 L -> F (in Ref. 5; AAD42075).
FT CONFLICT 57 57 E -> D (in Ref. 5; AAD42075).
FT CONFLICT 86 86 A -> F (in Ref. 5; AAD42075).
FT CONFLICT 97 97 F -> L (in Ref. 5; AAD42075).
FT CONFLICT 172 172 D -> G (in Ref. 1; BAA91803).
FT CONFLICT 363 363 E -> K (in Ref. 6; BAD97264).
FT CONFLICT 422 422 T -> A (in Ref. 5; AAD42075).
FT CONFLICT 520 520 N -> S (in Ref. 1; BAA92105).
FT CONFLICT 531 531 M -> L (in Ref. 5; AAD42075).
FT CONFLICT 541 541 V -> L (in Ref. 5; AAD42075).
FT CONFLICT 746 746 L -> P (in Ref. 5; AAD42075).
FT STRAND 390 392
FT STRAND 394 396
FT STRAND 399 407
FT STRAND 410 412
FT STRAND 416 420
FT HELIX 426 437
FT HELIX 443 455
FT TURN 457 460
FT HELIX 548 559
FT HELIX 564 566
FT HELIX 571 584
FT HELIX 593 603
FT TURN 607 609
FT HELIX 611 620
FT HELIX 624 631
FT TURN 633 635
FT HELIX 636 645
FT HELIX 653 665
FT HELIX 666 668
FT HELIX 670 678
FT HELIX 680 688
FT HELIX 689 691
FT HELIX 696 715
FT HELIX 719 733
FT HELIX 739 753
FT HELIX 757 765
FT HELIX 768 771
FT HELIX 772 777
FT HELIX 782 792
SQ SEQUENCE 795 AA; 87157 MW; D6E7330AC9891637 CRC64;
MTSGATRYRL SCSLRGHELD VRGLVCCAYP PGAFVSVSRD RTTRLWAPDS PNRSFTEMHC
MSGHSNFVSC VCIIPSSDIY PHGLIATGGN DHNICIFSLD SPMPLYILKG HKNTVCSLSS
GKFGTLLSGS WDTTAKVWLN DKCMMTLQGH TAAVWAVKIL PEQGLMLTGS ADKTVKLWKA
GRCERTFSGH EDCVRGLAIL SETEFLSCAN DASIRRWQIT GECLEVYYGH TNYIYSISVF
PNCRDFVTTA EDRSLRIWKH GECAQTIRLP AQSIWCCCVL DNGDIVVGAS DGIIRVFTES
EDRTASAEEI KAFEKELSHA TIDSKTGDLG DINAEQLPGR EHLNEPGTRE GQTRLIRDGE
KVEAYQWSVS EGRWIKIGDV VGSSGANQQT SGKVLYEGKE FDYVFSIDVN EGGPSYKLPY
NTSDDPWLTA YNFLQKNDLN PMFLDQVAKF IIDNTKGQML GLGNPSFSDP FTGGGRYVPG
SSGSSNTLPT ADPFTGAGRY VPGSASMGTT MAGVDPFTGN SAYRSAASKT MNIYFPKKEA
VTFDQANPTQ ILGKLKELNG TAPEEKKLTE DDLILLEKIL SLICNSSSEK PTVQQLQILW
KAINCPEDIV FPALDILRLS IKHPSVNENF CNEKEGAQFS SHLINLLNPK GKPANQLLAL
RTFCNCFVGQ AGQKLMMSQR ESLMSHAIEL KSGSNKNIHI ALATLALNYS VCFHKDHNIE
GKAQCLSLIS TILEVVQDLE ATFRLLVALG TLISDDSNAV QLAKSLGVDS QIKKYSSVSE
PAKVSECCRF ILNLL
//
ID PLAP_HUMAN Reviewed; 795 AA.
AC Q9Y263; Q53EU5; Q5VY33; Q9NUL8; Q9NVE9; Q9UF53; Q9Y5L1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-JUN-2006, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Phospholipase A-2-activating protein;
DE Short=PLA2P;
DE Short=PLAP;
GN Name=PLAA; Synonyms=PLAP;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-795.
RX PubMed=10644453; DOI=10.1006/geno.1999.5999;
RA Beatty B., Qi S., Pienkowska M., Scherer S.W., Testa J.R., Cheng J.Q.,
RA Herbrick J.-A., Scheidl T., Zhang Z., Kola I., Seth A.;
RT "Chromosomal localization of phospholipase A2 activating protein, an
RT ets2 target gene, to 9p21.";
RL Genomics 62:529-532(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-795.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-795.
RC TISSUE=Fetal brain;
RX PubMed=10571045; DOI=10.1016/S0378-1119(99)00354-6;
RA Ruiz A., Nadal M., Puig S., Estivill X.;
RT "Cloning of the human phospholipase A2 activating protein (hPLAP) gene
RT on the chromosome 9p21 melanoma deleted region.";
RL Gene 239:155-161(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-795.
RX PubMed=9931468; DOI=10.1016/S0167-4781(98)00249-8;
RA Chopra A.K., Ribardo D.A., Wood T.G., Prusak D.J., Xu X.-J.,
RA Peterson J.W.;
RT "Molecular characterization of cDNA for phospholipase A2-activating
RT protein.";
RL Biochim. Biophys. Acta 1444:125-130(1999).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-529, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(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).
RN [11]
RP STRUCTURE BY NMR OF 386-465, AND INTERACTION WITH UBIQUITIN.
RX PubMed=19423704; DOI=10.1074/jbc.M109.009126;
RA Fu Q.-S., Zhou C.-J., Gao H.-C., Jiang Y.-J., Zhou Z.-R., Hong J.,
RA Yao W.-M., Song A.-X., Lin D.-H., Hu H.-Y.;
RT "Structural basis for ubiquitin recognition by a novel domain from
RT human phospholipase A2-activating protein.";
RL J. Biol. Chem. 284:19043-19052(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 511-795 IN COMPLEX WITH VCP,
RP AND DOMAIN ARM REPEATS.
RX PubMed=19887378; DOI=10.1074/jbc.M109.044685;
RA Qiu L., Pashkova N., Walker J.R., Winistorfer S., Allali-Hassani A.,
RA Akutsu M., Piper R., Dhe-Paganon S.;
RT "Structure and function of the PLAA/Ufd3-p97/Cdc48 complex.";
RL J. Biol. Chem. 285:365-372(2010).
CC -!- FUNCTION: Involved in the maintenance of ubiquitin levels (By
CC similarity).
CC -!- SUBUNIT: Interacts with ubiquitin. Interacts with VCP.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=3; IntAct=EBI-1994037, EBI-6248077;
CC -!- DOMAIN: The PUL domain is composed of 6 armadillo-like repeats and
CC mediates the interaction with VCP C-terminus.
CC -!- DOMAIN: The PFU domain mediates interaction with ubiquitin.
CC -!- SIMILARITY: Belongs to the WD repeat PLAP family.
CC -!- SIMILARITY: Contains 6 ARM repeats.
CC -!- SIMILARITY: Contains 1 PFU domain.
CC -!- SIMILARITY: Contains 1 PUL domain.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03030.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD42075.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD42075.1; Type=Frameshift; Positions=698;
CC Sequence=BAA92105.1; Type=Erroneous termination; Positions=545; Note=Translated as Gln;
CC Sequence=BAD97264.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB42881.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAH72641.1; Type=Erroneous gene model prediction;
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DR EMBL; AK001642; BAA91803.1; -; mRNA.
DR EMBL; AK002143; BAA92105.1; ALT_SEQ; mRNA.
DR EMBL; AL133608; CAB63739.1; -; mRNA.
DR EMBL; AL356133; CAH72641.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC032551; AAH32551.1; -; mRNA.
DR EMBL; AF145020; AAD42075.1; ALT_SEQ; mRNA.
DR EMBL; AK223544; BAD97264.1; ALT_INIT; mRNA.
DR EMBL; AJ238243; CAB42881.1; ALT_INIT; mRNA.
DR EMBL; AF083395; AAD03030.1; ALT_INIT; mRNA.
DR PIR; T43447; T43447.
DR RefSeq; NP_001026859.1; NM_001031689.2.
DR UniGene; Hs.27182; -.
DR PDB; 2K89; NMR; -; A=386-465.
DR PDB; 2K8A; NMR; -; A=386-465.
DR PDB; 2K8B; NMR; -; B=386-465.
DR PDB; 2K8C; NMR; -; B=386-465.
DR PDB; 3EBB; X-ray; 1.90 A; A/B/C/D=511-795.
DR PDBsum; 2K89; -.
DR PDBsum; 2K8A; -.
DR PDBsum; 2K8B; -.
DR PDBsum; 2K8C; -.
DR PDBsum; 3EBB; -.
DR ProteinModelPortal; Q9Y263; -.
DR SMR; Q9Y263; 13-378, 386-465, 531-795.
DR IntAct; Q9Y263; 13.
DR MINT; MINT-3084225; -.
DR STRING; 9606.ENSP00000380460; -.
DR BindingDB; Q9Y263; -.
DR ChEMBL; CHEMBL6114; -.
DR PhosphoSite; Q9Y263; -.
DR DMDM; 108935868; -.
DR PaxDb; Q9Y263; -.
DR PRIDE; Q9Y263; -.
DR DNASU; 9373; -.
DR Ensembl; ENST00000397292; ENSP00000380460; ENSG00000137055.
DR GeneID; 9373; -.
DR KEGG; hsa:9373; -.
DR UCSC; uc003zqd.3; human.
DR CTD; 9373; -.
DR GeneCards; GC09M026903; -.
DR HGNC; HGNC:9043; PLAA.
DR HPA; CAB005035; -.
DR HPA; HPA020994; -.
DR HPA; HPA020996; -.
DR MIM; 603873; gene.
DR neXtProt; NX_Q9Y263; -.
DR PharmGKB; PA33370; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000174247; -.
DR HOVERGEN; HBG008204; -.
DR InParanoid; Q9Y263; -.
DR KO; K14018; -.
DR OMA; AQSVWCC; -.
DR OrthoDB; EOG7D2FCZ; -.
DR SignaLink; Q9Y263; -.
DR ChiTaRS; PLAA; human.
DR EvolutionaryTrace; Q9Y263; -.
DR GeneWiki; PLAA_(gene); -.
DR GenomeRNAi; 9373; -.
DR NextBio; 35110; -.
DR PRO; PR:Q9Y263; -.
DR ArrayExpress; Q9Y263; -.
DR Bgee; Q9Y263; -.
DR CleanEx; HS_PLAA; -.
DR Genevestigator; Q9Y263; -.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0016005; F:phospholipase A2 activator activity; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015155; PLAA_fam_Ub-bd_PFU.
DR InterPro; IPR013535; PUL.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF09070; PFU; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
DR PROSITE; PS51394; PFU; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1 795 Phospholipase A-2-activating protein.
FT /FTId=PRO_0000051130.
FT REPEAT 17 56 WD 1.
FT REPEAT 63 107 WD 2.
FT REPEAT 110 148 WD 3.
FT REPEAT 149 188 WD 4.
FT REPEAT 190 227 WD 5.
FT REPEAT 229 268 WD 6.
FT REPEAT 270 307 WD 7.
FT DOMAIN 366 465 PFU.
FT DOMAIN 533 794 PUL.
FT REPEAT 546 588 ARM 1.
FT REPEAT 589 620 ARM 2.
FT REPEAT 621 669 ARM 3.
FT REPEAT 670 715 ARM 4.
FT REPEAT 716 755 ARM 5.
FT REPEAT 756 795 ARM 6.
FT MOD_RES 529 529 N6-acetyllysine.
FT CONFLICT 14 14 L -> F (in Ref. 5; AAD42075).
FT CONFLICT 57 57 E -> D (in Ref. 5; AAD42075).
FT CONFLICT 86 86 A -> F (in Ref. 5; AAD42075).
FT CONFLICT 97 97 F -> L (in Ref. 5; AAD42075).
FT CONFLICT 172 172 D -> G (in Ref. 1; BAA91803).
FT CONFLICT 363 363 E -> K (in Ref. 6; BAD97264).
FT CONFLICT 422 422 T -> A (in Ref. 5; AAD42075).
FT CONFLICT 520 520 N -> S (in Ref. 1; BAA92105).
FT CONFLICT 531 531 M -> L (in Ref. 5; AAD42075).
FT CONFLICT 541 541 V -> L (in Ref. 5; AAD42075).
FT CONFLICT 746 746 L -> P (in Ref. 5; AAD42075).
FT STRAND 390 392
FT STRAND 394 396
FT STRAND 399 407
FT STRAND 410 412
FT STRAND 416 420
FT HELIX 426 437
FT HELIX 443 455
FT TURN 457 460
FT HELIX 548 559
FT HELIX 564 566
FT HELIX 571 584
FT HELIX 593 603
FT TURN 607 609
FT HELIX 611 620
FT HELIX 624 631
FT TURN 633 635
FT HELIX 636 645
FT HELIX 653 665
FT HELIX 666 668
FT HELIX 670 678
FT HELIX 680 688
FT HELIX 689 691
FT HELIX 696 715
FT HELIX 719 733
FT HELIX 739 753
FT HELIX 757 765
FT HELIX 768 771
FT HELIX 772 777
FT HELIX 782 792
SQ SEQUENCE 795 AA; 87157 MW; D6E7330AC9891637 CRC64;
MTSGATRYRL SCSLRGHELD VRGLVCCAYP PGAFVSVSRD RTTRLWAPDS PNRSFTEMHC
MSGHSNFVSC VCIIPSSDIY PHGLIATGGN DHNICIFSLD SPMPLYILKG HKNTVCSLSS
GKFGTLLSGS WDTTAKVWLN DKCMMTLQGH TAAVWAVKIL PEQGLMLTGS ADKTVKLWKA
GRCERTFSGH EDCVRGLAIL SETEFLSCAN DASIRRWQIT GECLEVYYGH TNYIYSISVF
PNCRDFVTTA EDRSLRIWKH GECAQTIRLP AQSIWCCCVL DNGDIVVGAS DGIIRVFTES
EDRTASAEEI KAFEKELSHA TIDSKTGDLG DINAEQLPGR EHLNEPGTRE GQTRLIRDGE
KVEAYQWSVS EGRWIKIGDV VGSSGANQQT SGKVLYEGKE FDYVFSIDVN EGGPSYKLPY
NTSDDPWLTA YNFLQKNDLN PMFLDQVAKF IIDNTKGQML GLGNPSFSDP FTGGGRYVPG
SSGSSNTLPT ADPFTGAGRY VPGSASMGTT MAGVDPFTGN SAYRSAASKT MNIYFPKKEA
VTFDQANPTQ ILGKLKELNG TAPEEKKLTE DDLILLEKIL SLICNSSSEK PTVQQLQILW
KAINCPEDIV FPALDILRLS IKHPSVNENF CNEKEGAQFS SHLINLLNPK GKPANQLLAL
RTFCNCFVGQ AGQKLMMSQR ESLMSHAIEL KSGSNKNIHI ALATLALNYS VCFHKDHNIE
GKAQCLSLIS TILEVVQDLE ATFRLLVALG TLISDDSNAV QLAKSLGVDS QIKKYSSVSE
PAKVSECCRF ILNLL
//
MIM
603873
*RECORD*
*FIELD* NO
603873
*FIELD* TI
*603873 PHOSPHOLIPASE A2-ACTIVATING PROTEIN; PLAA
;;PLAP
*FIELD* TX
Phospholipase A2-activating protein (PLAP) is potentially important in
read moreregulating the inflammatory response through its activation of
phospholipase A2 (e.g., 600522), which catalyzes the release of
arachidonic acid. By screening a human monocyte cDNA library with a
mouse Plap cDNA, Chopra et al. (1999) isolated human PLAP cDNAs. The
738-amino acid human PLAP protein predicted by the cDNA sequence has a
molecular mass of 80,826 kD; however, immunoblot analysis using
antibodies against PLAP detected a 72- to 74-kD protein in human
monocyte cell lysates. In mouse macrophages, an antisense Plap
oligonucleotide blocked cholera toxin-induced arachidonic acid release,
indicating a role for PLAP in the regulation of phospholipase A2
activation.
*FIELD* RF
1. Chopra, A. K.; Ribardo, D. A.; Wood, T. G.; Prusak, D. J.; Xu,
X.-J.; Peterson, J. W.: Molecular characterization of cDNA for phospholipase
A2-activating protein. Biochim. Biophys. Acta 1444: 125-130, 1999.
*FIELD* CD
Stefanie A. Nelson: 6/3/1999
*FIELD* ED
psherman: 06/03/1999
*RECORD*
*FIELD* NO
603873
*FIELD* TI
*603873 PHOSPHOLIPASE A2-ACTIVATING PROTEIN; PLAA
;;PLAP
*FIELD* TX
Phospholipase A2-activating protein (PLAP) is potentially important in
read moreregulating the inflammatory response through its activation of
phospholipase A2 (e.g., 600522), which catalyzes the release of
arachidonic acid. By screening a human monocyte cDNA library with a
mouse Plap cDNA, Chopra et al. (1999) isolated human PLAP cDNAs. The
738-amino acid human PLAP protein predicted by the cDNA sequence has a
molecular mass of 80,826 kD; however, immunoblot analysis using
antibodies against PLAP detected a 72- to 74-kD protein in human
monocyte cell lysates. In mouse macrophages, an antisense Plap
oligonucleotide blocked cholera toxin-induced arachidonic acid release,
indicating a role for PLAP in the regulation of phospholipase A2
activation.
*FIELD* RF
1. Chopra, A. K.; Ribardo, D. A.; Wood, T. G.; Prusak, D. J.; Xu,
X.-J.; Peterson, J. W.: Molecular characterization of cDNA for phospholipase
A2-activating protein. Biochim. Biophys. Acta 1444: 125-130, 1999.
*FIELD* CD
Stefanie A. Nelson: 6/3/1999
*FIELD* ED
psherman: 06/03/1999