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Putative phospholipase B-like 2 (EC 3.1.1.-) (66.3 kDa protein) (76 kDa protein) (p76) (LAMA-like protein 2) (Lamina ancestor homolog 2) (Phospholipase B domain-containing protein 2) [Cleaved into: Putative phospholipase B-like 2 28 kDa form; Putative phospholipase B-like 2 40 kDa form; Putative phospholipase B-like 2 15 kDa form]

 PLBL2_MOUSE             Reviewed;         594 AA.
Q3TCN2; Q3TD43; Q3TPP8; Q8BHG8; Q8BMB6; Q8BXI3; Q8C0M4; Q8R0V3;
Q9DBG4; Q9EQI9;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
28-FEB-2018, entry version 94.
RecName: Full=Putative phospholipase B-like 2;
EC=3.1.1.-;
AltName: Full=66.3 kDa protein;
AltName: Full=76 kDa protein;
Short=p76;
AltName: Full=LAMA-like protein 2;
AltName: Full=Lamina ancestor homolog 2;
AltName: Full=Phospholipase B domain-containing protein 2;
Contains:
RecName: Full=Putative phospholipase B-like 2 28 kDa form;
Contains:
RecName: Full=Putative phospholipase B-like 2 40 kDa form;
Contains:
RecName: Full=Putative phospholipase B-like 2 15 kDa form;
Flags: Precursor;
Name=Plbd2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C3H/RV;
PubMed=12080145; DOI=10.1073/pnas.142287799;
Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
Brinton M.A.;
"Positional cloning of the murine flavivirus resistance gene.";
Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD;
TISSUE=Brain cortex, Cerebellum, Liver, Testis, Thymus, and
Wolffian duct;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
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).
[4]
GLYCOSYLATION AT ASN-93; ASN-115; ASN-236; ASN-441 AND ASN-520,
SUBCELLULAR LOCATION, PROCESSING, TISSUE SPECIFICITY, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17007843; DOI=10.1016/j.febslet.2006.09.029;
Deuschl F., Kollmann K., von Figura K., Luebke T.;
"Molecular characterization of the hypothetical 66.3-kDa protein in
mouse: lysosomal targeting, glycosylation, processing and tissue
distribution.";
FEBS Lett. 580:5747-5752(2006).
[5]
SUBCELLULAR LOCATION, AND PROCESSING.
PubMed=17105447; DOI=10.1042/BJ20061205;
Jensen A.G., Chemali M., Chapel A., Kieffer-Jaquinod S., Jadot M.,
Garin J., Journet A.;
"Biochemical characterization and lysosomal localization of the
mannose-6-phosphate protein p76 (hypothetical protein LOC196463).";
Biochem. J. 402:449-458(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 47-594, GLYCOSYLATION AT
ASN-115; ASN-236; ASN-441 AND ASN-520, AND DISULFIDE BONDS.
PubMed=19237744; DOI=10.1107/S0907444908041814;
Lakomek K., Dickmanns A., Mueller U., Kollmann K., Deuschl F.,
Berndt A., Lubke T., Ficner R.;
"De novo sulfur SAD phasing of the lysosomal 66.3 kDa protein from
mouse.";
Acta Crystallogr. D 65:220-228(2009).
-!- FUNCTION: Putative phospholipase. {ECO:0000250}.
-!- SUBUNIT: Interacts with IGF2R. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:17007843,
ECO:0000269|PubMed:17105447}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3TCN2-1; Sequence=Displayed;
Name=2;
IsoId=Q3TCN2-2; Sequence=VSP_024998, VSP_024999;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Present at highest levels in spleen, lung and
brain (at protein level). {ECO:0000269|PubMed:17007843}.
-!- PTM: The p76 protein is synthesized as a 76 kDa precursor which is
then processed into a N-terminal 28 kDa form and a C-terminal 40
kDa form. The C-terminal peptide is further processed into a 15
kDa form.
-!- PTM: Glycosylated; contains mannose 6-phosphate sugars.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the phospholipase B-like family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH26395.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF217003; AAG44101.1; -; mRNA.
EMBL; AK004973; BAB23709.1; -; mRNA.
EMBL; AK030234; BAC26858.1; -; mRNA.
EMBL; AK032930; BAC28089.1; -; mRNA.
EMBL; AK042089; BAC31160.1; -; mRNA.
EMBL; AK043608; BAC31595.1; -; mRNA.
EMBL; AK046937; BAC32923.1; -; mRNA.
EMBL; AK164220; BAE37687.1; -; mRNA.
EMBL; AK170387; BAE41761.1; -; mRNA.
EMBL; AK170631; BAE41924.1; -; mRNA.
EMBL; BC026395; AAH26395.1; ALT_INIT; mRNA.
EMBL; BC038605; AAH38605.1; -; mRNA.
EMBL; BC048826; AAH48826.1; -; mRNA.
CCDS; CCDS19620.1; -. [Q3TCN2-1]
RefSeq; NP_076114.2; NM_023625.4. [Q3TCN2-1]
UniGene; Mm.100065; -.
PDB; 3FBX; X-ray; 2.40 A; A=47-594.
PDB; 3FGR; X-ray; 1.80 A; A=47-248, B=249-594.
PDB; 3FGT; X-ray; 2.40 A; A=47-248, B=249-594.
PDB; 3FGW; X-ray; 2.80 A; A=47-594.
PDBsum; 3FBX; -.
PDBsum; 3FGR; -.
PDBsum; 3FGT; -.
PDBsum; 3FGW; -.
ProteinModelPortal; Q3TCN2; -.
SMR; Q3TCN2; -.
IntAct; Q3TCN2; 2.
MINT; Q3TCN2; -.
MEROPS; C95.001; -.
iPTMnet; Q3TCN2; -.
PhosphoSitePlus; Q3TCN2; -.
EPD; Q3TCN2; -.
MaxQB; Q3TCN2; -.
PaxDb; Q3TCN2; -.
PeptideAtlas; Q3TCN2; -.
PRIDE; Q3TCN2; -.
Ensembl; ENSMUST00000031597; ENSMUSP00000031597; ENSMUSG00000029598. [Q3TCN2-1]
GeneID; 71772; -.
KEGG; mmu:71772; -.
UCSC; uc008zhh.2; mouse. [Q3TCN2-1]
UCSC; uc008zhi.2; mouse. [Q3TCN2-2]
CTD; 196463; -.
MGI; MGI:1919022; Plbd2.
eggNOG; KOG3774; Eukaryota.
eggNOG; ENOG410XQRV; LUCA.
GeneTree; ENSGT00530000063509; -.
HOVERGEN; HBG096591; -.
InParanoid; Q3TCN2; -.
OMA; KKYWFQF; -.
OrthoDB; EOG091G0G9H; -.
PhylomeDB; Q3TCN2; -.
TreeFam; TF315042; -.
ChiTaRS; Plbd2; mouse.
EvolutionaryTrace; Q3TCN2; -.
PRO; PR:Q3TCN2; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029598; -.
CleanEx; MM_1300012G16RIK; -.
Genevisible; Q3TCN2; MM.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
InterPro; IPR007000; PLipase_B-like.
PANTHER; PTHR12370; PTHR12370; 1.
Pfam; PF04916; Phospholip_B; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
Lysosome; Reference proteome; Signal.
SIGNAL 1 46
CHAIN 47 594 Putative phospholipase B-like 2.
/FTId=PRO_0000286111.
CHAIN 47 248 Putative phospholipase B-like 2 28 kDa
form.
/FTId=PRO_0000314076.
CHAIN 249 594 Putative phospholipase B-like 2 40 kDa
form.
/FTId=PRO_0000314077.
CHAIN 514 594 Putative phospholipase B-like 2 15 kDa
form.
/FTId=PRO_0000314078.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17007843}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17007843,
ECO:0000269|PubMed:19237744}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17007843,
ECO:0000269|PubMed:19237744}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17007843,
ECO:0000269|PubMed:19237744}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17007843,
ECO:0000269|PubMed:19237744}.
DISULFID 147 157 {ECO:0000269|PubMed:19237744}.
DISULFID 497 500 {ECO:0000269|PubMed:19237744}.
VAR_SEQ 436 451 FETVFNASGLQALVAQ -> VALFFHVAPSPQVCPP (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024998.
VAR_SEQ 452 594 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024999.
CONFLICT 22 22 A -> S (in Ref. 2; BAC28089).
{ECO:0000305}.
CONFLICT 91 91 W -> L (in Ref. 2; BAC28089).
{ECO:0000305}.
CONFLICT 107 107 D -> G (in Ref. 2; BAE41761).
{ECO:0000305}.
CONFLICT 173 173 R -> M (in Ref. 2; BAB23709).
{ECO:0000305}.
CONFLICT 223 223 Q -> H (in Ref. 2; BAB23709).
{ECO:0000305}.
CONFLICT 227 227 D -> Y (in Ref. 2; BAB23709).
{ECO:0000305}.
CONFLICT 230 230 D -> N (in Ref. 2; BAB23709).
{ECO:0000305}.
CONFLICT 232 232 E -> K (in Ref. 2; BAB23709).
{ECO:0000305}.
CONFLICT 315 315 D -> N (in Ref. 2; BAB23709).
{ECO:0000305}.
CONFLICT 348 348 V -> E (in Ref. 2; BAE37687).
{ECO:0000305}.
CONFLICT 381 381 N -> S (in Ref. 1; AAG44101).
{ECO:0000305}.
CONFLICT 553 553 A -> T (in Ref. 2; BAE41924).
{ECO:0000305}.
STRAND 64 72 {ECO:0000244|PDB:3FGR}.
TURN 73 76 {ECO:0000244|PDB:3FGR}.
STRAND 77 83 {ECO:0000244|PDB:3FGR}.
STRAND 88 96 {ECO:0000244|PDB:3FGR}.
HELIX 98 101 {ECO:0000244|PDB:3FGR}.
STRAND 104 110 {ECO:0000244|PDB:3FGR}.
HELIX 116 142 {ECO:0000244|PDB:3FGR}.
TURN 143 147 {ECO:0000244|PDB:3FGR}.
HELIX 154 177 {ECO:0000244|PDB:3FGR}.
HELIX 182 202 {ECO:0000244|PDB:3FGR}.
TURN 216 219 {ECO:0000244|PDB:3FGR}.
HELIX 220 223 {ECO:0000244|PDB:3FGR}.
HELIX 225 234 {ECO:0000244|PDB:3FGR}.
STRAND 250 255 {ECO:0000244|PDB:3FGR}.
HELIX 257 259 {ECO:0000244|PDB:3FGR}.
STRAND 262 267 {ECO:0000244|PDB:3FGR}.
STRAND 269 271 {ECO:0000244|PDB:3FGR}.
HELIX 272 274 {ECO:0000244|PDB:3FGR}.
STRAND 278 283 {ECO:0000244|PDB:3FGR}.
STRAND 287 291 {ECO:0000244|PDB:3FGR}.
STRAND 300 306 {ECO:0000244|PDB:3FGR}.
STRAND 317 320 {ECO:0000244|PDB:3FGR}.
STRAND 323 330 {ECO:0000244|PDB:3FGR}.
HELIX 336 341 {ECO:0000244|PDB:3FGR}.
STRAND 344 346 {ECO:0000244|PDB:3FGR}.
HELIX 350 360 {ECO:0000244|PDB:3FGR}.
HELIX 364 371 {ECO:0000244|PDB:3FGR}.
TURN 372 374 {ECO:0000244|PDB:3FGR}.
STRAND 381 387 {ECO:0000244|PDB:3FGR}.
HELIX 388 390 {ECO:0000244|PDB:3FGR}.
STRAND 399 409 {ECO:0000244|PDB:3FGR}.
STRAND 412 417 {ECO:0000244|PDB:3FGR}.
HELIX 419 425 {ECO:0000244|PDB:3FGR}.
STRAND 426 430 {ECO:0000244|PDB:3FGR}.
HELIX 437 442 {ECO:0000244|PDB:3FGR}.
HELIX 445 452 {ECO:0000244|PDB:3FGR}.
HELIX 454 456 {ECO:0000244|PDB:3FGR}.
TURN 458 460 {ECO:0000244|PDB:3FGR}.
HELIX 462 470 {ECO:0000244|PDB:3FGR}.
HELIX 471 473 {ECO:0000244|PDB:3FGR}.
HELIX 477 484 {ECO:0000244|PDB:3FGR}.
TURN 489 491 {ECO:0000244|PDB:3FGR}.
HELIX 493 495 {ECO:0000244|PDB:3FGR}.
STRAND 500 504 {ECO:0000244|PDB:3FGR}.
STRAND 508 511 {ECO:0000244|PDB:3FGR}.
HELIX 514 516 {ECO:0000244|PDB:3FGR}.
HELIX 526 528 {ECO:0000244|PDB:3FGR}.
STRAND 532 535 {ECO:0000244|PDB:3FGR}.
STRAND 537 541 {ECO:0000244|PDB:3FGR}.
HELIX 543 547 {ECO:0000244|PDB:3FGR}.
STRAND 551 557 {ECO:0000244|PDB:3FGR}.
STRAND 560 562 {ECO:0000244|PDB:3FGR}.
HELIX 567 569 {ECO:0000244|PDB:3FGR}.
TURN 571 574 {ECO:0000244|PDB:3FGR}.
STRAND 582 584 {ECO:0000244|PDB:3FGR}.
STRAND 589 591 {ECO:0000244|PDB:3FGR}.
SEQUENCE 594 AA; 66289 MW; 202556A56C1AD0BA CRC64;
MAAPVDGSSG GWAARALRRA LALTSLTTLA LLASLTGLLL SGPAGALPTL GPGWQRQNPD
PPVSRTRSLL LDAASGQLRL EDGFHPDAVA WANLTNAIRE TGWAYLDLST NGRYNDSLQA
YAAGVVEASV SEELIYMHWM NTVVNYCGPF EYEVGYCEKL KNFLEANLEW MQREMELNPD
SPYWHQVRLT LLQLKGLEDS YEGRLTFPTG RFTIKPLGFL LLQISGDLED LEPALNKTNT
KPSLGSGSCS ALIKLLPGGH DLLVAHNTWN SYQNMLRIIK KYRLQFREGP QEEYPLVAGN
NLVFSSYPGT IFSGDDFYIL GSGLVTLETT IGNKNPALWK YVQPQGCVLE WIRNVVANRL
ALDGATWADV FKRFNSGTYN NQWMIVDYKA FLPNGPSPGS RVLTILEQIP GMVVVADKTA
ELYKTTYWAS YNIPYFETVF NASGLQALVA QYGDWFSYTK NPRAKIFQRD QSLVEDMDAM
VRLMRYNDFL HDPLSLCEAC NPKPNAENAI SARSDLNPAN GSYPFQALHQ RAHGGIDVKV
TSFTLAKYMS MLAASGPTWD QCPPFQWSKS PFHSMLHMGQ PDLWMFSPIR VPWD


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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