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Q8VCI0 (PLBL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase B-like 1
EC=3.1.1.-
Alternative name(s):
LAMA-like protein 1
Lamina ancestor homolog 1
Phospholipase B domain-containing protein 1
Gene names
Name:Plbd1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phospholipase acting on various phospholipids including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids. May have a role in the defense against invading microorganisms and in the generation of lipid mediators of inflammation By similarity.

Subunit structure

May exist as a non-covalently associated tetramer of two 22 kDa and two 42 kDa chains By similarity.

Subcellular location

Cytoplasmic granule By similarity. Secreted By similarity.

Post-translational modification

Proteolytic processing leading to a 22 kDa N-terminal and a 42 kDa C-terminal fragment appears necessary for activity, which seems to derive from the 42 kDa chain By similarity.

Sequence similarities

Belongs to the phospholipase B-like family.

Sequence caution

The sequence BAE42780.1 differs from that shown. Reason: Frameshift at position 51.

Ontologies

Keywords
   Biological processImmunity
Lipid degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 550519Phospholipase B-like 1
PRO_0000286107

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) (high mannose) Ref.3

Experimental info

Sequence conflict1271I → F in BAB22618. Ref.1
Sequence conflict5281E → D in BAB22618. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VCI0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C89FC31C0D14B5F6

FASTA55062,998
        10         20         30         40         50         60 
MCHRSPGRSL RPPSPLLLLL PLLLQPPWAA GAASQSDPTG VHCATAYWSP ESKKVEIKTV 

        70         80         90        100        110        120 
LDKNGDAYGY YNDSIKTTGW GILEIRAGYG SQVLSNEIIM FLAGYLEGYL TALHMYDHFT 

       130        140        150        160        170        180 
NLYPQLIKNP SIVKKVQDFM EKQEMWTRQN IKAQKDDPFW RHTGYVVTQL DGLYLGAQKR 

       190        200        210        220        230        240 
ASEEKIKPMT MFQIQFLNAV GDLLDLIPSL SPTKSSSMMK FKIWEMGHCS ALIKVLPGFE 

       250        260        270        280        290        300 
NIYFAHSSWY TYAAMLRIYK HWDFNIKDKY TLSKRLSFSS YPGFLESLDD FYILSSGLIL 

       310        320        330        340        350        360 
LQTTNSVYNK TLLKQVVPKT LLAWQRVRVA NMMAEGGKEW AQIFSKHNSG TYNNQYMVLD 

       370        380        390        400        410        420 
LKKVTINRSL DKGTLYIVEQ IPTYVEYSDQ TNVLRKGYWA SYNIPFHKTI YNWSGYPLLV 

       430        440        450        460        470        480 
HKLGLDYSYD LAPRAKIFRR DQGNVTDMAS MKYIMRYNNY KEDPYSKGDP CSTICCREDL 

       490        500        510        520        530        540 
NGASPSPGGC YDTKVADIFL ASQYKAYAIS GPTVQDGLPP FNWNRFNETL HRGMPEVFDF 

       550 
NFVTMKPILS

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Spleen.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[3]"High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed: 16170054] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-72, MASS SPECTROMETRY.
Tissue: Epidermis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK003169 mRNA. Translation: BAB22618.1.
AK172021 mRNA. Translation: BAE42780.1. Frameshift.
BC019793 mRNA. Translation: AAH19793.1.
IPIIPI00471081.
RefSeqNP_080082.1. NM_025806.2.
UniGeneMm.3311.

3D structure databases

ProteinModelPortalQ8VCI0.
SMRQ8VCI0. Positions 38-546.
ModBaseSearch...

PTM databases

PhosphoSiteQ8VCI0.

Proteomic databases

PRIDEQ8VCI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032336; ENSMUSP00000032336; ENSMUSG00000030214.
GeneID66857.
KEGGmmu:66857.
UCSCuc009elz.2. mouse.

Organism-specific databases

CTD79887.
MGIMGI:1914107. Plbd1.

Phylogenomic databases

eggNOGroNOG12945.
GeneTreeENSGT00530000063509.
HOGENOMHBG443824.
HOVERGENHBG108264.
InParanoidQ8VCI0.
OrthoDBEOG49S663.

Gene expression databases

ArrayExpressQ8VCI0.
BgeeQ8VCI0.
CleanExMM_1100001H23RIK.
GenevestigatorQ8VCI0.

Family and domain databases

InterProIPR007000. PLipase_B-like.
[Graphical view]
PANTHERPTHR12370. Laminin_A. 1 hit.
PfamPF04916. Phospholip_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio322835.
SOURCESearch...

Entry information

Entry namePLBL1_MOUSE
AccessionPrimary (citable) accession number: Q8VCI0
Secondary accession number(s): Q3TA89, Q9D1S0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2002
Last modified: November 16, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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