Reviewed, UniProtKB/Swiss-Prot Q8NHP8 (PLBL2_HUMAN)

Names and origin

Protein names

Recommended name:
    Putative phospholipase B-like 2
    EC=3.1.1.-
Alternative name(s):
    Phospholipase B domain-containing protein 2
    Lamina ancestor homolog 2
    LAMA-like protein 2
    76 kDa protein
    p76
Cleaved into the following 2 chains:
    1- Recommended name:
            Putative phospholipase B-like 2 32 kDa form
    2- Recommended name:
            Putative phospholipase B-like 2 45 kDa form

Gene names

Name:

PLBD2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Putative phospholipase By similarity.
Subunit structure	Interacts with IGF2R. Ref.3
Subcellular location	Lysosome lumen. Ref.3
Tissue specificity	Ubiquitously expressed, with highest levels in heart, brain and liver. Ref.3
Post-translational modification	The p76 protein is synthesized as a 80 kDa precursor which is then processed into a N-terminal 32 kDa form and a C-terminal 45 kDa form. Glycosylated; contains mannose 6-phosphate sugars. Ref.3
Sequence similarities	Belongs to the phospholipase B-like family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	lysosomal lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 41	41	Ref.3
	Chain	42 – 589	548	Putative phospholipase B-like 2		PRO_0000286110
	Chain	42 – 243	202	Putative phospholipase B-like 2 32 kDa form		PRO_0000314074
	Chain	244 – 589	346	Putative phospholipase B-like 2 45 kDa form		PRO_0000314075
Amino acid modifications
	Glycosylation	88	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	110	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	231	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	436	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	465	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	515	1	N-linked (GlcNAc...) Ref.3
Natural variations
	Natural variant	524	1	R → C: dbSNP rs12425042.		VAR_032075
Experimental info
	Sequence conflict	521	1	Q → K in AAH30618. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8NHP8-1 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: D0D1BACCFBF756BB	FASTA	589	65,472
	10 20 30 40 50 60 MVGQMYCYPG SHLARALTRA LALALVLALL VGPFLSGLAG AIPAPGGRWA RDGQVPPASR 70 80 90 100 110 120 SRSVLLDVSA GQLLMVDGRH PDAVAWANLT NAIRETGWAF LELGTSGQYN DSLQAYAAGV 130 140 150 160 170 180 VEAAVSEELI YMHWMNTVVN YCGPFEYEVG YCERLKSFLE ANLEWMQEEM ESNPDSPYWH 190 200 210 220 230 240 QVRLTLLQLK GLEDSYEGRV SFPAGKFTIK PLGFLLLQLS GDLEDLELAL NKTKIKPSLG 250 260 270 280 290 300 SGSCSALIKL LPGQSDLLVA HNTWNNYQHM LRVIKKYWLQ FREGPWGDYP LVPGNKLVFS 310 320 330 340 350 360 SYPGTIFSCD DFYILGSGLV TLETTIGNKN PALWKYVRPR GCVLEWVRNI VANRLASDGA 370 380 390 400 410 420 TWADIFKRFN SGTYNNQWMI VDYKAFIPGG PSPGSRVLTI LEQIPGMVVV ADKTSELYQK 430 440 450 460 470 480 TYWASYNIPS FETVFNASGL QALVAQYGDW FSYDGSPRAQ IFRRNQSLVQ DMDSMVRLMR 490 500 510 520 530 540 YNDFLHDPLS LCKACNPQPN GENAISARSD LNPANGSYPF QALRQRSHGG IDVKVTSMSL 550 560 570 580 ARILSLLAAS GPTWDQVPPF QWSTSPFSGL LHMGQPDLWK FAPVKVSWD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]. Tissue: Testis.
[3]	"Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463)." Jensen A.G., Chemali M., Chapel A., Kieffer-Jaquinod S., Jadot M., Garin J., Journet A. Biochem. J. 402:449-458(2007) [PubMed: 17105447] [Abstract] Cited for: PROTEIN SEQUENCE OF 42-49 AND 244-250, GLYCOSYLATION AT ASN-88; ASN-110; ASN-231; ASN-436; ASN-465 AND ASN-515, INTERACTION WITH IGF2R, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-465, MASS SPECTROMETRY. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC010178 Genomic DNA. No translation available. BC030618 mRNA. Translation: AAH30618.1.
IPI	IPI00169285.
RefSeq	NP_775813.1.
UniGene	Hs.115896
3D structure databases
ModBase	Search...
Proteomic databases
PeptideAtlas	Q8NHP8.
PRIDE	Q8NHP8.
Genome annotation databases
Ensembl	ENSG00000151176. Homo sapiens. [Contig view]
GeneID	196463.
KEGG	hsa:196463.
Organism-specific databases
GeneCards	GC12P112280.
HGNC	HGNC:27283. PLBD2.
HPA	HPA017163.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q8NHP8.
OMA	Q8NHP8. RYNDFLH.
Gene expression databases
ArrayExpress	Q8NHP8.
Bgee	Q8NHP8.
Family and domain databases
InterPro	IPR007000. Phospholipase_B-like. [Graphical view]
PANTHER	PTHR12370. Laminin_A. 1 hit.
Pfam	PF04916. Phospholip_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	89484.

Entry information

Entry name

PLBL2_HUMAN

Accession

Primary (citable) accession number: Q8NHP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	March 3, 2009
Last modified:	June 16, 2009
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)