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Protein

Phospholipase B-like 1

Gene

PLBD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In view of the small size of the putative binding pocket, it has been proposed that it may act as an amidase or a peptidase (By similarity). Exhibits a weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids.By similarity1 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.5. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.
R-HSA-1483115. Hydrolysis of LPC.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following 3 chains:
Gene namesi
Name:PLBD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26215. PLBD1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular space Source: UniProtKB
  • lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164724597.

Polymorphism and mutation databases

BioMutaiPLBD1.
DMDMi269849630.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence analysisAdd
BLAST
Chaini39 – 553515Phospholipase B-like 1PRO_0000286106Add
BLAST
Chaini39 – 208170Phospholipase B-like 1 chain APRO_0000425421Add
BLAST
Chaini93 – 208116Phospholipase B-like 1 chain CPRO_0000425422Add
BLAST
Propeptidei209 – 22719Removed in mature formBy similarityPRO_0000425423Add
BLAST
Chaini228 – 553326Phospholipase B-like 1 chain BPRO_0000425424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi71 – 711N-linked (GlcNAc...) (high mannose or hybrid)By similarity
Glycosylationi308 – 3081N-linked (GlcNAc...) (high mannose or hybrid)By similarity
Glycosylationi366 – 3661N-linked (GlcNAc...) (high mannose or hybrid)By similarity
Glycosylationi411 – 4111N-linked (GlcNAc...)1 Publication
Disulfide bondi470 ↔ 475By similarity
Disulfide bondi474 ↔ 489By similarity
Glycosylationi526 – 5261N-linked (GlcNAc...) (high mannose or hybrid)By similarity

Post-translational modificationi

The maturation cleavages that produces chains A and B are required to open the putative substrate binding pocket. Both chains A and B remain associated in the mature protein.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ6P4A8.
PaxDbiQ6P4A8.
PRIDEiQ6P4A8.

PTM databases

iPTMnetiQ6P4A8.
PhosphoSiteiQ6P4A8.

Expressioni

Tissue specificityi

Expressed in neutrophils and monocytes.1 Publication

Gene expression databases

BgeeiQ6P4A8.
ExpressionAtlasiQ6P4A8. baseline and differential.
GenevisibleiQ6P4A8. HS.

Organism-specific databases

HPAiHPA040303.

Interactioni

Subunit structurei

May form a homodimer, each monomer is composed of a chain A and a chain B.1 Publication

Protein-protein interaction databases

BioGridi122972. 13 interactions.
IntActiQ6P4A8. 2 interactions.
STRINGi9606.ENSP00000240617.

Structurei

3D structure databases

ProteinModelPortaliQ6P4A8.
SMRiQ6P4A8. Positions 39-208, 229-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase B-like family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3774. Eukaryota.
ENOG410XQRV. LUCA.
GeneTreeiENSGT00530000063509.
HOGENOMiHOG000006903.
HOVERGENiHBG108264.
InParanoidiQ6P4A8.
OMAiCCREDLN.
OrthoDBiEOG7D2FD5.
PhylomeDBiQ6P4A8.
TreeFamiTF315042.

Family and domain databases

InterProiIPR007000. PLipase_B-like.
[Graphical view]
PANTHERiPTHR12370. PTHR12370. 1 hit.
PfamiPF04916. Phospholip_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6P4A8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRGGPGGRP GLPQPPPLLL LLLLLPLLLV TAEPPKPAGV YYATAYWMPA
60 70 80 90 100
EKTVQVKNVM DKNGDAYGFY NNSVKTTGWG ILEIRAGYGS QTLSNEIIMF
110 120 130 140 150
VAGFLEGYLT APHMNDHYTN LYPQLITKPS IMDKVQDFME KQDKWTRKNI
160 170 180 190 200
KEYKTDSFWR HTGYVMAQID GLYVGAKKRA ILEGTKPMTL FQIQFLNSVG
210 220 230 240 250
DLLDLIPSLS PTKNGSLKVF KRWDMGHCSA LIKVLPGFEN ILFAHSSWYT
260 270 280 290 300
YAAMLRIYKH WDFNVIDKDT SSSRLSFSSY PGFLESLDDF YILSSGLILL
310 320 330 340 350
QTTNSVFNKT LLKQVIPETL LSWQRVRVAN MMADSGKRWA DIFSKYNSGT
360 370 380 390 400
YNNQYMVLDL KKVKLNHSLD KGTLYIVEQI PTYVEYSEQT DVLRKGYWPS
410 420 430 440 450
YNVPFHEKIY NWSGYPLLVQ KLGLDYSYDL APRAKIFRRD QGKVTDTASM
460 470 480 490 500
KYIMRYNNYK KDPYSRGDPC NTICCREDLN SPNPSPGGCY DTKVADIYLA
510 520 530 540 550
SQYTSYAISG PTVQGGLPVF RWDRFNKTLH QGMPEVYNFD FITMKPILKL

DIK
Length:553
Mass (Da):63,255
Last modified:November 24, 2009 - v2
Checksum:iB4258DD2E1A16FE0
GO

Sequence cautioni

The sequence AAH00909.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15442.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181Missing in BAF83603 (PubMed:14702039).Curated
Sequence conflicti18 – 181Missing in AAH63561 (PubMed:15489334).Curated
Sequence conflicti241 – 2411I → V in BAB15442 (PubMed:15489334).Curated
Sequence conflicti302 – 3021T → A in BAF83603 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti265 – 2651V → I.2 Publications
Corresponds to variant rs7957558 [ dbSNP | Ensembl ].
VAR_032072
Natural varianti377 – 3771V → A.
Corresponds to variant rs2287541 [ dbSNP | Ensembl ].
VAR_032073
Natural varianti534 – 5341P → A.1 Publication
Corresponds to variant rs1600 [ dbSNP | Ensembl ].
VAR_032074

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026315 mRNA. Translation: BAB15442.1. Different initiation.
AK290914 mRNA. Translation: BAF83603.1.
AC008114 Genomic DNA. No translation available.
BC000909 mRNA. Translation: AAH00909.2. Different initiation.
BC063561 mRNA. Translation: AAH63561.1.
CCDSiCCDS31751.1.
RefSeqiNP_079105.4. NM_024829.5.
UniGeneiHs.131933.

Genome annotation databases

EnsembliENST00000240617; ENSP00000240617; ENSG00000121316.
GeneIDi79887.
KEGGihsa:79887.
UCSCiuc001rcc.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK026315 mRNA. Translation: BAB15442.1. Different initiation.
AK290914 mRNA. Translation: BAF83603.1.
AC008114 Genomic DNA. No translation available.
BC000909 mRNA. Translation: AAH00909.2. Different initiation.
BC063561 mRNA. Translation: AAH63561.1.
CCDSiCCDS31751.1.
RefSeqiNP_079105.4. NM_024829.5.
UniGeneiHs.131933.

3D structure databases

ProteinModelPortaliQ6P4A8.
SMRiQ6P4A8. Positions 39-208, 229-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122972. 13 interactions.
IntActiQ6P4A8. 2 interactions.
STRINGi9606.ENSP00000240617.

PTM databases

iPTMnetiQ6P4A8.
PhosphoSiteiQ6P4A8.

Polymorphism and mutation databases

BioMutaiPLBD1.
DMDMi269849630.

Proteomic databases

MaxQBiQ6P4A8.
PaxDbiQ6P4A8.
PRIDEiQ6P4A8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000240617; ENSP00000240617; ENSG00000121316.
GeneIDi79887.
KEGGihsa:79887.
UCSCiuc001rcc.2. human.

Organism-specific databases

CTDi79887.
GeneCardsiPLBD1.
H-InvDBHIX0010454.
HGNCiHGNC:26215. PLBD1.
HPAiHPA040303.
neXtProtiNX_Q6P4A8.
PharmGKBiPA164724597.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3774. Eukaryota.
ENOG410XQRV. LUCA.
GeneTreeiENSGT00530000063509.
HOGENOMiHOG000006903.
HOVERGENiHBG108264.
InParanoidiQ6P4A8.
OMAiCCREDLN.
OrthoDBiEOG7D2FD5.
PhylomeDBiQ6P4A8.
TreeFamiTF315042.

Enzyme and pathway databases

BRENDAi3.1.1.5. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482922. Acyl chain remodelling of PI.
R-HSA-1483115. Hydrolysis of LPC.

Miscellaneous databases

GenomeRNAii79887.
NextBioi69699.
PROiQ6P4A8.

Gene expression databases

BgeeiQ6P4A8.
ExpressionAtlasiQ6P4A8. baseline and differential.
GenevisibleiQ6P4A8. HS.

Family and domain databases

InterProiIPR007000. PLipase_B-like.
[Graphical view]
PANTHERiPTHR12370. PTHR12370. 1 hit.
PfamiPF04916. Phospholip_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-265.
    Tissue: Neutrophil and Small intestine.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ILE-265 AND ALA-534.
    Tissue: Placenta.
  4. "The identification of a phospholipase B precursor in human neutrophils."
    Xu S., Zhao L., Larsson A., Venge P.
    FEBS J. 276:175-186(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Granulocyte.
  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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411.
    Tissue: Liver.

Entry informationi

Entry nameiPLBL1_HUMAN
AccessioniPrimary (citable) accession number: Q6P4A8
Secondary accession number(s): A8K4E9, Q9BVV3, Q9H625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: November 24, 2009
Last modified: March 16, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.