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Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

PAFAH1B2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit.

Catalytic activityi

1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei48By similarity1
Active sitei193By similarity1
Active sitei196By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.47 908
ReactomeiR-BTA-6798695 Neutrophil degranulation
R-BTA-6811436 COPI-independent Golgi-to-ER retrograde traffic

Chemistry databases

SwissLipidsiSLP:000000692

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-activating factor acetylhydrolase IB subunit beta (EC:3.1.1.47)
Alternative name(s):
PAF acetylhydrolase 30 kDa subunit
Short name:
PAF-AH 30 kDa subunit
PAF-AH subunit beta
Short name:
PAFAH subunit beta
Gene namesi
Name:PAFAH1B2
Synonyms:PAFAHB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Organism-specific databases

VGNCiVGNC:32550 PAFAH1B2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000581492 – 229Platelet-activating factor acetylhydrolase IB subunit betaAdd BLAST228

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei64PhosphoserineBy similarity1
Modified residuei220PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP68401
PeptideAtlasiP68401
PRIDEiP68401

Expressioni

Gene expression databases

BgeeiENSBTAG00000005627
ExpressionAtlasiP68401 baseline and differential

Interactioni

Subunit structurei

Cytosolic PAF-AH IB is formed of three subunits of 45 kDa (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of the enzyme resides in the beta and gamma subunits, whereas the alpha subunit has regulatory activity. Trimer formation is not essential for the catalytic activity.

Protein-protein interaction databases

IntActiP68401, 1 interactor
MINTiP68401
STRINGi9913.ENSBTAP00000007398

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Beta strandi18 – 21Combined sources4
Helixi23 – 37Combined sources15
Beta strandi41 – 47Combined sources7
Helixi48 – 51Combined sources4
Helixi52 – 55Combined sources4
Helixi57 – 62Combined sources6
Helixi64 – 66Combined sources3
Beta strandi68 – 72Combined sources5
Helixi78 – 86Combined sources9
Turni87 – 90Combined sources4
Beta strandi96 – 101Combined sources6
Helixi111 – 128Combined sources18
Beta strandi133 – 137Combined sources5
Beta strandi143 – 145Combined sources3
Helixi148 – 163Combined sources16
Beta strandi164 – 173Combined sources10
Turni188 – 190Combined sources3
Beta strandi194 – 197Combined sources4
Helixi199 – 216Combined sources18

3D structure databases

ProteinModelPortaliP68401
SMRiP68401
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68401

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IMK6 Eukaryota
ENOG410XPWQ LUCA
GeneTreeiENSGT00390000016520
HOGENOMiHOG000232143
HOVERGENiHBG053477
InParanoidiP68401
KOiK16795
OMAiRGQQPNK
OrthoDBiEOG091G0OII
TreeFamiTF323955

Family and domain databases

Gene3Di3.40.50.1110, 1 hit
InterProiView protein in InterPro
IPR013830 SGNH_hydro
IPR036514 SGNH_hydro_sf
PfamiView protein in Pfam
PF13472 Lipase_GDSL_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P68401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV
60 70 80 90 100
QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV
110 120 130 140 150
WVGTNNHENT AEEVAGGIEA IVQLINTRQP QAKIIVLGLL PRGEKPNPLR
160 170 180 190 200
QKNAKVNQLL KVSLPKLANV QLLDTDGGFV HSDGAISCHD MFDFLHLTGG
210 220
GYAKICKPLH ELIMQLLEET PEEKQTTIA
Length:229
Mass (Da):25,569
Last modified:November 23, 2004 - v1
Checksum:i14CF5D48621AA504
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49678 mRNA Translation: BAA08534.1
BC103452 mRNA Translation: AAI03453.1
RefSeqiNP_777089.1, NM_174664.2
UniGeneiBt.49728

Genome annotation databases

EnsembliENSBTAT00000007398; ENSBTAP00000007398; ENSBTAG00000005627
GeneIDi282514
KEGGibta:282514

Similar proteinsi

Entry informationi

Entry nameiPA1B2_BOVIN
AccessioniPrimary (citable) accession number: P68401
Secondary accession number(s): O00687, Q29459, Q3ZBB8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: May 23, 2018
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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