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Protein

Platelet-activating factor acetylhydrolase IB subunit gamma

Gene

PAFAH1B3

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. Plays an important role during the development of brain.

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 sitei47Combined sources1 Publication1
Active sitei192Combined sources1 Publication1
Active sitei195Combined sources1 Publication1

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-6811436 COPI-independent Golgi-to-ER retrograde traffic

Chemistry databases

SwissLipidsiSLP:000000693

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-activating factor acetylhydrolase IB subunit gamma (EC:3.1.1.47)
Alternative name(s):
PAF acetylhydrolase 29 kDa subunit
Short name:
PAF-AH 29 kDa subunit
PAF-AH subunit gamma
Short name:
PAFAH subunit gamma
Gene namesi
Name:PAFAH1B3
Synonyms:PAFAHG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

Organism-specific databases

VGNCiVGNC:32551 PAFAH1B3

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000581542 – 232Platelet-activating factor acetylhydrolase IB subunit gammaAdd BLAST231

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ29460
PeptideAtlasiQ29460
PRIDEiQ29460

Expressioni

Gene expression databases

BgeeiENSBTAG00000019787

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.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ29460, 1 interactor
MINTiQ29460
STRINGi9913.ENSBTAP00000026366

Structurei

Secondary structure

1232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Beta strandi17 – 20Combined sources4
Helixi22 – 36Combined sources15
Beta strandi40 – 46Combined sources7
Helixi47 – 50Combined sources4
Helixi52 – 55Combined sources4
Helixi58 – 61Combined sources4
Helixi63 – 65Combined sources3
Beta strandi67 – 71Combined sources5
Helixi77 – 85Combined sources9
Turni86 – 91Combined sources6
Beta strandi95 – 100Combined sources6
Helixi110 – 127Combined sources18
Beta strandi132 – 136Combined sources5
Beta strandi142 – 144Combined sources3
Helixi147 – 164Combined sources18
Beta strandi169 – 172Combined sources4
Turni187 – 189Combined sources3
Beta strandi193 – 196Combined sources4
Helixi198 – 215Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BWPX-ray2.10A1-232[»]
1BWQX-ray2.30A1-232[»]
1BWRX-ray2.40A1-232[»]
1ES9X-ray1.30A1-232[»]
1FXWX-ray2.10A1-232[»]
1WABX-ray1.70A1-232[»]
3DT6X-ray2.10A1-232[»]
3DT8X-ray1.85A1-232[»]
3DT9X-ray1.85A1-232[»]
ProteinModelPortaliQ29460
SMRiQ29460
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29460

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IMK6 Eukaryota
ENOG410XPWQ LUCA
GeneTreeiENSGT00390000016520
HOGENOMiHOG000232143
HOVERGENiHBG053477
InParanoidiQ29460
KOiK16795
OMAiHQDMYDY
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.

Q29460-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ
60 70 80 90 100
LMHQCEIWRE LFSPLHALNF GIGGDSTQHV LWRLENGELE HIRPKIVVVW
110 120 130 140 150
VGTNNHGHTA EQVTGGIKAI VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE
160 170 180 190 200
KNRRVNELVR AALAGHPRAH FLDADPGFVH SDGTISHHDM YDYLHLSRLG
210 220 230
YTPVCRALHS LLLRLLTQDQ GQGGAPLPEP SP
Length:232
Mass (Da):25,865
Last modified:November 1, 1996 - v1
Checksum:i81C2CECA8E2204ED
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti79Missing AA sequence (PubMed:8083218).Curated1
Sequence conflicti150E → L AA sequence (PubMed:8083218).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30789 mRNA Translation: BAA06455.1
BC120202 mRNA Translation: AAI20203.1
PIRiA54754
RefSeqiNP_777090.1, NM_174665.2
UniGeneiBt.4040

Genome annotation databases

EnsembliENSBTAT00000026366; ENSBTAP00000026366; ENSBTAG00000019787
GeneIDi282515
KEGGibta:282515

Similar proteinsi

Entry informationi

Entry nameiPA1B3_BOVIN
AccessioniPrimary (citable) accession number: Q29460
Secondary accession number(s): Q0VCF0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 128 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
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Main funding by: National Institutes of Health