Search by BoMiProt ID - Bomi8057


Primary Information

BoMiProt ID Bomi8057
Protein Name Platelet-activating factor acetylhydrolase IB subunit beta/Lissencephaly-1 protein( LIS-1)/PAF acetylhydrolase 45 kDa subunit/PAF-AH alpha
Organism Bos taurus
Uniprot IdP43033
Milk FractionWhey
Ref Sequence Id NP_777088.1
Aminoacid Length 410
Molecular Weight 46613
Fasta Sequence https://www.uniprot.org/uniprot/P43033.fasta
Gene Name PAFAH1B1/LIS1/PAFAHA
Gene Id 282513
Protein Existence Status reviewed

Secondary Information

Protein Function Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase,an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in the PAF inactivation. essential regulator of dynein-mediated motility, as well as mitosis, nuclear positioning, and microtubule organization.
Biochemical Properties beta subunit is imp for catalytic activity.
Significance in milk related to fertility
PTMs Acetylation and phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P43033|LIS1_BOVIN Platelet-activating factor acetylhydrolase IB subunit beta OS=Bos taurus OX=9913 GN=PAFAH1B1 PE=1 SV=2 MVLSQRQRDELNRAIADYLRSNGYEAAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIR LQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRS*109PVTRVIFHPVF SVMVSASEDATIKVWDYETGDFERTLKGHTDSVEDISFDHSGKLLASCSADMTIKLWDFQ GFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSE TKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDK TLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
Predicted Disorder Regions 79-86, 296-307
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs phosphorylated on serine residues by a kinase associated with microtubules,probably affecting its catalytic function.
Bibliography Sapir T, Cahana A, Seger R, Nekhai S, Reiner O. LIS1 is a microtubule-associated phosphoprotein. Eur J Biochem. 1999 Oct 1;265(1):181-8. doi: 10.1046/j.1432-1327.1999.00711.x. PMID: 10491172.