Primary Information |
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| BoMiProt ID | Bomi8308 |
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| Protein Name | Protein 4.1/P4.1/4.1R/Band 4.1/Erythrocyte membrane protein band 4.1 |
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| Organism | Bos taurus |
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| Uniprot ID | Q9N179 |
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| Milk Fraction | whey |
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| Ref Sequence ID | NP_776736.1 |
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| Aminoacid Length | 617 |
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| Molecular Weight | 69258 |
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| FASTA Sequence |
Download |
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| Gene Name | EPB41/E41P |
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| Gene ID | 281753 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Protein Function | Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes |
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| Biochemical Properties | Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate with contractile apparatus and tight junctions. |
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| PTMs | Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q9N179|EPB41_BOVIN Protein 4.1 OS=Bos taurus OX=9913 GN=EPB41 PE=2 SV=1
MHCKVSLLDDTVY*13ECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAK
EIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVSGRLPCSFATLALLG
SYTIQSELGDYDPELHGADYVSDFKLAPNQTKELEEKVMELHKSYRSMT*169PAQADLEFLEN
AKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKEKLRINRFPWPKVLKISYKRSSFFI
KIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRY
SGRTQAQTRQAS*312ALIDRPAPHFERTASKRAS*331RS*333LDGAAAVEPADRTPRPTSAPAIAPSPA
AEGGVPGAPVKKAQKETVQVEVKQEEAPPEDAEPEPSEAWKKKRERLDGENIY*413IRHS*417NLM
LEDLDKS*427QEEIKKHHAS*437ISELKKNFMESVPEPRPSEWDKRLS*462THS*465PFRTLNINGQIPTGEGPPLVKTQT*489VTISDTANAVKSEIPTKDVPIVHTETKTITYEAAQTDDSNGDLDPGVLLTA
QTITSETTSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPD
MSVTKVVVHQET*612EISEE
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| Predicted Disorder Regions | 346-401, 448-465, 495-551, 577-617 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Phosphorylation on Tyr-413 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex. |
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| Bibliography | Baines, A. J., Bennett, P. M., Carter, E. W., & Terracciano, C. (2009). Protein 4.1 and the control of ion channels. Blood cells, molecules & diseases, 42(3), 211–215. https://doi.org/10.1016/j.bcmd.2009.01.016 |
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