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Protein

55 kDa erythrocyte membrane protein

Gene

Mpp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity.1 Publication

GO - Biological processi

  • regulation of neutrophil chemotaxis Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
55 kDa erythrocyte membrane protein
Short name:
p55
Alternative name(s):
Membrane protein, palmitoylated 1
Gene namesi
Name:Mpp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:105941. Mpp1.

Subcellular locationi

GO - Cellular componenti

  • cortical cytoskeleton Source: MGI
  • intracellular Source: MGI
  • membrane Source: MGI
  • stereocilium Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Neutrophils form multiple transient pseudopods upon chemotactic stimulation, and do not migrate efficiently in vitro.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000945662 – 46655 kDa erythrocyte membrane proteinAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei49PhosphothreonineBy similarity1
Modified residuei52PhosphoserineCombined sources1
Modified residuei57PhosphoserineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Modified residuei243PhosphoserineBy similarity1

Post-translational modificationi

Extensively palmitoylated by ZDHHC17, palmitoylation is essential for membrane organization and is crucial for proper erythrocytes morphology.By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP70290.
PaxDbiP70290.
PeptideAtlasiP70290.
PRIDEiP70290.

PTM databases

iPTMnetiP70290.
PhosphoSitePlusiP70290.
SwissPalmiP70290.

Expressioni

Tissue specificityi

Abundantly expressed in the erythrocytes (at protein level).1 Publication

Developmental stagei

During development of the retina, expression is highest in the inner, neuroblastic layer, while at later stages it is also present in the photoreceptor cell layer. Detected in the eye from E14.5 onwards. Highly expressed in the liver and primitive gut, and at lower levels in the umbilical vein, the ventricular layer of the CNS and upper/lower jaw region. At E14.5 and E16.5, expression in the liver and stomach is maintained. In addition, expression is present in bone structures (e.g. zygomatic bone, lower jawbone), cranial nerve ganglia [e.g. trigeminal (V) ganglion] and cochlea. The expression in the eye is seen in the neuroblastic layer. At E16.5 and E18.5, a slightly higher expression is seen in the neuroblastic layer. At E16.5, strong expression in the upper part of the gut is maintained and with the onset of ossification, expression is seen in all bone structures of the body. At P7 and P90, expression in the eye is seen in the ganglion cell layer, the inner nuclear layer (INL) and photoreceptor cell layer.1 Publication

Gene expression databases

BgeeiENSMUSG00000031402.
CleanExiMM_MPP1.
ExpressionAtlasiP70290. baseline and differential.
GenevisibleiP70290. MM.

Interactioni

Subunit structurei

Heterodimer with MPP5. Interacts with DLG5 and NF2. Interacts (via guanylate kinase-like domain) with WHRN (via third PDZ domain).2 Publications

Protein-protein interaction databases

DIPiDIP-61219N.
IntActiP70290. 3 interactors.
MINTiMINT-4094335.
STRINGi10090.ENSMUSP00000033775.

Structurei

3D structure databases

ProteinModelPortaliP70290.
SMRiP70290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 152PDZPROSITE-ProRule annotationAdd BLAST82
Domaini158 – 228SH3PROSITE-ProRule annotationAdd BLAST71
Domaini282 – 451Guanylate kinase-likePROSITE-ProRule annotationAdd BLAST170

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni268 – 466Interaction with MPP5By similarityAdd BLAST199

Sequence similaritiesi

Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiKOG0609. Eukaryota.
COG0194. LUCA.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000233034.
HOVERGENiHBG001858.
InParanoidiP70290.
OMAiIPNQQSR.
OrthoDBiEOG091G065I.
PhylomeDBiP70290.
TreeFamiTF314263.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P70290-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLKSSEGEG GNSMRTALSD LYLEHLLQKR NRPETSLNQS NVTTEDMYTN
60 70 80 90 100
GSPAPGSPAH AKGQEARRVR LIQFEKITEE PMGITLKLNE KQSCTVARIL
110 120 130 140 150
HGGMIHRQGS LHVGDEILEI NGTNVTNHSV DQLQKAMKET KGMISLKVIA
160 170 180 190 200
NQQSRLPALQ MFMRAQFDYD PQKDNLIPCK EAGLKFVTGD IIQIINKDDS
210 220 230 240 250
NWWQGRVEGS SKESAGLIPS PELQEWRVAS VAHSAPSEAP SCSPFGKKKK
260 270 280 290 300
CKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN
310 320 330 340 350
GLLSHNPEKF AYPAPYTTRP PKKSEEDGKE YHFISTEEMT KNISANEFLE
360 370 380 390 400
FGSYQGNMFG TKFETVHQIH KQDKIAILDI EPQTLKTVRT AELSPFIVFI
410 420 430 440 450
APTDQGTQTE ALQQLQKDSE AIRSQYAHYF DLSLVNNSVD ETLKKLQEAF
460
DQACSSPQWV PVSWVY
Length:466
Mass (Da):52,227
Last modified:February 1, 1997 - v1
Checksum:i8724DE75A717A464
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38196 mRNA. Translation: AAC52970.1.
BC013444 mRNA. Translation: AAH13444.1.
CCDSiCCDS30236.1.
RefSeqiNP_032647.1. NM_008621.3.
UniGeneiMm.391267.

Genome annotation databases

EnsembliENSMUST00000033775; ENSMUSP00000033775; ENSMUSG00000031402.
GeneIDi17524.
KEGGimmu:17524.
UCSCiuc009tpp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38196 mRNA. Translation: AAC52970.1.
BC013444 mRNA. Translation: AAH13444.1.
CCDSiCCDS30236.1.
RefSeqiNP_032647.1. NM_008621.3.
UniGeneiMm.391267.

3D structure databases

ProteinModelPortaliP70290.
SMRiP70290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61219N.
IntActiP70290. 3 interactors.
MINTiMINT-4094335.
STRINGi10090.ENSMUSP00000033775.

PTM databases

iPTMnetiP70290.
PhosphoSitePlusiP70290.
SwissPalmiP70290.

Proteomic databases

EPDiP70290.
PaxDbiP70290.
PeptideAtlasiP70290.
PRIDEiP70290.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033775; ENSMUSP00000033775; ENSMUSG00000031402.
GeneIDi17524.
KEGGimmu:17524.
UCSCiuc009tpp.1. mouse.

Organism-specific databases

CTDi4354.
MGIiMGI:105941. Mpp1.

Phylogenomic databases

eggNOGiKOG0609. Eukaryota.
COG0194. LUCA.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000233034.
HOVERGENiHBG001858.
InParanoidiP70290.
OMAiIPNQQSR.
OrthoDBiEOG091G065I.
PhylomeDBiP70290.
TreeFamiTF314263.

Miscellaneous databases

ChiTaRSiMpp1. mouse.
PROiP70290.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031402.
CleanExiMM_MPP1.
ExpressionAtlasiP70290. baseline and differential.
GenevisibleiP70290. MM.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEM55_MOUSE
AccessioniPrimary (citable) accession number: P70290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.