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Protein

Erythrocyte band 7 integral membrane protein

Gene

Stom

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

Functioni

Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase binding Source: MGI

GO - Biological processi

  • mitophagy in response to mitochondrial depolarization Source: Ensembl
  • positive regulation by host of viral genome replication Source: AgBase
  • positive regulation of defense response to virus by host Source: Ensembl
  • positive regulation of protein targeting to membrane Source: AgBase
  • positive regulation of viral process Source: AgBase
  • protein homooligomerization Source: UniProtKB
  • regulation of acid-sensing ion channel activity Source: UniProtKB
  • regulation of ion transmembrane transport Source: UniProtKB
  • xenophagy Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythrocyte band 7 integral membrane protein
Alternative name(s):
Protein 7.2b
Stomatin
Gene namesi
Name:Stom
Synonyms:Epb7.2, Epb72
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:95403. Stom.

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cytoplasmcytoskeleton By similarity
  • Cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
  • Membrane raft By similarity
  • Melanosome By similarity
  • Cytoplasmic vesicle 1 Publication

  • Note: Localizes to juxtanuclear structure probably derived from the Golgi apparatus. Colocalizes with cortical actin microfilaments at small plasma membrane protrusions. Associates with alpha-granular lipid rafts. Translocates from the alpha-granular lipid rafts to the cell membrane on thrombin activation and selectively enriched in released microvesicles. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 31CytoplasmicSequence analysisAdd BLAST31
Intramembranei32 – 52Sequence analysisAdd BLAST21
Topological domaini53 – 284CytoplasmicSequence analysisAdd BLAST232

GO - Cellular componenti

  • blood microparticle Source: MGI
  • cytoplasm Source: AgBase
  • cytoskeleton Source: UniProtKB
  • endoplasmic reticulum Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: MGI
  • membrane raft Source: UniProtKB
  • mitochondrion Source: AgBase
  • perinuclear region of cytoplasm Source: AgBase
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97R → D: Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-109 and D-145. 1 Publication1
Mutagenesisi109L → D: Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-145. 1 Publication1
Mutagenesisi145L → D: Does not abolish interaction with ASIC3, but abolishes regulation of ASIC3 channel activity; when associated with D-97 and D-109. 1 Publication1
Mutagenesisi182T → W: Does not abolish interaction with ASIC3, but abolishes regulation of ASIC2 and ASIC3 channel activity. 1 Publication1
Mutagenesisi197V → P: Abolishes homodimerization and oligomerization. Abolishes regulation of ASIC2 and ASIC3 channel activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000940281 – 284Erythrocyte band 7 integral membrane proteinAdd BLAST284

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18PhosphoserineBy similarity1
Lipidationi30S-palmitoyl cysteineBy similarity1
Lipidationi87S-palmitoyl cysteineBy similarity1
Modified residuei161PhosphoserineCombined sources1
Modified residuei244PhosphoserineCombined sources1

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP54116.
PaxDbiP54116.
PeptideAtlasiP54116.
PRIDEiP54116.

PTM databases

iPTMnetiP54116.
PhosphoSitePlusiP54116.
SwissPalmiP54116.

Expressioni

Tissue specificityi

Expressed in all sensory neurons of the dorsal root ganglia. In the CNS, expressed in many neurons of the spinal cord, medulla and pons. Expressed only in scattered neurons in the cortex, hippocampus, thalamus and basal ganglia. In the cerebellum, expressed in all Purkinje cells (at protein level). Widely expressed with high levels in heart, liver, skeletal muscle and testis and low levels in lung, brain and spleen.2 Publications

Developmental stagei

First expressed in the developing embryo at E11.5 when target innervation is complete. Expression continues into adulthood.1 Publication

Gene expression databases

BgeeiENSMUSG00000026880.
CleanExiMM_STOM.
GenevisibleiP54116. MM.

Interactioni

Subunit structurei

Interacts with LANCL1. Interacts with SLC2A1 and SLC4A1. Identified in large complexes with SLC40A1, SLC14A1, SLC29A1 and AQP1 (By similarity). Homodimer and higher order homooligomers. The homodimer is banana-shaped. Interacts with ASIC1, ASIC2 and ASIC3.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-8004826,EBI-8004826
Asic3O352403EBI-8004826,EBI-982374From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase binding Source: MGI

Protein-protein interaction databases

BioGridi199465. 1 interactor.
IntActiP54116. 2 interactors.
STRINGi10090.ENSMUSP00000028241.

Structurei

Secondary structure

1284
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi99 – 109Combined sources11
Beta strandi115 – 127Combined sources13
Helixi129 – 134Combined sources6
Beta strandi135 – 137Combined sources3
Helixi139 – 156Combined sources18
Helixi160 – 165Combined sources6
Helixi167 – 182Combined sources16
Helixi183 – 185Combined sources3
Beta strandi187 – 198Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FVFX-ray2.46A/B86-213[»]
4FVGX-ray1.80A86-213[»]
4FVJX-ray2.69A/B/C/D/E/F/G/H86-213[»]
ProteinModelPortaliP54116.
SMRiP54116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni265 – 273Required for homooligomerizationBy similarity9
Regioni267 – 269Required for lipid raft associationBy similarity3
Regioni273 – 284Interaction with LANCL1By similarityAdd BLAST12

Sequence similaritiesi

Belongs to the band 7/mec-2 family.Curated

Phylogenomic databases

eggNOGiKOG2621. Eukaryota.
COG0330. LUCA.
GeneTreeiENSGT00550000074454.
HOGENOMiHOG000217040.
HOVERGENiHBG004815.
InParanoidiP54116.
KOiK17286.
OMAiIIPEYER.
OrthoDBiEOG091G0G9K.
PhylomeDBiP54116.
TreeFamiTF105750.

Family and domain databases

InterProiIPR001107. Band_7.
IPR018080. Band_7/stomatin-like_CS.
IPR028515. Stomatin.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERiPTHR10264. PTHR10264. 1 hit.
PTHR10264:SF86. PTHR10264:SF86. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSiPR00721. STOMATIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.
PROSITEiPS01270. BAND_7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKRQSSHV QSQRIPESFR ENSKTELGAC GWILVAASFF FVIITFPISI
60 70 80 90 100
WICIKIVKEY ERVIIFRLGR ILQGGAKGPG LFFILPCTDS LIKVDMRTIS
110 120 130 140 150
FDIPPQEVLT KDSVTISVDG VVYYRVQNAT LAVANITNAD SATRLLAQTT
160 170 180 190 200
LRNALGTKNL SQILSDREEI AHHMQSTLDD ATDDWGIKVE RVEIKDVKLP
210 220 230 240 250
VQLQRAMAAE AEAAREARAK VIAAEGEMNA SRALKEASMV ITESPAALQL
260 270 280
RYLQTLTTIA AEKNSTIVFP LPVDMLQGIM GSNH
Length:284
Mass (Da):31,375
Last modified:January 9, 2007 - v3
Checksum:iAB7CC0E5FF2DF4A9
GO

Sequence cautioni

The sequence AAB18857 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3D → V in AAC64173 (PubMed:10383825).Curated1
Sequence conflicti37A → V in CAA62503 (PubMed:8921901).Curated1
Sequence conflicti40F → I in CAA62503 (PubMed:8921901).Curated1
Sequence conflicti43I → L in CAA62503 (PubMed:8921901).Curated1
Sequence conflicti91L → F in CAA62503 (PubMed:8921901).Curated1
Sequence conflicti273V → I in CAA62503 (PubMed:8921901).Curated1
Sequence conflicti283N → H in CAA62503 (PubMed:8921901).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17297 mRNA. Translation: AAA75024.1.
X91043 mRNA. Translation: CAA62503.1.
U50999
, U50993, U50994, U50995, U50996, U50997, U50998 Genomic DNA. Translation: AAB18857.1. Sequence problems.
AF093620 mRNA. Translation: AAC64173.1.
AK139242 mRNA. Translation: BAE23930.1.
AK143724 mRNA. Translation: BAE25516.1.
AK148975 mRNA. Translation: BAE28708.1.
AK149689 mRNA. Translation: BAE29028.1.
AK149821 mRNA. Translation: BAE29103.1.
AK149991 mRNA. Translation: BAE29219.1.
AK151129 mRNA. Translation: BAE30137.1.
CCDSiCCDS15961.1.
PIRiJC5221.
RefSeqiNP_038543.1. NM_013515.2.
UniGeneiMm.295284.

Genome annotation databases

EnsembliENSMUST00000028241; ENSMUSP00000028241; ENSMUSG00000026880.
GeneIDi13830.
KEGGimmu:13830.
UCSCiuc008jkh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17297 mRNA. Translation: AAA75024.1.
X91043 mRNA. Translation: CAA62503.1.
U50999
, U50993, U50994, U50995, U50996, U50997, U50998 Genomic DNA. Translation: AAB18857.1. Sequence problems.
AF093620 mRNA. Translation: AAC64173.1.
AK139242 mRNA. Translation: BAE23930.1.
AK143724 mRNA. Translation: BAE25516.1.
AK148975 mRNA. Translation: BAE28708.1.
AK149689 mRNA. Translation: BAE29028.1.
AK149821 mRNA. Translation: BAE29103.1.
AK149991 mRNA. Translation: BAE29219.1.
AK151129 mRNA. Translation: BAE30137.1.
CCDSiCCDS15961.1.
PIRiJC5221.
RefSeqiNP_038543.1. NM_013515.2.
UniGeneiMm.295284.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FVFX-ray2.46A/B86-213[»]
4FVGX-ray1.80A86-213[»]
4FVJX-ray2.69A/B/C/D/E/F/G/H86-213[»]
ProteinModelPortaliP54116.
SMRiP54116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199465. 1 interactor.
IntActiP54116. 2 interactors.
STRINGi10090.ENSMUSP00000028241.

PTM databases

iPTMnetiP54116.
PhosphoSitePlusiP54116.
SwissPalmiP54116.

Proteomic databases

MaxQBiP54116.
PaxDbiP54116.
PeptideAtlasiP54116.
PRIDEiP54116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028241; ENSMUSP00000028241; ENSMUSG00000026880.
GeneIDi13830.
KEGGimmu:13830.
UCSCiuc008jkh.1. mouse.

Organism-specific databases

CTDi2040.
MGIiMGI:95403. Stom.

Phylogenomic databases

eggNOGiKOG2621. Eukaryota.
COG0330. LUCA.
GeneTreeiENSGT00550000074454.
HOGENOMiHOG000217040.
HOVERGENiHBG004815.
InParanoidiP54116.
KOiK17286.
OMAiIIPEYER.
OrthoDBiEOG091G0G9K.
PhylomeDBiP54116.
TreeFamiTF105750.

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiStom. mouse.
PROiP54116.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026880.
CleanExiMM_STOM.
GenevisibleiP54116. MM.

Family and domain databases

InterProiIPR001107. Band_7.
IPR018080. Band_7/stomatin-like_CS.
IPR028515. Stomatin.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERiPTHR10264. PTHR10264. 1 hit.
PTHR10264:SF86. PTHR10264:SF86. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSiPR00721. STOMATIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.
PROSITEiPS01270. BAND_7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTOM_MOUSE
AccessioniPrimary (citable) accession number: P54116
Secondary accession number(s): O88988
, Q3UP81, Q60744, Q62455
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 9, 2007
Last modified: November 30, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.