LipidDB-9606-00740

Lipid Modification Database

Tag

Content

LipidDB ID

LipidDB-9606-00740

Entry Name

STOM_HUMAN

UniProt Accession

P27105; B1AM77; Q14087; Q15609; Q5VX96; Q96FK4;

Theoretical PI

7.71

Molecular Weight

31730.8

Genbank Protein ID

CAA42671.1; AAA58432.1; CAA59436.1; CAA59436.1; AAC50296.1; AAC50296.1; AAC50296.1; AAC50296.1; AAC50296.1; AAC50296.1; AAC50296.1; CAG46897.1; CAH70728.1; CAH70728.1; CAH70729.1; CAH70729.1; CAH72706.1; CAH72706.1; CAH72707.1; CAH72707.1; AAH10703.1;

Genbank Nucleotide ID

X60067; M81635; X85116; X85117; U33931; U33925; U33926; U33927; U33928; U33929; U33930; CR542100; AL359644; AL161784; AL359644; AL161784; AL161784; AL359644; AL161784; AL359644; BC010703; BI603242;

Protein Name

Erythrocyte band 7 integral membrane protein

Protein Synonyms/Alias

Protein 7.2b; Stomatin;

Gene Name

STOM

Gene Synonyms/Alias

BND7; EPB72;

Created Date

01-AUG-1992

Lipid Modification Sites
Position	Sequence Form	Peptide	References	Modification Type
30	Canonical	PSKGLGPCGWILVAF	[1]	S-Palmitoylation
87	Canonical	GLFFILPCTDSFIKV	[1]	S-Palmitoylation

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Snyers L, Umlauf E, Prohaska R. Cysteine 29 is the major palmitoylation siteon stomatin. FEBS Lett. 1999 Apr 23;449(2-3):101-4.[PMID:10338112]

Functional Description

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

Sequence Annotation

Topological domain: 1 25 Cytoplasmic.
Topological domain: 55 288 Cytoplasmic.
Region: 265 273 Required for homooligomerization.
Region: 267 269 Required for lipid raft association.
Region: 273 287 Interaction with LANCL1.
Modified residue: 10 10 Phosphoserine; by PKA.
Modified residue: 161 161 Phosphoserine.
Modified residue: 244 244 Phosphoserine.

Protein Length

288 AA.

Protein Sequence
(Canonical)

MAEKRHTRDS EAQRLPDSFK DSPSKGLGPC GWILVAFSFL FTVITFPISI WMCIKIIKEY  60
ERAIIFRLGR ILQGGAKGPG LFFILPCTDS FIKVDMRTIS FDIPPQEILT KDSVTISVDG  120
VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNVLGTKNL SQILSDREEI AHNMQSTLDD  180
ATDAWGIKVE RVEIKDVKLP VQLQRAMAAE AEASREARAK VIAAEGEMNA SRALKEASMV  240
ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPIDMLQGII GAKHSHLG               288

FASTA
(Canonical)

>LipidDB-9606-00740|P27105
MAEKRHTRDSEAQRLPDSFKDSPSKGLGPCGWILVAFSFLFTVITFPISIWMCIKIIKEY
ERAIIFRLGRILQGGAKGPGLFFILPCTDSFIKVDMRTISFDIPPQEILTKDSVTISVDG
VVYYRVQNATLAVANITNADSATRLLAQTTLRNVLGTKNLSQILSDREEIAHNMQSTLDD
ATDAWGIKVERVEIKDVKLPVQLQRAMAAEAEASREARAKVIAAEGEMNASRALKEASMV
ITESPAALQLRYLQTLTTIAAEKNSTIVFPLPIDMLQGIIGAKHSHLG

Gene Ontology

GO:0072562; C:blood microparticle; IDA:UniProt
GO:0005737; C:cytoplasm; IDA:HPA
GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW
GO:0005856; C:cytoskeleton; IDA:UniProtKB
GO:0005615; C:extracellular space; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0045121; C:membrane raft; IDA:UniProtKB
GO:0031982; C:vesicle; IDA:UniProtKB
GO:0051260; P:protein homooligomerization; IDA:UniProtKB
GO:1901585; P:regulation of acid-sensing ion channel activity; IEA:Ensembl

Interpro

InterPro; IPR001107; Band_7
InterPro; IPR018080; Band_7/stomatin-like_CS
InterPro; IPR028515; Stomatin
InterPro; IPR001972; Stomatin_fam

Pfam

Pfam; PF01145; Band_7;

SMART

SMART; SM00244; PHB;

PROSITE

PROSITE; PS01270; BAND_7;

PRINTS

PRINTS; PR00721; STOMATIN;