Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00685
Entry Name
UniProt Accession
Theoretical PI
7.08
Molecular Weight
47355.28
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Flotillin-1
Protein Synonyms/Alias
Gene Name
FLOT1
Gene Synonyms/Alias
Created Date
21-FEB-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
5
Canonical
***MFFTCGPNEAMV
[2]
S-Palmitoylation
34
Canonical
GRVFVLPCIQQIQRI
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Morrow IC, Rea S, Martin S, Prior IA, Prohaska R, Hancock JF, James DE, PartonRG. Flotillin-1/reggie-2 traffics to surface raft domains via a novelgolgi-independent pathway. Identification of a novel membrane targeting domainand a role for palmitoylation. J Biol Chem. 2002 Dec 13;277(50):48834-41. Epub2002 Oct 4.[PMID:12370178]
[2] Predicted from GPS-Lipid
Functional Description
May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Sequence Annotation
Modified residue: 19 19 Phosphoserine.
Modified residue: 385 385 Phosphoserine.
Protein Length
427 AA.
Protein Sequence
(Canonical)
MFFTCGPNEA MVVSGFCRSP PVMVAGGRVF VLPCIQQIQR ISLNTLTLNV KSEKVYTRHG  60
VPISVTGIAQ VKIQGQNKEM LAAACQMFLG KTEAEIAHIA LETLEGHQRA IMAHMTVEEI  120
YKDRQKFSEQ VFKVASSDLV NMGISVVSYT LKDIHDDQDY LHSLGKARTA QVQKDARIGE  180
AEAKRDAGIR EAKAKQEKVS AQYLSEIEMA KAQRDYELKK AAYDIEVNTR RAQADLAYQL  240
QVAKTKQQIE EQRVQVQVVE RAQQVAVQEQ EIARREKELE ARVRKPAEAE RYKLERLAEA  300
EKSQLIMQAE AEAASVRMRG EAEAFAIGAR ARAEAEQMAK KAEAFQLYQE AAQLDMLLEK  360
LPQVAEEISG PLTSANKITL VSSGSGTMGA AKVTGEVLDI LTRLPESVER LTGVSISQVN  420
HKPLRTA                                                            427
FASTA
(Canonical)
>LipidDB-9606-00685|O75955
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHG
VPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEI
YKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGE
AEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQL
QVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEA
EKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEK
LPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVN
HKPLRTA
Gene Ontology
GO:0005901; C:caveola; TAS:ProtInc
GO:0034451; C:centriolar satellite; IDA:BHF-UCL
GO:0005768; C:endosome; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0016600; C:flotillin complex; IEA:Ensembl
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0016021; C:integral component of membrane; TAS:ProtInc
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0045121; C:membrane raft; IDA:BHF-UCL
GO:0005815; C:microtubule organizing center; IDA:BHF-UCL
GO:0042383; C:sarcolemma; IEA:Ensembl
GO:0002020; F:protease binding; IPI:UniProtKB
GO:0007409; P:axonogenesis; IEA:Ensembl
GO:0090002; P:establishment of protein localization to plasma membrane; IMP:UniProtKB
GO:0022617; P:extracellular matrix disassembly; IMP:UniProt
GO:0035023; P:regulation of Rho protein signal transduction; IEA:Ensembl
Interpro
InterPro; IPR001107; Band_7
InterPro; IPR027705; Flotillin_fam
Pfam
Pfam; PF01145; Band_7;
SMART
SMART; SM00244; PHB;
PROSITE
PRINTS