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Signal Peptide Database - Drosophila melanogaster
Entry Details
ID
3340
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
Q9VSL7 (Created: 2005-02-15 Updated: 2008-12-16)
UniProtKB/Swiss-Prot Entry Name
FOI_DROME
Protein Name
Zinc transporter foi
Gene
foi
Organism Scientific
Drosophila melanogaster
Organism Common
Fruit fly
Lineage
Eukaryota
Metazoa
Arthropoda
Hexapoda
Insecta
Pterygota
Neoptera
Endopterygota
Diptera
Brachycera
Muscomorpha
Ephydroidea
Drosophilidae
Drosophila
Sophophora
Protein Length [aa]
706
Protein Mass [Da]
77376
Features
Type
Description
Status
Start
End
signal peptide
potential
1
21
chain
Zinc transporter foi
22
706
transmembrane region
1
potential
262
282
transmembrane region
2
potential
293
313
transmembrane region
3
potential
330
350
transmembrane region
4
potential
605
625
transmembrane region
5
potential
632
652
transmembrane region
6
potential
666
686
topological domain
Extracellular
potential
22
261
topological domain
Cytoplasmic
potential
283
292
topological domain
Extracellular
potential
314
329
topological domain
Cytoplasmic
potential
351
604
topological domain
Extracellular
potential
626
631
topological domain
Cytoplasmic
potential
653
665
topological domain
Extracellular
potential
687
706
modified residue
Phosphoserine
376
376
modified residue
Phosphoserine
377
377
modified residue
Phosphoserine
381
381
glycosylation site
N-linked (GlcNAc...)
potential
74
74
glycosylation site
N-linked (GlcNAc...)
potential
119
119
glycosylation site
N-linked (GlcNAc...)
potential
176
176
glycosylation site
N-linked (GlcNAc...)
potential
182
182
glycosylation site
N-linked (GlcNAc...)
potential
196
196
glycosylation site
N-linked (GlcNAc...)
potential
207
207
mutagenesis site
4-fold reduction in zinc transport activity in yeast assay
0
0
mutagenesis site
Severely reduced zinc transport activity in yeast assay
0
0
mutagenesis site
2-fold reduction in zinc transport activity in yeast assay; when in association with A-588 and A-591
0
0
mutagenesis site
2-fold reduction in zinc transport activity in yeast assay; when in association with A-584 and A-591
0
0
mutagenesis site
2-fold reduction in zinc transport activity in yeast assay; when in association with A-584 and A-588
0
0
mutagenesis site
2-fold reduction zinc transport activity in yeast assay
0
0
SP Length
21
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
MARHIMAVCVVCLLCAHRLHC
Sequence
MARHIMAVCVVCLLCAHRLHC
QDHIESLLGPARVTTHNSQDQLNARVYTN
LSPSSETTDRRQQRSASGDDDTF
N
YSISPPSRREKRHAGHEHGPTSESRV
PQITQYYLEKLMAQDELM
N
SSGFDGLLQQLSLHSLASGASEGTCVPGSRL
VHHVQPHDHHHAHHHEEEDHSLQLN
N
CTLIQ
N
GTTSNVICPSLPN
N
NTHP
LGKEAK
N
FTLSDKDLLHLCPILLYELKAQSGGCIEPAILSDIDTTEELLE
AEKDKDIFYVW
IYAFISVFACGILGLVGVAII
PFMGSRYYKY
IIQYLVAL
AVGTMTGDALLHL
LPHSLAGQDERGMIMK
GLGCLGGIIFFYVMEHALTMI
SEWRKSVEKKETKKPSRAKVMRDPD
S
S
VNN
S
VAGDKICKQKYSSYPYCYD
EITMNNKQSEWMHLPFDVAAGAGGDAPSVAELRNGVGDHDGSNDMAAAAE
SLISPLHTNCVEMNHHNHNHKHNSHQQNHEGQDSNTIVTDLDGNAVYAVN
KAKDKDSRNDHVTVILREHESSHHGHSHRHGHVHSPPETLSAVAWMIIMG
DGLHNFTDGMAIGAAFAENIAGGFSTSLAVFCHELPHELGDFAILIKAGM
SVKS
AVYYNLLTGVLSFIGMIFGIA
FGQSQD
VAQWMFAVAAGLFIYIALV
DM
MPEISASHKSLGQ
FLLQILGMLSGVGIMLLIALY
EGDLMSAFGTAGAA
SHQHAH
Original
MARHIMAVCVVCLLCAHRLHCQDHIESLLGPARVTTHNSQDQLNARVYTN
LSPSSETTDRRQQRSASGDDDTFNYSISPPSRREKRHAGHEHGPTSESRV
PQITQYYLEKLMAQDELMNSSGFDGLLQQLSLHSLASGASEGTCVPGSRL
VHHVQPHDHHHAHHHEEEDHSLQLNNCTLIQNGTTSNVICPSLPNNNTHP
LGKEAKNFTLSDKDLLHLCPILLYELKAQSGGCIEPAILSDIDTTEELLE
AEKDKDIFYVWIYAFISVFACGILGLVGVAIIPFMGSRYYKYIIQYLVAL
AVGTMTGDALLHLLPHSLAGQDERGMIMKGLGCLGGIIFFYVMEHALTMI
SEWRKSVEKKETKKPSRAKVMRDPDSSVNNSVAGDKICKQKYSSYPYCYD
EITMNNKQSEWMHLPFDVAAGAGGDAPSVAELRNGVGDHDGSNDMAAAAE
SLISPLHTNCVEMNHHNHNHKHNSHQQNHEGQDSNTIVTDLDGNAVYAVN
KAKDKDSRNDHVTVILREHESSHHGHSHRHGHVHSPPETLSAVAWMIIMG
DGLHNFTDGMAIGAAFAENIAGGFSTSLAVFCHELPHELGDFAILIKAGM
SVKSAVYYNLLTGVLSFIGMIFGIAFGQSQDVAQWMFAVAAGLFIYIALV
DMMPEISASHKSLGQFLLQILGMLSGVGIMLLIALYEGDLMSAFGTAGAA
SHQHAH
----+----1----+----2----+----3----+----4----+----5
Hydropathies
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Dr. Katja Kapp
, Kassel &
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, Dresden, Germany, last update 2010-06-11