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Protein

Protein spitz

Gene

spi

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ligand for the EGF receptor (Gurken). Involved in a number of unrelated developmental choices, for example, dorsal-ventral axis formation, glial migration, sensory organ determination, and muscle development. It is required for photoreceptor determination.1 Publication

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: FlyBase
  • gurken receptor binding Source: FlyBase

GO - Biological processi

  • behavioral response to ethanol Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • branched duct epithelial cell fate determination, open tracheal system Source: FlyBase
  • determination of genital disc primordium Source: FlyBase
  • epidermal growth factor receptor signaling pathway Source: FlyBase
  • epithelial cell proliferation involved in Malpighian tubule morphogenesis Source: FlyBase
  • G2/M transition of mitotic cell cycle Source: FlyBase
  • heart process Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • negative regulation of apoptotic process Source: FlyBase
  • negative regulation of compound eye retinal cell programmed cell death Source: FlyBase
  • neurogenesis Source: FlyBase
  • oenocyte development Source: FlyBase
  • olfactory learning Source: FlyBase
  • open tracheal system development Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of epidermal growth factor receptor signaling pathway Source: FlyBase
  • positive regulation of neurogenesis Source: FlyBase
  • R8 cell-mediated photoreceptor organization Source: FlyBase
  • salivary gland boundary specification Source: FlyBase
  • second mitotic wave involved in compound eye morphogenesis Source: FlyBase
  • spiracle morphogenesis, open tracheal system Source: FlyBase
  • stem cell fate commitment Source: FlyBase
  • stomatogastric nervous system development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

SignaLinkiQ01083.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein spitz
Gene namesi
Name:spi
ORF Names:CG10334
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0005672. spi.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 143115LumenalSequence analysisAdd
BLAST
Transmembranei144 – 16421HelicalSequence analysisAdd
BLAST
Topological domaini165 – 23470CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: FlyBase
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular region Source: FlyBase
  • Golgi apparatus Source: FlyBase
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 234206Protein spitzPRO_0000007737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)
Disulfide bondi82 ↔ 97PROSITE-ProRule annotation1 Publication
Disulfide bondi91 ↔ 110PROSITE-ProRule annotation1 Publication
Disulfide bondi112 ↔ 121PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Proteolytic processing by Rhomboid occurs in the Golgi. Cleavage takes place within the transmembrane domain close to residue 144 and the active growth factor is released.1 Publication
N-glycosylated and O-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ01083.

PTM databases

SwissPalmiQ01083.

Miscellaneous databases

PMAP-CutDBQ01083.

Expressioni

Tissue specificityi

Expressed throughout the embryo.

Gene expression databases

BgeeiQ01083.
ExpressionAtlasiQ01083. differential.
GenevisibleiQ01083. DM.

Interactioni

Subunit structurei

Interacts with Star via the lumenal domain.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EgfrP044124EBI-91342,EBI-197863

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: FlyBase
  • gurken receptor binding Source: FlyBase

Protein-protein interaction databases

BioGridi61229. 47 interactions.
DIPiDIP-18037N.
IntActiQ01083. 5 interactions.
MINTiMINT-785907.
STRINGi7227.FBpp0080808.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi84 – 896Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi105 – 1117Combined sources
Beta strandi116 – 1183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C9AX-ray1.60C/D76-127[»]
3CA7X-ray1.50A76-127[»]
3LTFX-ray3.20B/D76-133[»]
3LTGX-ray3.40D76-126[»]
ProteinModelPortaliQ01083.
SMRiQ01083. Positions 76-125.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01083.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 12245EGF-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi65 – 706Poly-Thr
Compositional biasi186 – 1894Poly-Asp

Sequence similaritiesi

Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IYKD. Eukaryota.
ENOG4111N7J. LUCA.
GeneTreeiENSGT00520000062215.
InParanoidiQ01083.
OMAiSGAMCAL.
OrthoDBiEOG7PZS0C.
PhylomeDBiQ01083.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q01083-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSTMSVQHG LVALVLIGCL AHPWHVEACS SRTVPKPRSS ISSSMSGTAL
60 70 80 90 100
PPTQAPVTSS TTMRTTTTTT PRPNITFPTY KCPETFDAWY CLNDAHCFAV
110 120 130 140 150
KIADLPVYSC ECAIGFMGQR CEYKEIDNTY LPKRPRPMLE KASIASGAMC
160 170 180 190 200
ALVFMLFVCL AFYLRFEQRA AKKAYELEQE LQQEYDDDDG QCECCRNRCC
210 220 230
PDGQEPVILE RKLPYHMRLE HALMSFAIRR SNKL
Length:234
Mass (Da):26,424
Last modified:July 19, 2004 - v2
Checksum:i237F7A3B03DBD685
GO

Sequence cautioni

The sequence AAA28894.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191Q → R in AAL90431 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95199 mRNA. Translation: AAA28894.1. Different initiation.
AE014134 Genomic DNA. Translation: AAF53831.2.
AY089693 mRNA. Translation: AAL90431.1.
PIRiA44074.
RefSeqiNP_001027281.1. NM_001032110.2.
NP_476909.2. NM_057561.6.
NP_599118.2. NM_134291.5.
NP_599119.2. NM_134292.3.
NP_599120.2. NM_134293.3.
UniGeneiDm.4573.

Genome annotation databases

EnsemblMetazoaiFBtr0081267; FBpp0080808; FBgn0005672.
FBtr0081268; FBpp0080809; FBgn0005672.
FBtr0081269; FBpp0080810; FBgn0005672.
FBtr0081270; FBpp0080811; FBgn0005672.
FBtr0100597; FBpp0100054; FBgn0005672.
GeneIDi35253.
KEGGidme:Dmel_CG10334.
UCSCiCG10334-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95199 mRNA. Translation: AAA28894.1. Different initiation.
AE014134 Genomic DNA. Translation: AAF53831.2.
AY089693 mRNA. Translation: AAL90431.1.
PIRiA44074.
RefSeqiNP_001027281.1. NM_001032110.2.
NP_476909.2. NM_057561.6.
NP_599118.2. NM_134291.5.
NP_599119.2. NM_134292.3.
NP_599120.2. NM_134293.3.
UniGeneiDm.4573.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C9AX-ray1.60C/D76-127[»]
3CA7X-ray1.50A76-127[»]
3LTFX-ray3.20B/D76-133[»]
3LTGX-ray3.40D76-126[»]
ProteinModelPortaliQ01083.
SMRiQ01083. Positions 76-125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61229. 47 interactions.
DIPiDIP-18037N.
IntActiQ01083. 5 interactions.
MINTiMINT-785907.
STRINGi7227.FBpp0080808.

PTM databases

SwissPalmiQ01083.

Proteomic databases

PaxDbiQ01083.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081267; FBpp0080808; FBgn0005672.
FBtr0081268; FBpp0080809; FBgn0005672.
FBtr0081269; FBpp0080810; FBgn0005672.
FBtr0081270; FBpp0080811; FBgn0005672.
FBtr0100597; FBpp0100054; FBgn0005672.
GeneIDi35253.
KEGGidme:Dmel_CG10334.
UCSCiCG10334-RA. d. melanogaster.

Organism-specific databases

CTDi35253.
FlyBaseiFBgn0005672. spi.

Phylogenomic databases

eggNOGiENOG410IYKD. Eukaryota.
ENOG4111N7J. LUCA.
GeneTreeiENSGT00520000062215.
InParanoidiQ01083.
OMAiSGAMCAL.
OrthoDBiEOG7PZS0C.
PhylomeDBiQ01083.

Enzyme and pathway databases

SignaLinkiQ01083.

Miscellaneous databases

ChiTaRSispi. fly.
EvolutionaryTraceiQ01083.
GenomeRNAii35253.
NextBioi792614.
PMAP-CutDBQ01083.
PROiQ01083.

Gene expression databases

BgeeiQ01083.
ExpressionAtlasiQ01083. differential.
GenevisibleiQ01083. DM.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila spitz gene encodes a putative EGF-like growth factor involved in dorsal-ventral axis formation and neurogenesis."
    Rutledge B.J., Zhang K., Bier E., Jan Y.N., Perrimon N.
    Genes Dev. 6:1503-1517(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "The spitz gene is required for photoreceptor determination in the Drosophila eye where it interacts with the EGF receptor."
    Freeman M.
    Mech. Dev. 48:25-33(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila."
    Lee J.R., Urban S., Garvey C.F., Freeman M.
    Cell 107:161-171(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  7. "EGF receptor signalling: roles of Star and Rhomboid revealed."
    Klaembt C.
    Curr. Biol. 12:R21-R23(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "Structural basis for EGFR ligand sequestration by Argos."
    Klein D.E., Stayrook S.E., Shi F., Narayan K., Lemmon M.A.
    Nature 453:1271-1275(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 76-127 IN COMPLEX WITH ARGOS, DISULFIDE BONDS.

Entry informationi

Entry nameiSPITZ_DROME
AccessioniPrimary (citable) accession number: Q01083
Secondary accession number(s): Q8SXE0, Q9VIT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 19, 2004
Last modified: May 11, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.