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Q24025 (SOG_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dorsal-ventral patterning protein Sog
Alternative name(s):
Short gastrulation protein
Gene names
Name:sog
ORF Names:CG9224
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1038 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative negative growth factor. Antagonist of dpp, a protein involved in patterning the dorsal region and in the development of the neuroectoderm; dpp inhibition is enhanced by tsg. Required for establishment of a narrow stripe of peak levels of BMP signaling in the dorsal midline of early embryos, that will give rise to the amnioserosa. Ref.1 Ref.5

Subunit structure

Component of a complex composed of dpp, sog and tsg.

Subcellular location

Membrane; Single-pass type II membrane protein Potential.

Tissue specificity

Abuts the dorsal dpp-expressing cells in a lateral stripe 14-16 cells wide. Later in embryogenesis it is expressed in neuroectoderm and in the endoderm spaced along the anterior-posterior axis of the developing gut. Ref.1

Developmental stage

Embryogenesis. Ref.1

Sequence similarities

Belongs to the chordin family.

Contains 4 CHRD domains.

Contains 4 VWFC domains.

Ontologies

Keywords
   Biological processGrowth regulation
   Cellular componentMembrane
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Growth factor
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Non-traceable author statement PubMed 11290316. Source: FlyBase

amnioserosa formation

Traceable author statement PubMed 1765005. Source: FlyBase

ectoderm development

Non-traceable author statement PubMed 9712300. Source: FlyBase

imaginal disc-derived wing vein morphogenesis

Inferred from mutant phenotype PubMed 15766758PubMed 15872004. Source: FlyBase

maternal specification of dorsal/ventral axis, oocyte, soma encoded

Inferred from mutant phenotype PubMed 16781701. Source: FlyBase

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement PubMed 11700289PubMed 15380237. Source: FlyBase

positive regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement PubMed 11700289. Source: FlyBase

posterior Malpighian tubule development

Inferred from mutant phenotype PubMed 17190812. Source: FlyBase

regulation of BMP signaling pathway

Traceable author statement PubMed 11532914. Source: FlyBase

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

ring gland development

Inferred from mutant phenotype PubMed 15385159. Source: FlyBase

terminal region determination

Inferred from genetic interaction PubMed 1905816. Source: FlyBase

torso signaling pathway

Inferred from genetic interaction PubMed 1905816. Source: FlyBase

zygotic determination of anterior/posterior axis, embryo

Non-traceable author statement PubMed 11290316. Source: FlyBase

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

   Molecular_functioncollagen binding

Inferred from direct assay PubMed 22733779. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10381038Dorsal-ventral patterning protein Sog
PRO_0000219089

Regions

Topological domain1 – 5353Cytoplasmic Potential
Transmembrane54 – 7421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain75 – 1038964Extracellular Potential
Domain100 – 17576VWFC 1
Domain197 – 337141CHRD 1
Domain339 – 471133CHRD 2
Domain474 – 588115CHRD 3
Domain592 – 713122CHRD 4
Domain742 – 80463VWFC 2
Domain830 – 89970VWFC 3
Domain939 – 102082VWFC 4

Amino acid modifications

Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation5201N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation7521N-linked (GlcNAc...) Potential
Glycosylation8211N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q24025 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B0E833AFD79A9037

FASTA1,038115,515
        10         20         30         40         50         60 
MANKLRKSNA IEWATATGTV PLLERSCCHS EDAALEPQAS KTSHREQAPI LRHLSQLSHL 

        70         80         90        100        110        120 
LIIAGLLIVC LAGVTEGRRH APLMFEESDT GRRSNRPAVT ECQFGKVLRE LGSTWYADLG 

       130        140        150        160        170        180 
PPFGVMYCIK CECVAIPKKR RIVARVQCRN IKNECPPAKC DDPISLPGKC CKTCPGDRND 

       190        200        210        220        230        240 
TDVALDVPVP NEEEERNMKH YAALLTGRTS YFLKGEEMKS MYTTYNPQNV VATARFLFHK 

       250        260        270        280        290        300 
KNLYYSFYTS SRIGRPRAIQ FVDDAGVILE EHQLETTLAG TLSVYQNATG KICGVWRRVP 

       310        320        330        340        350        360 
RDYKRILRDD RLHVVLLWGN KQQAELALAG KVAKYTALQT ELFSSLLEAP LPDGKTDPQL 

       370        380        390        400        410        420 
AGAGGTAIVS TSSGAASSMH LTLVFNGVFG AEEYADAALS VKIELAERKE VIFDEIPRVR 

       430        440        450        460        470        480 
KPSAEINVLE LSSPISIQNL RLMSRGKLLL TVESKKYPHL RIQGHIVTRA SCEIFQTLLA 

       490        500        510        520        530        540 
PHSAESSTKS SGLAWVYLNT DGSLAYNIET EHVNTRDRPN ISLIEEQGKR KAKLEDLTPS 

       550        560        570        580        590        600 
FNFNQAIGSV EKLGPKVLES LYAGELGVNV ATEHETSLIR GRLVPRPVAD ARDSAEPILL 

       610        620        630        640        650        660 
KRQEHTDAQN PHAVGMAWMS IDNECNLHYE VTLNGVPAQD LQLYLEEKPI EAIGAPVTRK 

       670        680        690        700        710        720 
LLEEFNGSYL EGFFLSMPSA ELIKLEMSVC YLEVHSKHSK QLLLRGKLKS TKVPGHCFPV 

       730        740        750        760        770        780 
YTDNNVPVPG DHNDNHLVNG ETKCFHSGRF YNESEQWRSA QDSCQMCACL RGQSSCEVIK 

       790        800        810        820        830        840 
CPALKCKSTE QLLQRDGECC PSCVPKKEAA DYSAQSSPAT NATDLLQQRR GCRLGEQFHP 

       850        860        870        880        890        900 
AGASWHPFLP PNGFDTCTTC SCDPLTLEIR CPRLVCPPLQ CSEKLAYRPD KKACCKICPE 

       910        920        930        940        950        960 
GKQSSSNGHK TTPNNPNVLQ DQAMQRSPSH SAEEVLANGG CKVVNKVYEN GQEWHPILMS 

       970        980        990       1000       1010       1020 
HGEQKCIKCR CKDSKVNCDR KRCSRSTCQQ QTRVTSKRRL FEKPDAAAPA IDECCSTQCR 

      1030 
RSRRHHKRQP HHQQRSSS 

« Hide

References

« Hide 'large scale' references
[1]"Dorsal-ventral patterning of the Drosophila embryo depends on a putative negative growth factor encoded by the short gastrulation gene."
Francois V., Solloway M., O'Neill J.W., Emery J., Bier E.
Genes Dev. 8:2602-2616(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[5]"Twisted gastrulation is a conserved extracellular BMP antagonist."
Ross J.J., Shimmi O., Vilmos P., Petryk A., Kim H., Gaudenz K., Hermanson S., Ekker S.C., O'Connor M.B., Marsh J.L.
Nature 410:479-483(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DPP AND TSG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18774 mRNA. Translation: AAA89117.1.
AE014298 Genomic DNA. Translation: AAF48481.1.
BT053679 mRNA. Translation: ACK77594.1.
PIRT13177.
RefSeqNP_001259576.1. NM_001272647.1.
NP_001259578.1. NM_001272649.1.
NP_476736.1. NM_057388.3.
UniGeneDm.3944.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58848. 14 interactions.
DIPDIP-20760N.
IntActQ24025. 3 interactions.
MINTMINT-299642.

Proteomic databases

PRIDEQ24025.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0074063; FBpp0073879; FBgn0003463.
FBtr0331760; FBpp0304148; FBgn0003463.
FBtr0331762; FBpp0304150; FBgn0003463.
GeneID32498.
KEGGdme:Dmel_CG9224.

Organism-specific databases

CTD32498.
FlyBaseFBgn0003463. sog.

Phylogenomic databases

eggNOGNOG85639.
GeneTreeENSGT00730000110792.
InParanoidQ24025.
KOK04657.
OMARDPGEGC.
OrthoDBEOG7QNVK7.
PhylomeDBQ24025.

Gene expression databases

BgeeQ24025.

Family and domain databases

InterProIPR016353. Chordin.
IPR010895. CHRD.
IPR001007. VWF_C.
[Graphical view]
PfamPF07452. CHRD. 4 hits.
PF00093. VWC. 4 hits.
[Graphical view]
PIRSFPIRSF002496. Chordin. 1 hit.
SMARTSM00754. CHRD. 4 hits.
SM00214. VWC. 3 hits.
[Graphical view]
PROSITEPS50933. CHRD. 4 hits.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi32498.
NextBio778773.
PROQ24025.

Entry information

Entry nameSOG_DROME
AccessionPrimary (citable) accession number: Q24025
Secondary accession number(s): B7FNI9, Q9VXS7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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