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Q24025

- SOG_DROME

UniProt

Q24025 - SOG_DROME

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Protein

Dorsal-ventral patterning protein Sog

Gene

sog

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. collagen binding Source: FlyBase

GO - Biological processi

  1. amnioserosa formation Source: FlyBase
  2. BMP signaling pathway Source: FlyBase
  3. ectoderm development Source: FlyBase
  4. imaginal disc-derived wing vein morphogenesis Source: FlyBase
  5. maternal specification of dorsal/ventral axis, oocyte, soma encoded Source: FlyBase
  6. negative regulation of transforming growth factor beta receptor signaling pathway Source: FlyBase
  7. positive regulation of transforming growth factor beta receptor signaling pathway Source: FlyBase
  8. posterior Malpighian tubule development Source: FlyBase
  9. regulation of BMP signaling pathway Source: FlyBase
  10. regulation of growth Source: UniProtKB-KW
  11. ring gland development Source: FlyBase
  12. terminal region determination Source: FlyBase
  13. torso signaling pathway Source: FlyBase
  14. zygotic determination of anterior/posterior axis, embryo Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor

Keywords - Biological processi

Growth regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Dorsal-ventral patterning protein Sog
Alternative name(s):
Short gastrulation protein
Gene namesi
Name:sog
ORF Names:CG9224
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003463. sog.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5353CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei54 – 7421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini75 – 1038964ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10381038Dorsal-ventral patterning protein SogPRO_0000219089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi821 – 8211N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ24025.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Embryogenesis.1 Publication

Gene expression databases

BgeeiQ24025.
ExpressionAtlasiQ24025. differential.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi58848. 14 interactions.
DIPiDIP-20760N.
IntActiQ24025. 3 interactions.
MINTiMINT-299642.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 17576VWFC 1PROSITE-ProRule annotationAdd
BLAST
Domaini197 – 337141CHRD 1PROSITE-ProRule annotationAdd
BLAST
Domaini339 – 471133CHRD 2PROSITE-ProRule annotationAdd
BLAST
Domaini474 – 588115CHRD 3PROSITE-ProRule annotationAdd
BLAST
Domaini592 – 713122CHRD 4PROSITE-ProRule annotationAdd
BLAST
Domaini742 – 80463VWFC 2PROSITE-ProRule annotationAdd
BLAST
Domaini830 – 89970VWFC 3PROSITE-ProRule annotationAdd
BLAST
Domaini939 – 102082VWFC 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the chordin family.Curated
Contains 4 CHRD domains.PROSITE-ProRule annotation
Contains 4 VWFC domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG85639.
GeneTreeiENSGT00730000110792.
InParanoidiQ24025.
KOiK04657.
OMAiRDPGEGC.
OrthoDBiEOG7QNVK7.
PhylomeDBiQ24025.

Family and domain databases

InterProiIPR016353. Chordin.
IPR010895. CHRD.
IPR001007. VWF_C.
[Graphical view]
PfamiPF07452. CHRD. 4 hits.
PF00093. VWC. 4 hits.
[Graphical view]
PIRSFiPIRSF002496. Chordin. 1 hit.
SMARTiSM00754. CHRD. 4 hits.
SM00214. VWC. 3 hits.
[Graphical view]
PROSITEiPS50933. CHRD. 4 hits.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24025-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANKLRKSNA IEWATATGTV PLLERSCCHS EDAALEPQAS KTSHREQAPI
60 70 80 90 100
LRHLSQLSHL LIIAGLLIVC LAGVTEGRRH APLMFEESDT GRRSNRPAVT
110 120 130 140 150
ECQFGKVLRE LGSTWYADLG PPFGVMYCIK CECVAIPKKR RIVARVQCRN
160 170 180 190 200
IKNECPPAKC DDPISLPGKC CKTCPGDRND TDVALDVPVP NEEEERNMKH
210 220 230 240 250
YAALLTGRTS YFLKGEEMKS MYTTYNPQNV VATARFLFHK KNLYYSFYTS
260 270 280 290 300
SRIGRPRAIQ FVDDAGVILE EHQLETTLAG TLSVYQNATG KICGVWRRVP
310 320 330 340 350
RDYKRILRDD RLHVVLLWGN KQQAELALAG KVAKYTALQT ELFSSLLEAP
360 370 380 390 400
LPDGKTDPQL AGAGGTAIVS TSSGAASSMH LTLVFNGVFG AEEYADAALS
410 420 430 440 450
VKIELAERKE VIFDEIPRVR KPSAEINVLE LSSPISIQNL RLMSRGKLLL
460 470 480 490 500
TVESKKYPHL RIQGHIVTRA SCEIFQTLLA PHSAESSTKS SGLAWVYLNT
510 520 530 540 550
DGSLAYNIET EHVNTRDRPN ISLIEEQGKR KAKLEDLTPS FNFNQAIGSV
560 570 580 590 600
EKLGPKVLES LYAGELGVNV ATEHETSLIR GRLVPRPVAD ARDSAEPILL
610 620 630 640 650
KRQEHTDAQN PHAVGMAWMS IDNECNLHYE VTLNGVPAQD LQLYLEEKPI
660 670 680 690 700
EAIGAPVTRK LLEEFNGSYL EGFFLSMPSA ELIKLEMSVC YLEVHSKHSK
710 720 730 740 750
QLLLRGKLKS TKVPGHCFPV YTDNNVPVPG DHNDNHLVNG ETKCFHSGRF
760 770 780 790 800
YNESEQWRSA QDSCQMCACL RGQSSCEVIK CPALKCKSTE QLLQRDGECC
810 820 830 840 850
PSCVPKKEAA DYSAQSSPAT NATDLLQQRR GCRLGEQFHP AGASWHPFLP
860 870 880 890 900
PNGFDTCTTC SCDPLTLEIR CPRLVCPPLQ CSEKLAYRPD KKACCKICPE
910 920 930 940 950
GKQSSSNGHK TTPNNPNVLQ DQAMQRSPSH SAEEVLANGG CKVVNKVYEN
960 970 980 990 1000
GQEWHPILMS HGEQKCIKCR CKDSKVNCDR KRCSRSTCQQ QTRVTSKRRL
1010 1020 1030
FEKPDAAAPA IDECCSTQCR RSRRHHKRQP HHQQRSSS
Length:1,038
Mass (Da):115,515
Last modified:November 1, 1996 - v1
Checksum:iB0E833AFD79A9037
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18774 mRNA. Translation: AAA89117.1.
AE014298 Genomic DNA. Translation: AAF48481.1.
BT053679 mRNA. Translation: ACK77594.1.
PIRiT13177.
RefSeqiNP_001259576.1. NM_001272647.2.
NP_001259578.1. NM_001272649.2.
NP_476736.1. NM_057388.4.
UniGeneiDm.3944.

Genome annotation databases

EnsemblMetazoaiFBtr0074063; FBpp0073879; FBgn0003463.
FBtr0331760; FBpp0304148; FBgn0003463.
FBtr0331762; FBpp0304150; FBgn0003463.
GeneIDi32498.
KEGGidme:Dmel_CG9224.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18774 mRNA. Translation: AAA89117.1 .
AE014298 Genomic DNA. Translation: AAF48481.1 .
BT053679 mRNA. Translation: ACK77594.1 .
PIRi T13177.
RefSeqi NP_001259576.1. NM_001272647.2.
NP_001259578.1. NM_001272649.2.
NP_476736.1. NM_057388.4.
UniGenei Dm.3944.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58848. 14 interactions.
DIPi DIP-20760N.
IntActi Q24025. 3 interactions.
MINTi MINT-299642.

Proteomic databases

PRIDEi Q24025.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0074063 ; FBpp0073879 ; FBgn0003463 .
FBtr0331760 ; FBpp0304148 ; FBgn0003463 .
FBtr0331762 ; FBpp0304150 ; FBgn0003463 .
GeneIDi 32498.
KEGGi dme:Dmel_CG9224.

Organism-specific databases

CTDi 32498.
FlyBasei FBgn0003463. sog.

Phylogenomic databases

eggNOGi NOG85639.
GeneTreei ENSGT00730000110792.
InParanoidi Q24025.
KOi K04657.
OMAi RDPGEGC.
OrthoDBi EOG7QNVK7.
PhylomeDBi Q24025.

Miscellaneous databases

GenomeRNAii 32498.
NextBioi 778773.
PROi Q24025.

Gene expression databases

Bgeei Q24025.
ExpressionAtlasi Q24025. differential.

Family and domain databases

InterProi IPR016353. Chordin.
IPR010895. CHRD.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF07452. CHRD. 4 hits.
PF00093. VWC. 4 hits.
[Graphical view ]
PIRSFi PIRSF002496. Chordin. 1 hit.
SMARTi SM00754. CHRD. 4 hits.
SM00214. VWC. 3 hits.
[Graphical view ]
PROSITEi PS50933. CHRD. 4 hits.
PS01208. VWFC_1. 2 hits.
PS50184. VWFC_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: FUNCTION, INTERACTION WITH DPP AND TSG.

Entry informationi

Entry nameiSOG_DROME
AccessioniPrimary (citable) accession number: Q24025
Secondary accession number(s): B7FNI9, Q9VXS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3