SOG_DROME
ID SOG_DROME Reviewed; 1038 AA.
AC Q24025; B7FNI9; Q9VXS7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Dorsal-ventral patterning protein Sog;
DE AltName: Full=Short gastrulation protein;
GN Name=sog; ORFNames=CG9224;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=7958919; DOI=10.1101/gad.8.21.2602;
RA Francois V., Solloway M., O'Neill J.W., Emery J., Bier E.;
RT "Dorsal-ventral patterning of the Drosophila embryo depends on a putative
RT negative growth factor encoded by the short gastrulation gene.";
RL Genes Dev. 8:2602-2616(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH DPP AND TSG.
RX PubMed=11260716; DOI=10.1038/35068578;
RA Ross J.J., Shimmi O., Vilmos P., Petryk A., Kim H., Gaudenz K.,
RA Hermanson S., Ekker S.C., O'Connor M.B., Marsh J.L.;
RT "Twisted gastrulation is a conserved extracellular BMP antagonist.";
RL Nature 410:479-483(2001).
RN [6]
RP INTERACTION WITH HIP14, SUBCELLULAR LOCATION, PALMITOYLATION, AND
RP MUTAGENESIS OF CYS-27 AND CYS-28.
RX PubMed=20599894; DOI=10.1016/j.ydbio.2010.06.024;
RA Kang K.H., Bier E.;
RT "dHIP14-dependent palmitoylation promotes secretion of the BMP antagonist
RT Sog.";
RL Dev. Biol. 346:1-10(2010).
CC -!- FUNCTION: Putative negative growth factor (PubMed:7958919). Antagonist
CC of dpp, a protein involved in patterning the dorsal region and in the
CC development of the neuroectoderm; dpp inhibition is enhanced by tsg
CC (PubMed:7958919). Required for establishment of a narrow stripe of peak
CC levels of BMP signaling in the dorsal midline of early embryos, that
CC will give rise to the amnioserosa (PubMed:11260716).
CC {ECO:0000269|PubMed:11260716, ECO:0000269|PubMed:7958919}.
CC -!- SUBUNIT: Component of a complex composed of dpp, sog and tsg
CC (PubMed:11260716). Interacts with palmitoyltransferase Hip14
CC (PubMed:20599894). {ECO:0000269|PubMed:11260716,
CC ECO:0000269|PubMed:20599894}.
CC -!- INTERACTION:
CC Q24025; O18407: vkg; NbExp=2; IntAct=EBI-184947, EBI-15721782;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:20599894}; Single-pass type II membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:20599894}; Single-pass
CC type I membrane protein {ECO:0000305}. Secreted
CC {ECO:0000269|PubMed:20599894}.
CC -!- TISSUE SPECIFICITY: Abuts the dorsal dpp-expressing cells in a lateral
CC stripe 14-16 cells wide. Later in embryogenesis it is expressed in
CC neuroectoderm and in the endoderm spaced along the anterior-posterior
CC axis of the developing gut. {ECO:0000269|PubMed:7958919}.
CC -!- DEVELOPMENTAL STAGE: Embryogenesis. {ECO:0000269|PubMed:7958919}.
CC -!- PTM: Palmitoylated, probably by Hip14. {ECO:0000269|PubMed:20599894}.
CC -!- SIMILARITY: Belongs to the chordin family. {ECO:0000305}.
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DR EMBL; U18774; AAA89117.1; -; mRNA.
DR EMBL; AE014298; AAF48481.1; -; Genomic_DNA.
DR EMBL; BT053679; ACK77594.1; -; mRNA.
DR PIR; T13177; T13177.
DR RefSeq; NP_001259576.1; NM_001272647.2.
DR RefSeq; NP_001259578.1; NM_001272649.2.
DR RefSeq; NP_476736.1; NM_057388.4.
DR AlphaFoldDB; Q24025; -.
DR BioGRID; 58848; 30.
DR DIP; DIP-20760N; -.
DR IntAct; Q24025; 5.
DR STRING; 7227.FBpp0304150; -.
DR GlyGen; Q24025; 6 sites.
DR PaxDb; Q24025; -.
DR DNASU; 32498; -.
DR EnsemblMetazoa; FBtr0074063; FBpp0073879; FBgn0003463.
DR EnsemblMetazoa; FBtr0331760; FBpp0304148; FBgn0003463.
DR EnsemblMetazoa; FBtr0340346; FBpp0309304; FBgn0003463.
DR GeneID; 32498; -.
DR KEGG; dme:Dmel_CG9224; -.
DR CTD; 32498; -.
DR FlyBase; FBgn0003463; sog.
DR VEuPathDB; VectorBase:FBgn0003463; -.
DR eggNOG; ENOG502QR4J; Eukaryota.
DR HOGENOM; CLU_008477_0_0_1; -.
DR InParanoid; Q24025; -.
DR OMA; CCKSCPG; -.
DR OrthoDB; 647180at2759; -.
DR PhylomeDB; Q24025; -.
DR SignaLink; Q24025; -.
DR BioGRID-ORCS; 32498; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32498; -.
DR PRO; PR:Q24025; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003463; Expressed in central brain anlage (Drosophila) and 48 other tissues.
DR ExpressionAtlas; Q24025; baseline and differential.
DR Genevisible; Q24025; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036122; F:BMP binding; IDA:FlyBase.
DR GO; GO:0005518; F:collagen binding; IDA:FlyBase.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007378; P:amnioserosa formation; IMP:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR GO; GO:0035592; P:establishment of protein localization to extracellular region; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007313; P:maternal specification of dorsal/ventral axis, oocyte, soma encoded; IMP:FlyBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:FlyBase.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:FlyBase.
DR GO; GO:0061328; P:posterior Malpighian tubule development; IMP:FlyBase.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0110107; P:regulation of imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0035271; P:ring gland development; IMP:FlyBase.
DR GO; GO:0038098; P:sequestering of BMP from receptor via BMP binding; IDA:FlyBase.
DR InterPro; IPR016353; Chordin.
DR InterPro; IPR010895; CHRD.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF07452; CHRD; 2.
DR Pfam; PF00093; VWC; 4.
DR PIRSF; PIRSF002496; Chordin; 1.
DR SMART; SM00754; CHRD; 4.
DR SMART; SM00214; VWC; 4.
DR PROSITE; PS50933; CHRD; 4.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Glycoprotein; Golgi apparatus;
KW Growth factor; Growth regulation; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1038
FT /note="Dorsal-ventral patterning protein Sog"
FT /id="PRO_0000219089"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..1038
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 100..175
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 197..337
FT /note="CHRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 339..471
FT /note="CHRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 474..588
FT /note="CHRD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 592..713
FT /note="CHRD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 742..804
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 830..899
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 939..1020
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 27
FT /note="C->S: No change in baseline secretion but eliminates
FT increased secretion normally caused by coexpression with
FT Hip14 and reduces intracellular levels of Sog."
FT /evidence="ECO:0000269|PubMed:20599894"
FT MUTAGEN 28
FT /note="C->S: No effect on secretion when coexpressed with
FT Hip14."
FT /evidence="ECO:0000269|PubMed:20599894"
SQ SEQUENCE 1038 AA; 115515 MW; B0E833AFD79A9037 CRC64;
MANKLRKSNA IEWATATGTV PLLERSCCHS EDAALEPQAS KTSHREQAPI LRHLSQLSHL
LIIAGLLIVC LAGVTEGRRH APLMFEESDT GRRSNRPAVT ECQFGKVLRE LGSTWYADLG
PPFGVMYCIK CECVAIPKKR RIVARVQCRN IKNECPPAKC DDPISLPGKC CKTCPGDRND
TDVALDVPVP NEEEERNMKH YAALLTGRTS YFLKGEEMKS MYTTYNPQNV VATARFLFHK
KNLYYSFYTS SRIGRPRAIQ FVDDAGVILE EHQLETTLAG TLSVYQNATG KICGVWRRVP
RDYKRILRDD RLHVVLLWGN KQQAELALAG KVAKYTALQT ELFSSLLEAP LPDGKTDPQL
AGAGGTAIVS TSSGAASSMH LTLVFNGVFG AEEYADAALS VKIELAERKE VIFDEIPRVR
KPSAEINVLE LSSPISIQNL RLMSRGKLLL TVESKKYPHL RIQGHIVTRA SCEIFQTLLA
PHSAESSTKS SGLAWVYLNT DGSLAYNIET EHVNTRDRPN ISLIEEQGKR KAKLEDLTPS
FNFNQAIGSV EKLGPKVLES LYAGELGVNV ATEHETSLIR GRLVPRPVAD ARDSAEPILL
KRQEHTDAQN PHAVGMAWMS IDNECNLHYE VTLNGVPAQD LQLYLEEKPI EAIGAPVTRK
LLEEFNGSYL EGFFLSMPSA ELIKLEMSVC YLEVHSKHSK QLLLRGKLKS TKVPGHCFPV
YTDNNVPVPG DHNDNHLVNG ETKCFHSGRF YNESEQWRSA QDSCQMCACL RGQSSCEVIK
CPALKCKSTE QLLQRDGECC PSCVPKKEAA DYSAQSSPAT NATDLLQQRR GCRLGEQFHP
AGASWHPFLP PNGFDTCTTC SCDPLTLEIR CPRLVCPPLQ CSEKLAYRPD KKACCKICPE
GKQSSSNGHK TTPNNPNVLQ DQAMQRSPSH SAEEVLANGG CKVVNKVYEN GQEWHPILMS
HGEQKCIKCR CKDSKVNCDR KRCSRSTCQQ QTRVTSKRRL FEKPDAAAPA IDECCSTQCR
RSRRHHKRQP HHQQRSSS
