GenomeNet

Database: UniProt
Entry: Q24025
LinkDB: Q24025
Original site: Q24025 
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   08-MAY-2019, entry version 147.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL 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
RT   putative negative growth factor encoded by the short gastrulation
RT   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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   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
RT   antagonist Sog.";
RL   Dev. Biol. 346:1-10(2010).
CC   -!- FUNCTION: Putative negative growth factor (PubMed:7958919).
CC       Antagonist of dpp, a protein involved in patterning the dorsal
CC       region and in the development of the neuroectoderm; dpp inhibition
CC       is enhanced by tsg (PubMed:7958919). Required for establishment of
CC       a narrow stripe of peak levels of BMP signaling in the dorsal
CC       midline of early embryos, that will give rise to the amnioserosa
CC       (PubMed:11260716). {ECO:0000269|PubMed:11260716,
CC       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       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
CC       protein {ECO:0000305}. Cell membrane
CC       {ECO:0000269|PubMed:20599894}; Single-pass type I membrane protein
CC       {ECO:0000305}. Secreted {ECO:0000269|PubMed:20599894}.
CC   -!- TISSUE SPECIFICITY: Abuts the dorsal dpp-expressing cells in a
CC       lateral stripe 14-16 cells wide. Later in embryogenesis it is
CC       expressed in neuroectoderm and in the endoderm spaced along the
CC       anterior-posterior axis of the developing gut.
CC       {ECO:0000269|PubMed:7958919}.
CC   -!- DEVELOPMENTAL STAGE: Embryogenesis. {ECO:0000269|PubMed:7958919}.
CC   -!- PTM: Palmitoylated, probably by Hip14.
CC       {ECO:0000269|PubMed:20599894}.
CC   -!- SIMILARITY: Belongs to the chordin family. {ECO:0000305}.
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   SMR; Q24025; -.
DR   BioGrid; 58848; 29.
DR   DIP; DIP-20760N; -.
DR   IntAct; Q24025; 5.
DR   STRING; 7227.FBpp0304150; -.
DR   PaxDb; Q24025; -.
DR   PRIDE; Q24025; -.
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   eggNOG; ENOG410IEDE; Eukaryota.
DR   eggNOG; ENOG410XSBA; LUCA.
DR   InParanoid; Q24025; -.
DR   KO; K04657; -.
DR   OMA; RRVPRDY; -.
DR   OrthoDB; 647180at2759; -.
DR   PhylomeDB; Q24025; -.
DR   GenomeRNAi; 32498; -.
DR   PRO; PR:Q24025; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0003463; Expressed in 42 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q24025; baseline and differential.
DR   Genevisible; Q24025; DM.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; ISS: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; TAS:FlyBase.
DR   GO; GO:0030509; P:BMP signaling pathway; NAS:FlyBase.
DR   GO; GO:0007398; P:ectoderm development; TAS: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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:FlyBase.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; TAS:FlyBase.
DR   GO; GO:0061328; P:posterior Malpighian tubule development; IMP:FlyBase.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; TAS:FlyBase.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0035271; P:ring gland development; IMP:FlyBase.
DR   GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; NAS: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; Complete proteome; Developmental protein; Glycoprotein;
KW   Golgi apparatus; Growth factor; Growth regulation; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Repeat; Secreted;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1038       Dorsal-ventral patterning protein Sog.
FT                                /FTId=PRO_0000219089.
FT   TOPO_DOM      1     53       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     54     74       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     75   1038       Extracellular. {ECO:0000255}.
FT   DOMAIN      100    175       VWFC 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      197    337       CHRD 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00230}.
FT   DOMAIN      339    471       CHRD 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00230}.
FT   DOMAIN      474    588       CHRD 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00230}.
FT   DOMAIN      592    713       CHRD 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00230}.
FT   DOMAIN      742    804       VWFC 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      830    899       VWFC 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      939   1020       VWFC 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   CARBOHYD    179    179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    287    287       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    520    520       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    666    666       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    752    752       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    821    821       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   MUTAGEN      27     27       C->S: No change in baseline secretion but
FT                                eliminates increased secretion normally
FT                                caused by coexpression with Hip14 and
FT                                reduces intracellular levels of Sog.
FT                                {ECO:0000269|PubMed:20599894}.
FT   MUTAGEN      28     28       C->S: No effect on secretion when
FT                                coexpressed with Hip14.
FT                                {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
//
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