MSS4_DROME
ID MSS4_DROME Reviewed; 122 AA.
AC Q9VLP3; Q8IGQ8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Guanine nucleotide exchange factor MSS4 homolog {ECO:0000303|PubMed:28228250};
DE AltName: Full=Guanine nucleotide exchange factor stratum {ECO:0000303|PubMed:28228250};
GN Name=strat {ECO:0000303|PubMed:28228250, ECO:0000312|FlyBase:FBgn0032020};
GN ORFNames=CG7787 {ECO:0000312|FlyBase:FBgn0032020};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, INTERACTION WITH RAB8, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28228250; DOI=10.1016/j.celrep.2017.02.002;
RA Devergne O., Sun G.H., Schuepbach T.;
RT "Stratum, a Homolog of the Human GEF Mss4, Partnered with Rab8, Controls
RT the Basal Restriction of Basement Membrane Proteins in Epithelial Cells.";
RL Cell Rep. 18:1831-1839(2017).
CC -!- FUNCTION: Guanine-nucleotide-releasing protein that acts on members of
CC the sec4/ypt1/rab subfamily such as Rab8. During egg development,
CC essential for establishing and maintaining epithelial cell polarity by
CC regulating the correct polarized deposition of basal membrane (BM)
CC proteins such as trol/Pcan and vkg/Coll IV to the basal surface of
CC follicular epithelial (FE) cells. Likely to function by restricting the
CC activity of the vesicle transport regulator Rab8 to the basal membrane,
CC and thus directs BM protein-containing vesicles to the basal side of
CC the FE cells. This function is independent of the Crag/Rab10 regulation
CC of polarized BM protein secretion in the FE.
CC {ECO:0000269|PubMed:28228250}.
CC -!- SUBUNIT: Interacts with Rab8. {ECO:0000269|PubMed:28228250}.
CC -!- SUBCELLULAR LOCATION: Basal cell membrane
CC {ECO:0000269|PubMed:28228250}; Peripheral membrane protein
CC {ECO:0000269|PubMed:28228250}. Note=Diffuse intracellular localization
CC early in oogenesis which later becomes basally enriched in follicular
CC epithelial cells. {ECO:0000269|PubMed:28228250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in follicle cells results
CC in the apical localization of the basal membrane (BM) proteins trol and
CC vkg. Results in the apical secretion of vkg, which associates with the
CC apical plasma membrane with an adherent organization. No effect of the
CC localization of proteins involved in intracellular trafficking such as
CC aPKC, dlg and arm. {ECO:0000269|PubMed:28228250}.
CC -!- MISCELLANEOUS: The name stratum (strat) refers to the geological term
CC for a layer of rock as mutants accumulate basal membrane proteins as a
CC continuous apical sheet/layer. The name also highlights the similarity
CC of the mislocalization phenotype to Crag mutant cells, as both names
CC are based upon geological descriptions of rock formations.
CC {ECO:0000269|PubMed:28228250}.
CC -!- SIMILARITY: Belongs to the DSS4/MSS4 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01132}.
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DR EMBL; AE014134; AAF52641.2; -; Genomic_DNA.
DR EMBL; BT001655; AAN71410.1; -; mRNA.
DR RefSeq; NP_609209.2; NM_135365.3.
DR AlphaFoldDB; Q9VLP3; -.
DR SMR; Q9VLP3; -.
DR BioGRID; 60268; 29.
DR DIP; DIP-17817N; -.
DR IntAct; Q9VLP3; 7.
DR STRING; 7227.FBpp0079221; -.
DR PaxDb; Q9VLP3; -.
DR PRIDE; Q9VLP3; -.
DR DNASU; 34142; -.
DR EnsemblMetazoa; FBtr0079601; FBpp0079221; FBgn0032020.
DR GeneID; 34142; -.
DR KEGG; dme:Dmel_CG7787; -.
DR UCSC; CG7787-RA; d. melanogaster.
DR CTD; 34142; -.
DR FlyBase; FBgn0032020; strat.
DR VEuPathDB; VectorBase:FBgn0032020; -.
DR eggNOG; KOG4113; Eukaryota.
DR GeneTree; ENSGT00390000016889; -.
DR HOGENOM; CLU_132754_0_0_1; -.
DR InParanoid; Q9VLP3; -.
DR OMA; VPLMMQK; -.
DR OrthoDB; 1495679at2759; -.
DR PhylomeDB; Q9VLP3; -.
DR BioGRID-ORCS; 34142; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34142; -.
DR PRO; PR:Q9VLP3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032020; Expressed in adult abdomen and 26 other tissues.
DR ExpressionAtlas; Q9VLP3; baseline and differential.
DR Genevisible; Q9VLP3; DM.
DR GO; GO:0045180; C:basal cortex; IDA:FlyBase.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0061865; P:polarized secretion of basement membrane proteins in epithelium; IMP:FlyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IGI:FlyBase.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 2.170.150.10; -; 1.
DR InterPro; IPR007515; Mss4.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR011323; Mss4/transl-control_tumour.
DR PANTHER; PTHR13276; PTHR13276; 1.
DR Pfam; PF04421; Mss4; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51796; MSS4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..122
FT /note="Guanine nucleotide exchange factor MSS4 homolog"
FT /id="PRO_0000174178"
FT DOMAIN 9..120
FT /note="MSS4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
SQ SEQUENCE 122 AA; 14021 MW; 6FB717404CEDEE55 CRC64;
MTEEADFSEQ ITDGKNKSNV RCQFCNCLML KAQEGTYNQE EVDVPLMTQK QDRTADSLNS
EPLKDFWLVK DMMTFENIGF SNTVDGRKFL VCADCERGPV GYHDLSTRHC YLALKRVVHK
DT