OBSTE_DROME
ID OBSTE_DROME Reviewed; 249 AA.
AC Q9VMM6; Q8IGU3; Q8T0V6;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein obstructor-E {ECO:0000303|PubMed:28076349};
DE Flags: Precursor;
GN Name=obst-E {ECO:0000303|PubMed:28076349, ECO:0000312|FlyBase:FBgn0031737};
GN ORFNames=CG11142 {ECO:0000312|FlyBase:FBgn0031737};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL39176.1, ECO:0000312|EMBL:AAN71355.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39176.1, ECO:0000312|EMBL:AAN71355.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAN71355.1}, and
RC Head {ECO:0000312|EMBL:AAL39176.1};
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] {ECO:0000312|EMBL:ACX47660.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION (ISOFORMS A AND B), SUBCELLULAR LOCATION (ISOFORM A), TISSUE
RP SPECIFICITY (ISOFORM A), AND DISRUPTION PHENOTYPE (ISOFORMS A AND B).
RX PubMed=28076349; DOI=10.1371/journal.pgen.1006548;
RA Tajiri R., Ogawa N., Fujiwara H., Kojima T.;
RT "Mechanical Control of Whole Body Shape by a Single Cuticular Protein
RT Obstructor-E in Drosophila melanogaster.";
RL PLoS Genet. 13:E1006548-E1006548(2017).
CC -!- FUNCTION: Chitin-binding protein that is important for the longitudinal
CC contraction and lateral expansion of the larval cuticle during its
CC conversion into the oval-shaped puparium case. Essential for survival
CC to the second instar larval stage. Confers the orientated contractility
CC and expandability of the larval cuticle by regulating the arrangement
CC of chitin and the formation of supracellular ridges on the cuticle of
CC third instar larvae. Essential for determining pupal body shape;
CC required for the orientated shape change of the cuticle during
CC metamorphosis which involves changes in the morphology of the
CC supracellular ridges. {ECO:0000269|PubMed:28076349}.
CC -!- FUNCTION: [Isoform A]: Mainly involved in regulating pupal shape.
CC {ECO:0000269|PubMed:28076349}.
CC -!- FUNCTION: [Isoform B]: Mainly involved in larvae survival, possibly by
CC maintaining the normal morphology of the larval hindgut during
CC development. {ECO:0000269|PubMed:28076349}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:28076349}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000303|PubMed:28076349, ECO:0000312|FlyBase:FBgn0031737};
CC IsoId=Q9VMM6-1; Sequence=Displayed;
CC Name=A {ECO:0000303|PubMed:28076349, ECO:0000312|FlyBase:FBgn0031737};
CC IsoId=Q9VMM6-2; Sequence=VSP_058877, VSP_058878, VSP_058879,
CC VSP_058880;
CC -!- TISSUE SPECIFICITY: [Isoform A]: Uniformly expressed throughout the
CC cuticle of third instar larva. {ECO:0000269|PubMed:28076349}.
CC -!- DISRUPTION PHENOTYPE: Larval lethal at the first instar stage. Hindgut
CC development during embryogenesis appears normal but at the first instar
CC larval stage the hindgut protrudes out of the anus and probably causes
CC the lethality. {ECO:0000269|PubMed:28076349}.
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DR EMBL; AE014134; AAF52287.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10555.1; -; Genomic_DNA.
DR EMBL; AY069031; AAL39176.1; -; mRNA.
DR EMBL; BT099959; ACX47660.1; -; mRNA.
DR EMBL; BT001600; AAN71355.1; -; mRNA.
DR RefSeq; NP_608957.1; NM_135113.3. [Q9VMM6-2]
DR RefSeq; NP_723116.1; NM_164659.3. [Q9VMM6-1]
DR AlphaFoldDB; Q9VMM6; -.
DR SMR; Q9VMM6; -.
DR IntAct; Q9VMM6; 4.
DR STRING; 7227.FBpp0078795; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR GlyGen; Q9VMM6; 1 site.
DR PaxDb; Q9VMM6; -.
DR DNASU; 33806; -.
DR EnsemblMetazoa; FBtr0079163; FBpp0078794; FBgn0031737. [Q9VMM6-2]
DR EnsemblMetazoa; FBtr0079164; FBpp0078795; FBgn0031737. [Q9VMM6-1]
DR GeneID; 33806; -.
DR KEGG; dme:Dmel_CG11142; -.
DR UCSC; CG11142-RA; d. melanogaster.
DR UCSC; CG11142-RB; d. melanogaster. [Q9VMM6-1]
DR CTD; 33806; -.
DR FlyBase; FBgn0031737; obst-E.
DR VEuPathDB; VectorBase:FBgn0031737; -.
DR eggNOG; ENOG502RXZX; Eukaryota.
DR HOGENOM; CLU_071682_2_1_1; -.
DR InParanoid; Q9VMM6; -.
DR OMA; AYTECLD; -.
DR PhylomeDB; Q9VMM6; -.
DR BioGRID-ORCS; 33806; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33806; -.
DR PRO; PR:Q9VMM6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031737; Expressed in second segment of antenna (Drosophila) and 16 other tissues.
DR ExpressionAtlas; Q9VMM6; baseline and differential.
DR GO; GO:0062129; C:chitin-based extracellular matrix; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IDA:FlyBase.
DR GO; GO:0008010; F:structural constituent of chitin-based larval cuticle; IDA:FlyBase.
DR GO; GO:0008011; F:structural constituent of pupal chitin-based cuticle; IDA:FlyBase.
DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR Pfam; PF01607; CBM_14; 3.
DR SMART; SM00494; ChtBD2; 3.
DR SUPFAM; SSF57625; SSF57625; 3.
DR PROSITE; PS50940; CHIT_BIND_II; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chitin-binding; Cuticle; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..249
FT /note="Protein obstructor-E"
FT /evidence="ECO:0000255"
FT /id="PRO_5009349125"
FT DOMAIN 22..80
FT /note="Chitin-binding type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 90..148
FT /note="Chitin-binding type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 170..227
FT /note="Chitin-binding type-2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 54..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 124..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 203..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT VAR_SEQ 20..50
FT /note="LGSPECPTPNGRFASGDQCDSYTECQDGTPV -> AAAAGACKEANGTAPVS
FT GSCDAYIECKNGVAE (in isoform A)"
FT /id="VSP_058877"
FT VAR_SEQ 60..123
FT /note="FHQRTKATGECTYAPYSTCKERARLQPANGTEECPRQFGFYPNGDATKCGVY
FT RNCAHGVASLTK -> YNEKSTGYPCGYPIDVECTQGQARLQAAQPTDECPHQFGYYRM
FT GDASHCGQFMNCAAGRGFVFD (in isoform A)"
FT /id="VSP_058878"
FT VAR_SEQ 130..136
FT /note="FNEETYQ -> WNPATYK (in isoform A)"
FT /id="VSP_058879"
FT VAR_SEQ 142..249
FT /note="LVESCNAEAYLGFNCPAADSADDSAAAAVDVSPEGELRYYRHPQTCKKYFVC
FT VNGHPRLYNCGKYLAFNSQTKLCDFYNKVPECYALLKEKQRLKAEKQQPQVAQPED ->
FT QVEDCDAEAFLGFRCPAPAPRSELLGEQEADYTFHPSQDNCQVYFICIEGRPRRIGCGE
FT DQAFNQELNQCDDIENVPNCSSAIREKGAQIKAARLHARKN (in isoform A)"
FT /id="VSP_058880"
FT CONFLICT 179
FT /note="R -> S (in Ref. 3; AAN71355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27480 MW; A8F9970D480B942C CRC64;
MAKILISALL CVAMFGSMAL GSPECPTPNG RFASGDQCDS YTECQDGTPV EKLCPDGLLF
HQRTKATGEC TYAPYSTCKE RARLQPANGT EECPRQFGFY PNGDATKCGV YRNCAHGVAS
LTKCPEGLAF NEETYQCDWP DLVESCNAEA YLGFNCPAAD SADDSAAAAV DVSPEGELRY
YRHPQTCKKY FVCVNGHPRL YNCGKYLAFN SQTKLCDFYN KVPECYALLK EKQRLKAEKQ
QPQVAQPED
