DISP_DROME
ID DISP_DROME Reviewed; 1218 AA.
AC Q9VNJ5; B6IDI9; Q5U173; Q8SY40; Q9U477;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein dispatched;
GN Name=disp; ORFNames=CG2019;
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10619433; DOI=10.1016/s0092-8674(00)81677-3;
RA Burke R., Nellen D., Bellotto M., Hafen E., Senti K.-A., Dickson B.J.,
RA Basler K.;
RT "Dispatched, a novel sterol-sensing domain protein dedicated to the release
RT of cholesterol-modified hedgehog from signaling cells.";
RL Cell 99:803-815(1999).
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; 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 [5]
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 (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 516-ASP-ASP-517 AND ASP-1030.
RX PubMed=12372301; DOI=10.1016/s0092-8674(02)00977-7;
RA Ma Y., Erkner A., Gong R., Yao S., Taipale J., Basler K., Beachy P.A.;
RT "Hedgehog-mediated patterning of the mammalian embryo requires transporter-
RT like function of dispatched.";
RL Cell 111:63-75(2002).
RN [7]
RP FUNCTION.
RX PubMed=12586063; DOI=10.1016/s1534-5807(03)00031-5;
RA Gallet A., Rodriguez R., Ruel L., Therond P.P.;
RT "Cholesterol modification of hedgehog is required for trafficking and
RT movement, revealing an asymmetric cellular response to hedgehog.";
RL Dev. Cell 4:191-204(2003).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-388, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Segment polarity protein which functions in hedgehog (Hh)
CC signaling. Regulates the trafficking and the release of cholesterol-
CC modified hedgehog protein from cells of the posterior compartment (P
CC cells) and is hence required for the effective production of the Hh
CC signal. {ECO:0000269|PubMed:10619433, ECO:0000269|PubMed:12372301,
CC ECO:0000269|PubMed:12586063}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout the embryo and
CC the imaginal discs. {ECO:0000269|PubMed:10619433}.
CC -!- DISRUPTION PHENOTYPE: Death during embryogenesis with a strong segment-
CC polarity phenotype. {ECO:0000269|PubMed:10619433}.
CC -!- SIMILARITY: Belongs to the dispatched family. {ECO:0000305}.
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DR EMBL; AF200691; AAF23397.1; -; mRNA.
DR EMBL; AE014297; AAF51938.1; -; Genomic_DNA.
DR EMBL; AY075394; AAL68228.1; -; mRNA.
DR EMBL; BT016019; AAV36904.1; -; mRNA.
DR EMBL; BT050429; ACJ13136.1; -; mRNA.
DR RefSeq; NP_524734.2; NM_079995.3.
DR PDB; 6TBU; EM; 3.16 A; A=1-1218.
DR PDB; 6TD6; EM; 4.76 A; A=1-1218.
DR PDBsum; 6TBU; -.
DR PDBsum; 6TD6; -.
DR AlphaFoldDB; Q9VNJ5; -.
DR SMR; Q9VNJ5; -.
DR BioGRID; 68938; 4.
DR IntAct; Q9VNJ5; 1.
DR STRING; 7227.FBpp0078314; -.
DR TCDB; 2.A.6.9.1; the resistance-nodulation-cell division (rnd) superfamily.
DR GlyGen; Q9VNJ5; 9 sites.
DR iPTMnet; Q9VNJ5; -.
DR PaxDb; Q9VNJ5; -.
DR PRIDE; Q9VNJ5; -.
DR DNASU; 44274; -.
DR EnsemblMetazoa; FBtr0078665; FBpp0078314; FBgn0029088.
DR GeneID; 44274; -.
DR KEGG; dme:Dmel_CG2019; -.
DR UCSC; CG2019-RA; d. melanogaster.
DR CTD; 44274; -.
DR FlyBase; FBgn0029088; disp.
DR VEuPathDB; VectorBase:FBgn0029088; -.
DR eggNOG; KOG3664; Eukaryota.
DR GeneTree; ENSGT00940000168705; -.
DR HOGENOM; CLU_004076_0_0_1; -.
DR InParanoid; Q9VNJ5; -.
DR OMA; NGLLAMC; -.
DR OrthoDB; 1156918at2759; -.
DR PhylomeDB; Q9VNJ5; -.
DR Reactome; R-DME-209471; Formation and transport of the N-HH ligand.
DR SignaLink; Q9VNJ5; -.
DR BioGRID-ORCS; 44274; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 44274; -.
DR PRO; PR:Q9VNJ5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0029088; Expressed in mouthpart and 21 other tissues.
DR Genevisible; Q9VNJ5; DM.
DR GO; GO:0035230; C:cytoneme; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; TAS:FlyBase.
DR GO; GO:0007225; P:patched ligand maturation; IDA:FlyBase.
DR GO; GO:0007280; P:pole cell migration; IGI:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0035222; P:wing disc pattern formation; IMP:FlyBase.
DR InterPro; IPR030223; Dispatched.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR PANTHER; PTHR45951:SF3; PTHR45951:SF3; 1.
DR Pfam; PF02460; Patched; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1218
FT /note="Protein dispatched"
FT /id="PRO_0000310699"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 670..690
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 975..995
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1058..1078
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1087..1107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 430..624
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 99..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..122
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 883
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 891
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 516..517
FT /note="DD->AA: Loss of function; when associated with A-
FT 1030."
FT /evidence="ECO:0000269|PubMed:12372301"
FT MUTAGEN 516..517
FT /note="DD->NN: Loss of function; when associated with N-
FT 1030."
FT /evidence="ECO:0000269|PubMed:12372301"
FT MUTAGEN 1030
FT /note="D->A: Loss of function; when associated with 516-A-
FT A-517."
FT /evidence="ECO:0000269|PubMed:12372301"
FT MUTAGEN 1030
FT /note="D->N: Loss of function; when associated with 517-N-
FT N-517."
FT /evidence="ECO:0000269|PubMed:12372301"
FT CONFLICT 727
FT /note="L -> W (in Ref. 1; AAF23397)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="D -> G (in Ref. 4; AAV36904)"
FT /evidence="ECO:0000305"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 20..41
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 397..404
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 424..432
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 436..466
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 469..491
FT /evidence="ECO:0007829|PDB:6TBU"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 502..513
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 516..530
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 559..587
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 594..628
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 649..668
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 671..689
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 710..716
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 734..740
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 771..784
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 802..811
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 837..853
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 863..867
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 898..911
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 916..934
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 945..949
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 951..981
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 985..1009
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 1015..1040
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 1047..1076
FT /evidence="ECO:0007829|PDB:6TBU"
FT STRAND 1078..1081
FT /evidence="ECO:0007829|PDB:6TBU"
FT HELIX 1082..1113
FT /evidence="ECO:0007829|PDB:6TBU"
SQ SEQUENCE 1218 AA; 138979 MW; 8214042F61156B63 CRC64;
MLCFDSERMN WYYHVLARRP YLVVVSIAVY CVACIIVALV LNKLPDFSDP TLGFETRGTK
IGERLTAWYN LLQETDHHGA LFSNPSDLWE RRRVEQGYVE TKLHPNHRRR KNKHKNRNKN
KRRKEQNQSS HEHHDVAQKM MQFKKRLKAT SSPSPNLGFD TWIGDSGVFR DYEITNDSAS
SSLEPTRRTE QIEYGHNTTS VDEEEHQQRV QTKKSTWRLL KQAATLPTDG WADMHRRQPI
EGFFCDSSPR KEYSHFVVQR IGPNATDSLF DLNGLLAMCQ LQDQITEVPS YRAFCEPEML
TTECCRPWSL PNYAAMLANK SSCFDLTTED VTSLHTLLLG CYEYFHDLKM DNHCNEIPHC
RAPEECKRLN IVFNVLNFLT DFSFIKSNDS NVYLKYAMIF IPVAQSNRLL PLFHEWEDVE
LINELVEVVA MDLGLENELF NELLLTDVWL VSLGGTFVMA SVWLYTGSAF ITLMSCVAIC
FSLGLAYFFY AIVLEFEFFP YMNLLAVVVI IGIGADDVFL FLKIWHCVLT ERFSNRCTLT
TQSQSALPTL ENSDHTESLE NIMALTMRHA AASMFVTSLT TAGAFYASYS SSITAIKCFG
IFAGTVVVTN YLLMITWLPA SVSIMERLFA TRMSCHHPMS IKLIHACKKS INRFCQMFEE
CITKSIMNYA YLWLLIFGAL GASSAVIVFW YPGLQLPEKS HFQLFVSKHP FEVYSSLKQQ
FWFEKPLQAY ENFKMHMHFV WGVQAVDDGD YTNPNSYGHL HYDNNFNVSS RPAQLWILDF
CQSVRQQPFY KETLGMLLPN CFIENLIDYM KRRCIDDMDS TRKDRSPCCD AQFPFEPHIF
EYCLPQSISN MYDTTFFRPG VAGPKFAEAP RLETEDYLGM SGNESAEYST NGSFTPLLVK
ALVIEFESNV AYSTIYANIR QFYESVEHWF QMQLKTAPPE LQGGWFTSDL KFYNVQDTLS
HDTFVAICLA MAASLAVLLC FTVNILISIY AVLTVSLSIF NTVAVLILLG WQLNILESIA
VSTAIGLAVD FSLHYGIHYR MSPVKERLAA TQFVLSRIIG PTVMAATTTG LAGGIMMASN
ILPYIQIGVF LVVVMIVSWF YATFFLMSLL RVAGPQHGFL ELKWPLWSKR SSGSSKFYER
KPSQVIASEQ LLTPTSSAIV ELANSETHEL ESLNSNSLIK TISGIESAHA LSSLPRDFEH
SFQTMHECKY QTYPSTSN
