BDL_DROME
ID BDL_DROME Reviewed; 719 AA.
AC Q9U4G1; C0PTX2; Q95U86; Q9VQY3;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein borderless {ECO:0000305};
DE Flags: Precursor;
GN Name=bdl {ECO:0000312|FlyBase:FBgn0028482};
GN ORFNames=CG16857 {ECO:0000312|FlyBase:FBgn0028482};
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;
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:AAD55430.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4] {ECO:0000312|EMBL:ACN58580.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-650.
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAL13474.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-719.
RC STRAIN=Berkeley; TISSUE=Head;
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 [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TUTL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24174674; DOI=10.1523/jneurosci.1878-13.2013;
RA Cameron S., Chang W.T., Chen Y., Zhou Y., Taran S., Rao Y.;
RT "Visual circuit assembly requires fine tuning of the novel Ig transmembrane
RT protein Borderless.";
RL J. Neurosci. 33:17413-17421(2013).
CC -!- FUNCTION: In the developing eye, has a role in axonal targeting of the
CC R7 photoreceptor where it functions together with tutl. Probably
CC mediates homotypic cell adhesion; the effect is inhibited by Lar.
CC {ECO:0000269|PubMed:24174674}.
CC -!- SUBUNIT: Interacts with tutl. {ECO:0000269|PubMed:24174674}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:24174674}.
CC -!- TISSUE SPECIFICITY: In the visual system, expressed in lamina and
CC medulla (at protein level). {ECO:0000269|PubMed:24174674}.
CC -!- DEVELOPMENTAL STAGE: During the mid-pupal stage, strongly expressed in
CC the lamina, medulla and inner optic lobe of the developing eye.
CC Specifically detected in R7 and R8 axonal terminals in the medulla.
CC {ECO:0000269|PubMed:24174674}.
CC -!- DISRUPTION PHENOTYPE: In the eye, axonal targeting of the R1-R6, R7 and
CC R8 cells appears to be normal. Double knockouts of bdl and tutl rescue
CC the R7 axonal tiling defect of tutl mutants. Double knockouts of bdl
CC and Lar partly rescue the R7 axonal targeting defect of Lar mutants.
CC {ECO:0000269|PubMed:24174674}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13474.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF51028.2; -; Genomic_DNA.
DR EMBL; AF181644; AAD55430.1; -; mRNA.
DR EMBL; BT071817; ACN58580.1; -; mRNA.
DR EMBL; AY058245; AAL13474.1; ALT_INIT; mRNA.
DR RefSeq; NP_608822.1; NM_134978.3.
DR AlphaFoldDB; Q9U4G1; -.
DR SMR; Q9U4G1; -.
DR STRING; 7227.FBpp0077115; -.
DR PaxDb; Q9U4G1; -.
DR PRIDE; Q9U4G1; -.
DR EnsemblMetazoa; FBtr0077425; FBpp0077115; FBgn0028482.
DR GeneID; 33635; -.
DR KEGG; dme:Dmel_CG16857; -.
DR UCSC; CG16857-RA; d. melanogaster.
DR CTD; 33635; -.
DR FlyBase; FBgn0028482; bdl.
DR VEuPathDB; VectorBase:FBgn0028482; -.
DR eggNOG; KOG3510; Eukaryota.
DR HOGENOM; CLU_008130_1_0_1; -.
DR InParanoid; Q9U4G1; -.
DR OMA; YIVHWSK; -.
DR OrthoDB; 291729at2759; -.
DR PhylomeDB; Q9U4G1; -.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-210991; Basigin interactions.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-376172; DSCAM interactions.
DR Reactome; R-DME-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR Reactome; R-DME-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-DME-70268; Pyruvate metabolism.
DR Reactome; R-DME-9749641; Aspirin ADME.
DR BioGRID-ORCS; 33635; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33635; -.
DR PRO; PR:Q9U4G1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028482; Expressed in second segment of antenna (Drosophila) and 14 other tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IPI:FlyBase.
DR GO; GO:0008366; P:axon ensheathment; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0098930; P:axonal transport; IMP:FlyBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0042065; P:glial cell growth; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:FlyBase.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR10075; PTHR10075; 3.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..719
FT /note="Protein borderless"
FT /evidence="ECO:0000255"
FT /id="PRO_5006752482"
FT TOPO_DOM 34..650
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 40..128
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 134..241
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 246..334
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 341..429
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 434..527
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 555..646
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 685..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 55..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 267..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 363..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 719 AA; 81213 MW; 0908862B242343D1 CRC64;
MPAKRSRTFR QSGSALLALL AIILLMNISC TSAARDHRRQ TNLEAKVGSH VVFNCYIDFP
FDAPIPYLVH WTKDNKKIFT WYEQETSTSE LFNGRLHLVE NHPEFGRASV NLTAIRESDQ
GWYHCQVSFP NRSPSVRNNG TAYHLAVQGG SLIRIPPVNQ TIREGQTAFF HCVMKHPENS
QASWYKDGVL LQEVQDLVRR FYMGPDGSLS IDPTMMSDLG EYECKVRNSD GELQTAKAFL
NIQYKAKVIY APPEVFLPYG QPAVLDCHFR ANPPLKNLRW EKDGLLFDSY NVPGVFYKMN
GSLFFAKVDE NHAGSYTCTP YNDLGTDGPS PVISVIVLRP PIFSVTPKAI YIQKLGEAAE
LPCEAIDRDG NNRPSIIWGR KDGQPLPADR FSLSGGNLTI TGLVEGDRGI YECSATNEAA
TITAEAELMI ENIAPRAPYN LTANSTETCI TIRWQPGYLR PNLEYTVWYR LMEAPEWRTL
RVLDKKVMEA TVQHLQPGKE YEFMVLSQDK YGDGMFSKQF RFQTLPSPIR ADDFDAQQLQ
HDLGQVTAPA GGLGAPWNLT AISNQQGWLL HWEHPVQGLE GLRLYAVRWW KEPEHFLIGH
AETFDNYYQL RHLKEDTLFK VQVLAVGTET QQSVPSHELL IDVPSQRKVR ALIIGSSVGV
IFLLCALCAF LYVKRSCLRH LFAKDSSASE DEDTAESGDC DSDEQDQRDR DSIKIRQST
