LACH_DROME
ID LACH_DROME Reviewed; 359 AA.
AC Q24372; Q86PE5; Q8ML12; Q9V6C2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Lachesin;
DE Flags: Precursor;
GN Name=Lac; ORFNames=CG12369;
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, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8223276; DOI=10.1242/dev.118.2.509;
RA Karlstrom R.O., Wilder L.P., Bastiani M.J.;
RT "Lachesin: an immunoglobulin superfamily protein whose expression
RT correlates with neurogenesis in grasshopper embryos.";
RL Development 118:509-522(1993).
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 PARTIAL 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; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=14681183; DOI=10.1242/dev.00917;
RA Llimargas M., Strigini M., Katidou M., Karagogeos D., Casanova J.;
RT "Lachesin is a component of a septate junction-based mechanism that
RT controls tube size and epithelial integrity in the Drosophila tracheal
RT system.";
RL Development 131:181-190(2004).
CC -!- FUNCTION: Required for normal tracheal development and maintenance of
CC the trans-epithelial diffusion barrier. Functions as a homophilic cell-
CC adhesion molecule. May play a role in early neuronal differentiation
CC and axon outgrowth. {ECO:0000269|PubMed:14681183,
CC ECO:0000269|PubMed:8223276}.
CC -!- INTERACTION:
CC Q24372; Q9VGH2: 6959; NbExp=2; IntAct=EBI-221813, EBI-6896902;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14681183,
CC ECO:0000269|PubMed:8223276}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:14681183, ECO:0000269|PubMed:8223276};
CC Extracellular side {ECO:0000269|PubMed:14681183,
CC ECO:0000269|PubMed:8223276}. Note=Located at the extracellular face of
CC the membrane and becomes associated with septate junctions.
CC -!- TISSUE SPECIFICITY: Expressed on differentiating neuronal cells from
CC the onset of neurogenesis in both the central and peripheral nervous
CC systems. First detected in the cellularized blastoderm, apart from in
CC the ventral side. Expression persists uniformly in the early ectoderm
CC until the end of gastrulation. From stage 10, expressed in an
CC alternating strong/weak pattern in each segment until stage 15 when it
CC disappears. From stage 11, expressed in subsets of neurons and later
CC subsets of glial cells. From early stage 13, strongly expressed in
CC trachea, hindgut, foregut and the nervous system.
CC {ECO:0000269|PubMed:14681183}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC {ECO:0000269|PubMed:14681183, ECO:0000269|PubMed:8223276}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit more sinuous tracheal branches and
CC uneven lumen with numerous breaks in the dorsal and lateral branches.
CC {ECO:0000269|PubMed:14681183}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO24932.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; L13255; AAC37184.1; -; mRNA.
DR EMBL; AE013599; AAF58506.1; -; Genomic_DNA.
DR EMBL; AY051829; AAK93253.1; -; mRNA.
DR EMBL; BT003177; AAO24932.1; ALT_SEQ; mRNA.
DR RefSeq; NP_523713.2; NM_078989.3.
DR AlphaFoldDB; Q24372; -.
DR SMR; Q24372; -.
DR BioGRID; 62140; 7.
DR IntAct; Q24372; 36.
DR STRING; 7227.FBpp0087044; -.
DR GlyGen; Q24372; 2 sites.
DR PaxDb; Q24372; -.
DR PRIDE; Q24372; -.
DR DNASU; 36363; -.
DR EnsemblMetazoa; FBtr0087933; FBpp0087044; FBgn0010238.
DR GeneID; 36363; -.
DR KEGG; dme:Dmel_CG12369; -.
DR CTD; 36363; -.
DR FlyBase; FBgn0010238; Lac.
DR VEuPathDB; VectorBase:FBgn0010238; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000174385; -.
DR HOGENOM; CLU_027228_4_0_1; -.
DR InParanoid; Q24372; -.
DR OMA; INNLWHA; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q24372; -.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-419037; NCAM1 interactions.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR SignaLink; Q24372; -.
DR BioGRID-ORCS; 36363; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36363; -.
DR PRO; PR:Q24372; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010238; Expressed in second segment of antenna (Drosophila) and 82 other tissues.
DR ExpressionAtlas; Q24372; baseline and differential.
DR Genevisible; Q24372; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0005918; C:septate junction; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IMP:FlyBase.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR Gene3D; 2.60.40.10; -; 3.
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 Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Developmental protein; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..336
FT /note="Lachesin"
FT /id="PRO_0000014810"
FT PROPEP 337..359
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014811"
FT DOMAIN 29..130
FT /note="Ig-like V-type"
FT DOMAIN 135..221
FT /note="Ig-like C2-type 1"
FT DOMAIN 226..317
FT /note="Ig-like C2-type 2"
FT LIPID 336
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 247..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 244
FT /note="D -> Y (in Ref. 5; AAO24932)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="L -> S (in Ref. 1; AAC37184)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="A -> R (in Ref. 1; AAC37184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39939 MW; 12F513E2B9C156F4 CRC64;
MWRPSISNCV WSTLLLAIFV QQTLAQRTPT ISYITQEQIK DIGGTVEFDC SVQYAKEYNV
LFLKTDSDPV FLSTGSTLVI KDSRFSLRYD PNSSTYKLQI KDIQETDAGT YTCQVVISTV
HKVSAEVKLS VRRPPVISDN STQSVVASEG SEVQMECYAS GYPTPTITWR RENNAILPTD
SATYVGNTLR IKSVKKEDRG TYYCVADNGV SKGDRRNINV EVEFAPVITV PRPRLGQALQ
YDMDLECHIE AYPPPAIVWT KDDIQLANNQ HYSISHFATA DEYTDSTLRV ITVEKRQYGD
YVCKATNRFG EAEARVNLFE TIIPVCPPAC GQAYIAGAED VSATSFALVG ILAALLFAR
