CONT_DROME
ID CONT_DROME Reviewed; 1390 AA.
AC Q9VN14; Q5BI91; Q8SWW3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Contactin;
DE Flags: Precursor;
GN Name=Cont; ORFNames=CG1084;
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, TISSUE
RP SPECIFICITY, GPI-ANCHOR, GLYCOSYLATION, AND IDENTIFICATION IN A COMPLEX
RP WITH NRX AND NRG.
RC STRAIN=Oregon-R; TISSUE=Larva;
RX PubMed=15459097; DOI=10.1242/dev.01372;
RA Faivre-Sarrailh C., Banerjee S., Li J., Hortsch M., Laval M., Bhat M.A.;
RT "Drosophila contactin, a homolog of vertebrate contactin, is required for
RT septate junction organization and paracellular barrier function.";
RL Development 131:4931-4942(2004).
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;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-1390.
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-912 AND ASN-1307, AND
RP IDENTIFICATION BY MASS 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).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-369 AND ASN-912, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Required for organization of septate junctions and
CC paracellular barrier functions. Septate junctions, which are the
CC equivalent of vertebrates tight junctions, are characterized by regular
CC arrays of transverse structures that span the intermembrane space and
CC form a physical barrier to diffusion. {ECO:0000269|PubMed:15459097}.
CC -!- SUBUNIT: Forms a complex with Nrg and Nrx.
CC {ECO:0000269|PubMed:15459097}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15459097};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15459097}. Cell junction,
CC septate junction {ECO:0000269|PubMed:15459097}. Note=Component of
CC epithelial septate junctions. Nrx is required for its cell surface
CC localization.
CC -!- TISSUE SPECIFICITY: Expressed in ectodermally derived epithelial cells
CC from stage 12. All these tissues, such as epidermis, hindgut, foregut,
CC salivary glands and trachea, which contain pleated septate junctions.
CC Expressed by ectodermally derived epithelial cells and along peripheral
CC nerves. Not present in midline glial cells. Expressed in epithelial
CC cells and glial cells of peripheral nerves.
CC {ECO:0000269|PubMed:15459097}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15459097,
CC ECO:0000269|PubMed:17893096, ECO:0000269|PubMed:19349973}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11368.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY229991; AAP44004.1; -; mRNA.
DR EMBL; AE014297; AAF52137.2; -; Genomic_DNA.
DR EMBL; BT021333; AAX33481.1; -; mRNA.
DR EMBL; AY095040; AAM11368.1; ALT_INIT; mRNA.
DR RefSeq; NP_649461.2; NM_141204.4.
DR AlphaFoldDB; Q9VN14; -.
DR SMR; Q9VN14; -.
DR BioGRID; 65773; 7.
DR IntAct; Q9VN14; 1.
DR STRING; 7227.FBpp0078557; -.
DR GlyGen; Q9VN14; 12 sites.
DR iPTMnet; Q9VN14; -.
DR PaxDb; Q9VN14; -.
DR PRIDE; Q9VN14; -.
DR DNASU; 40553; -.
DR EnsemblMetazoa; FBtr0078917; FBpp0078557; FBgn0037240.
DR GeneID; 40553; -.
DR KEGG; dme:Dmel_CG1084; -.
DR UCSC; CG1084-RA; d. melanogaster.
DR CTD; 40553; -.
DR FlyBase; FBgn0037240; Cont.
DR VEuPathDB; VectorBase:FBgn0037240; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000170323; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q9VN14; -.
DR OMA; KICKAYT; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q9VN14; -.
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; 40553; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40553; -.
DR PRO; PR:Q9VN14; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037240; Expressed in eye disc (Drosophila) and 42 other tissues.
DR ExpressionAtlas; Q9VN14; baseline and differential.
DR Genevisible; Q9VN14; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0005918; C:septate junction; IDA:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0008366; P:axon ensheathment; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IC:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0021682; P:nerve maturation; IMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
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; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR10075; PTHR10075; 4.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1362
FT /note="Contactin"
FT /id="PRO_0000014703"
FT PROPEP 1363..1390
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014704"
FT DOMAIN 362..463
FT /note="Ig-like C2-type 1"
FT DOMAIN 468..561
FT /note="Ig-like C2-type 2"
FT DOMAIN 576..656
FT /note="Ig-like C2-type 3"
FT DOMAIN 661..745
FT /note="Ig-like C2-type 4"
FT DOMAIN 756..843
FT /note="Ig-like C2-type 5"
FT DOMAIN 848..939
FT /note="Ig-like C2-type 6"
FT DOMAIN 946..1048
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1053..1151
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1156..1254
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1259..1357
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 25..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1362
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 388..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 489..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 593..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 682..734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 779..827
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 870..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1390 AA; 158239 MW; C4292F60B8B5F0F6 CRC64;
MLAKIGLLAS ILVLNLVGQI TPQFSENLPD PDPQSGQQPQ NYQPSYNKDY SPRYNPLYTG
QQSADPNQFD NTLVDGQSPN TYKGYYDGRA GGGGLGGNVV GPGNNLGGLG PQYDPFNRNS
IGSAGVSYRD AYTDEDNFCP EHWVSFRQTC YRFIRSPKRN WAEAKKICKA HNADLINVDN
VEKHSFILKN LILQNQRQNR FFISARQTGP LNWVNDDNTQ LVQIEDSFSM DEQVPLENED
LHDNRFLVQN DLNNQNINNP NQFYNSLPGT VNQRNQNNLR GFIGPNQPYG DNRYVRDRVV
YAFSKKRDRW MFMPAYEIEL NLFICESKVL YSSDNVNIKL DDKRPYHYGL DINDMERIPR
GPYFVKQPND TTFDVNKNRL INDVTLSCLA NGYPTPSYTW YREVYVDDRL EYQKIDPLAQ
DRYTISGGNL IIYEPKQALD QGAYHCVAEN KFGRIRSESA HLNFGFIMEF NLKRSAETSE
MNWGKSIFCD PPQHYPDVRY YWARDYFPNF VEEDQRVFVS RDGALYFSFI ETVDRANYSC
TVQTLVSDTG RNGPFFPLRV TPNSNYQALI FANTFPKVFP EAPVAGDEIR LECMAFGYPI
PSYNWTRQGL PLQRNAYTIN YGRVLIIQNA TTNDNGEYSC TITNPRKTLM KSIYINIQMR
PQFTIPLKDM IKDYNSDVTF ICEAFAIPDA NYTWYKNAER LDPANINRDR YIIQDNVLTI
KFLEKDKDDA MYQCGAQNQL KTSFSSAQLR VLSMKPSFKK HPLESEVYAV YNGNTTIVCD
PEAAPRPKFQ WKKDGQVIGS GGHRRILPSG TLTISPTSRD DEGIYTCIAS NQAGTDESHA
RVIVLQEIRF IETPPQRIVS KEHDLIFLHC EAAFDELLDI AYVWKHNGEV LKNNHDGTGR
IIVDWNRLTV HNTSMRDAGD YECVVKSAVN EISSKTSVSI EGAPGAPGGV QVIQISKTKA
IIEWVDGSHN GRAIRYYNIL GRTNWNRTWV NVSTHVQARE VDRYTSRQQA EVVNLTPWSA
YEFSVTAVND LGIGTPSAPS PIYSTYEDKP YIAPRNVGGG GGKIGDLTIT WDPLLPQEQH
SHGIHYKVFW KLKGAIEWAS DEIKKQDHMG VAVVNIPLNN YYTEYEVKVQ AINSVGKGPE
SEIAVIHSAE DMPQVAPQKP IALAYNSTCF NVTWQPIDMS RENIRGKLIG HRLKYWKTTH
QEEDSVYYLS RTTRNWALIV GLQPDTYYFV KVMAYNAAGE GPESERFEER TYRKAPQKPP
SSVHVYGINP STVRVVWRYV SPSQDEEPVE GYKVRIWESD QNMITANNTI VPIGQKLESY
INNLTPGKSY NMRVLAYSNG GDGRMSSPTL HFQMGKTTRN GANTRHGHNI NTALILSTLL
LISTFLYTSQ
