CONN_DROME
ID CONN_DROME Reviewed; 682 AA.
AC Q01819; Q8MRN1; Q9VZ74;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Connectin;
DE Flags: Precursor;
GN Name=Con; ORFNames=CG7503;
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].
RX PubMed=1505024; DOI=10.1016/0092-8674(92)90426-d;
RA Nose A., Mahajan V.B., Goodman C.S.;
RT "Connectin: a homophilic cell adhesion molecule expressed on a subset of
RT muscles and the motoneurons that innervate them in Drosophila.";
RL Cell 70:553-567(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=1363542; DOI=10.1242/dev.116.4.1163;
RA Gould A.P., White R.A.H.;
RT "Connectin, a target of homeotic gene control in Drosophila.";
RL Development 116:1163-1174(1992).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-682.
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).
CC -!- FUNCTION: Cell adhesion protein involved in target recognition during
CC neuromuscular development. Mediates homophilic cellular adhesion.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in abdominal and thoracic
CC segment muscle and motorneuron cells.
CC -!- DEVELOPMENTAL STAGE: Embryo.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF47952.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM50172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M96647; AAA28424.1; -; mRNA.
DR EMBL; X68701; CAA48652.1; -; mRNA.
DR EMBL; AE014296; AAF47952.3; ALT_INIT; Genomic_DNA.
DR EMBL; AY119518; AAM50172.1; ALT_INIT; mRNA.
DR PIR; A43318; A43318.
DR PIR; A49121; A49121.
DR RefSeq; NP_001246635.1; NM_001259706.2.
DR RefSeq; NP_523930.3; NM_079206.5.
DR AlphaFoldDB; Q01819; -.
DR SMR; Q01819; -.
DR BioGRID; 64058; 2.
DR STRING; 7227.FBpp0301699; -.
DR PaxDb; Q01819; -.
DR EnsemblMetazoa; FBtr0073375; FBpp0073231; FBgn0005775.
DR GeneID; 38590; -.
DR KEGG; dme:Dmel_CG7503; -.
DR UCSC; CG7503-RA; d. melanogaster.
DR CTD; 38590; -.
DR FlyBase; FBgn0005775; Con.
DR VEuPathDB; VectorBase:FBgn0005775; -.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_405049_0_0_1; -.
DR InParanoid; Q01819; -.
DR PhylomeDB; Q01819; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 38590; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38590; -.
DR PRO; PR:Q01819; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0005775; Expressed in brain and 37 other tissues.
DR ExpressionAtlas; Q01819; baseline and differential.
DR Genevisible; Q01819; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; IDA:FlyBase.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007413; P:axonal fasciculation; TAS:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0016200; P:synaptic target attraction; TAS:FlyBase.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 8.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Developmental protein; Glycoprotein;
KW GPI-anchor; Leucine-rich repeat; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..24
FT CHAIN 25..658
FT /note="Connectin"
FT /id="PRO_0000020979"
FT PROPEP 659..682
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020980"
FT REPEAT 149..172
FT /note="LRR 1"
FT REPEAT 173..196
FT /note="LRR 2"
FT REPEAT 199..220
FT /note="LRR 3"
FT REPEAT 223..244
FT /note="LRR 4"
FT REPEAT 247..268
FT /note="LRR 5"
FT REPEAT 271..292
FT /note="LRR 6"
FT REPEAT 295..316
FT /note="LRR 7"
FT REPEAT 319..342
FT /note="LRR 8"
FT REPEAT 343..364
FT /note="LRR 9"
FT REPEAT 367..388
FT /note="LRR 10"
FT REPEAT 389..404
FT /note="LRR 11"
FT DOMAIN 405..462
FT /note="LRRCT"
FT REGION 29..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 658
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CONFLICT 631
FT /note="E -> G (in Ref. 2; CAA48652)"
FT /evidence="ECO:0000305"
FT CONFLICT 674..677
FT /note="VALM -> QVAL (in Ref. 1; AAA28424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 75995 MW; E7F26353438ED06F CRC64;
MATLADSAIC FLLLSLLLIG ACLVTPTEGR AKDDRRTRGR GSSSGVLSSS SSSSNNMNNG
YYSGSSSTAG SSSGYVFTSS SAVNSGSTGY SGPMDSTGFC TRRRDMKLMC YCTPDENHVP
VQKAECWVFS EGLHQNDTTW TRFYQQKRLR ELKFVIQNNA RLDYIPTMII EPLKNLSSIV
IEYSQVEIVK SYAFANLPFL ERIILNNNHI MALDQDAFAN HIRLRELNLE HNQIFEMDRY
AFRNLPLCER LFLNNNNIST LHEGLFADMA RLTFLNLAHN QINVLTSEIF RGLGNLNVLK
LTRNNLNFIG DTVFAELWSL SELELDDNRI ERISERALDG LNTLKTLNLR NNLLKKIDNG
LLRGTPALLS INVQANKLET LTFYTFQPIM DNLVNSTSEL LVSDNKFICD CRLQWIFELK
NRTRHLQLRD SLEDLHCTLQ EPKLSHFVDP VPPTILDVLN IGGFTAIGSN SASMGGVGNS
VVGSSYSGLT MDDSRKHLGS RSRQALRGQR QFASSAENVV ESKMRRRRKR QEEVKEKDLA
AVAPAHKRYD YYDDNNGGMS LGHGLDLDDN LSLHKQGFYG AGSPVVGHND VDVLMTSHSA
SGDALDILTT KNAIYIKLFL LKPEMLPCHD ELSDPTELPL SRDLMDVRSN VGQDMSTAGA
NSLAQGMTII VSLVALMMIS RG
