CHAO_DROME
ID CHAO_DROME Reviewed; 1315 AA.
AC P12024; Q9VA01;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Chaoptin;
DE AltName: Full=Photoreceptor cell-specific membrane protein;
DE Flags: Precursor;
GN Name=chp; Synonyms=CHT; ORFNames=CG1744;
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 [GENOMIC DNA].
RC TISSUE=Head;
RX PubMed=3124963; DOI=10.1016/0092-8674(88)90518-1;
RA Reinke R., Krantz D.E., Yen D., Zipursky S.L.;
RT "Chaoptin, a cell surface glycoprotein required for Drosophila
RT photoreceptor cell morphogenesis, contains a repeat motif found in yeast
RT and human.";
RL Cell 52:291-301(1988).
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 [GENOMIC DNA] OF 30-50.
RC TISSUE=Head;
RX PubMed=3920657; DOI=10.1073/pnas.82.6.1855;
RA Zipursky S.L., Venkatesh T.R., Benzer S.;
RT "From monoclonal antibody to gene for a neuron-specific glycoprotein in
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1855-1859(1985).
RN [5]
RP PROTEIN SEQUENCE OF 30-50, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=6420071; DOI=10.1016/0092-8674(84)90069-2;
RA Zipursky S.L., Venkatesh T.R., Teplow D.B., Benzer S.;
RT "Neuronal development in the Drosophila retina: monoclonal antibodies as
RT molecular probes.";
RL Cell 36:15-26(1984).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-692; ASN-936; ASN-1122
RP AND ASN-1171, AND 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 AT ASN-77; ASN-267; ASN-305; ASN-361; ASN-422; ASN-680;
RP ASN-692; ASN-718; ASN-936; ASN-970; ASN-1012; ASN-1122; ASN-1152 AND
RP ASN-1171, AND FUNCTION.
RX PubMed=19415110; DOI=10.1371/journal.pone.0005434;
RA Kanie Y., Yamamoto-Hino M., Karino Y., Yokozawa H., Nishihara S., Ueda R.,
RA Goto S., Kanie O.;
RT "Insight into the regulation of glycan synthesis in Drosophila chaoptin
RT based on mass spectrometry.";
RL PLoS ONE 4:E5434-E5434(2009).
CC -!- FUNCTION: Required for photoreceptor cell morphogenesis. Mediates
CC homophilic cellular adhesion. {ECO:0000269|PubMed:19415110}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Extracellular side. Note=Extracellular surface of R-cell plasma
CC membrane.
CC -!- TISSUE SPECIFICITY: Expressed in photoreceptor cells and their axons in
CC the adult retina, the ocellus and larval photoreceptor organ.
CC {ECO:0000269|PubMed:6420071}.
CC -!- DEVELOPMENTAL STAGE: Expressed 24 hours after initiation of
CC photoreceptor cell differentiation, persists through development to
CC adulthood.
CC -!- SIMILARITY: Belongs to the chaoptin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28425.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M19017; AAA28425.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M19008; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; M19009; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; M19010; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; M19011; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; M19012; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; M19013; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; M19014; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; M19016; AAA28425.1; JOINED; Genomic_DNA.
DR EMBL; AE014297; AAF57127.1; -; Genomic_DNA.
DR EMBL; K03274; AAA28851.1; -; Genomic_DNA.
DR PIR; A29944; A29944.
DR RefSeq; NP_524605.1; NM_079866.3.
DR AlphaFoldDB; P12024; -.
DR SMR; P12024; -.
DR BioGRID; 68535; 3.
DR IntAct; P12024; 2.
DR STRING; 7227.FBpp0085139; -.
DR GlyGen; P12024; 15 sites.
DR iPTMnet; P12024; -.
DR PaxDb; P12024; -.
DR DNASU; 43690; -.
DR EnsemblMetazoa; FBtr0085778; FBpp0085139; FBgn0267435.
DR GeneID; 43690; -.
DR KEGG; dme:Dmel_CG1744; -.
DR CTD; 43690; -.
DR FlyBase; FBgn0267435; chp.
DR VEuPathDB; VectorBase:FBgn0267435; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000164586; -.
DR HOGENOM; CLU_006060_0_0_1; -.
DR InParanoid; P12024; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P12024; -.
DR Reactome; R-DME-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-DME-388844; Receptor-type tyrosine-protein phosphatases.
DR BioGRID-ORCS; 43690; 0 hits in 1 CRISPR screen.
DR ChiTaRS; chp; fly.
DR GenomeRNAi; 43690; -.
DR PRO; PR:P12024; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0267435; Expressed in head capsule and 15 other tissues.
DR ExpressionAtlas; P12024; baseline and differential.
DR Genevisible; P12024; DM.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0035996; C:rhabdomere microvillus; IDA:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0032528; P:microvillus organization; IMP:FlyBase.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 7.
DR InterPro; IPR000225; Armadillo.
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; 9.
DR SMART; SM00369; LRR_TYP; 27.
DR PROSITE; PS51450; LRR; 29.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Glycoprotein;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat;
KW Sensory transduction; Signal; Vision.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:6420071"
FT CHAIN 30..1315
FT /note="Chaoptin"
FT /id="PRO_0000020923"
FT REPEAT 80..101
FT /note="LRR 1"
FT REPEAT 103..124
FT /note="LRR 2"
FT REPEAT 128..149
FT /note="LRR 3"
FT REPEAT 152..173
FT /note="LRR 4"
FT REPEAT 177..198
FT /note="LRR 5"
FT REPEAT 201..222
FT /note="LRR 6"
FT REPEAT 226..247
FT /note="LRR 7"
FT REPEAT 250..271
FT /note="LRR 8"
FT REPEAT 279..300
FT /note="LRR 9"
FT REPEAT 326..347
FT /note="LRR 10"
FT REPEAT 351..372
FT /note="LRR 11"
FT REPEAT 375..396
FT /note="LRR 12"
FT REPEAT 401..424
FT /note="LRR 13"
FT REPEAT 477..498
FT /note="LRR 14"
FT REPEAT 527..548
FT /note="LRR 15"
FT REPEAT 551..572
FT /note="LRR 16"
FT REPEAT 577..598
FT /note="LRR 17"
FT REPEAT 601..622
FT /note="LRR 18"
FT REPEAT 625..646
FT /note="LRR 19"
FT REPEAT 649..670
FT /note="LRR 20"
FT REPEAT 676..696
FT /note="LRR 21"
FT REPEAT 708..729
FT /note="LRR 22"
FT REPEAT 733..754
FT /note="LRR 23"
FT REPEAT 757..778
FT /note="LRR 24"
FT REPEAT 781..802
FT /note="LRR 25"
FT REPEAT 805..826
FT /note="LRR 26"
FT REPEAT 828..849
FT /note="LRR 27"
FT REPEAT 854..875
FT /note="LRR 28"
FT REPEAT 879..900
FT /note="LRR 29"
FT REPEAT 903..924
FT /note="LRR 30"
FT REPEAT 928..948
FT /note="LRR 31"
FT REPEAT 949..970
FT /note="LRR 32"
FT REPEAT 973..994
FT /note="LRR 33"
FT REPEAT 996..1017
FT /note="LRR 34"
FT REPEAT 1021..1044
FT /note="LRR 35"
FT REPEAT 1045..1066
FT /note="LRR 36"
FT DOMAIN 1211..1274
FT /note="LRRCT"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19415110"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19415110"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19415110"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19415110"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19415110"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 1012
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 1122
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19415110"
FT CARBOHYD 1152
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:19415110"
FT CARBOHYD 1171
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19415110"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; AAA28425)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="C -> H (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="C -> H (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="I -> V (in Ref. 1; AAA28425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1315 AA; 151983 MW; D2D89A64EB46FCE5 CRC64;
MGLEFFFKFG YAFLTITLMI MIWMSLARAS MFDREMEETH YPPCTYNVMC TCSKSSTDLG
IVHCKNVPFP ALPRMVNQSK VFMLHMENTG LREIEPYFLQ STGMYRLKIS GNHLTEIPDD
AFTGLERSLW ELILPQNDLV EIPSKSLRHL QKLRHLDLGY NHITHIQHDS FRGLEDSLQT
LILRENCISQ LMSHSFSGLL ILETLDLSGN NLFEIDPNVF VDGMPRLTRL LLTDNILSEI
PYDALGPLKS LRTLDISHNV IWSLSGNETY EIKASTKLNL DNLHLEYNHI EVLPPNSFKY
FDTVNRTFFD GNPIHTLRED AFKPARIREI YMRYCGLTNI SPVAFDSLVN SLQILDLSGN
NLTKLHHKLF NNFDVLRVIS MRDNKIKIQK PTETFNAVHY TLLKLDLSGD RNDPTNLQTL
RNMTRMRNMR SLSISRLGSS SVGPEDFKDF GVELEDLQIT RASLSGIQSH AFKHVRGLKR
LDFSENGISS IENDAFHEIG HSLISLKMSH GYSGSALPAE PLRHLTSLQE LDFSNNHISS
MSDTSFHFLK NLRLLELHDN RIEQVLKGTF QGDIHSKLEE ISLRFNHLTS ISQHTFFDLE
ALRKLHLDDN KIDKIERRAF MNLDELEYLS LRGNKINNLA DESFQNLPKL EILDMAFNQL
PNFNFDYFDQ VGTLSNLNVN VSHNQIRQLM YNSSWSGRNE HGGMYHSNIK ILDLSHNNIS
IIHPGYFRPA EISLTHLHLG YNSLMNTTRD VFGNMPHLQW LDLSYNWIHE LDFDAFKNTK
QLQLVFFGHN YLSDIPQDIF KPVQGLRIVD FSHNHLRGLP DNLFYNGGME KLDVSHNMML
KIPSSSLSSL AALTLCELHL SNNFISTIHS MDLSNKFRSL RYLDISYNYL LRIDDAVFAT
MPKLAVLDLS HNRDLKVMDK SFMGLENSLI KLGLENISLS TVPEIRLKYL REFRLGYNEL
PSIPQELAHN MSNLRMLDLS NNDLTNVPLM TQALPHLRRL MLSGNPITSL NNNSFDGVNE
DLEMLDISNF RLHYFEYGCL DSLPHLRSLK LTAYSHLEHF NIPHLLRHHY NIRQLWIEAP
QPFTRIVKKG SGPTQEMQTL QLGNPTDLQR EMEGHLPSKL TNITFSGPQF TNLNERILRG
MRSPYLYMQL FNTSLQALPP NFFKYMGRVR NISLDIRYHN RNLKKIPNPN TGAVPYLPNS
VFLTDLKMSH TDLNCDCDLG WVEFWQRKRR QYICSSQTWT DTVFRTFMNS PCQVYGRHNC
DEHDDDLRET RCENKGGQQL MEALKFDLEC GWDNANCREA AFVVVMVCVA MVFWM
