CSTN1_DROME
ID CSTN1_DROME Reviewed; 978 AA.
AC Q9V498; A4V137; Q9GP64;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Calsyntenin-1;
DE AltName: Full=Cadherin-102F;
DE Flags: Precursor;
GN Name=Cals; Synonyms=Cad102F, CLSTN1; ORFNames=CG11059;
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].
RC TISSUE=Head;
RX PubMed=11161476; DOI=10.1006/mcne.2000.0937;
RA Vogt L., Schrimpf S.P., Meskenaite V., Frischknecht R., Kinter J.,
RA Leone D.P., Ziegler U., Sonderegger P.;
RT "Calsyntenin-1, a proteolytically processed postsynaptic membrane protein
RT with a cytoplasmic calcium-binding domain.";
RL Mol. Cell. Neurosci. 17:151-166(2001).
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;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-304, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: May modulate calcium-mediated postsynaptic signals.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9EPL2}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9EPL2}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q9EPL2}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9EPL2}. Vesicle {ECO:0000250|UniProtKB:Q9EPL2}.
CC -!- DOMAIN: Binds synaptic Ca(2+) with its cytoplasmic domain.
CC {ECO:0000250}.
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DR EMBL; AJ289018; CAC17749.1; -; mRNA.
DR EMBL; AE014135; AAF59384.2; -; Genomic_DNA.
DR EMBL; AE014135; AAN06580.1; -; Genomic_DNA.
DR EMBL; AY121644; AAM51971.1; -; mRNA.
DR RefSeq; NP_001284722.1; NM_001297793.1.
DR RefSeq; NP_524632.1; NM_079893.3.
DR RefSeq; NP_726646.1; NM_166823.2.
DR AlphaFoldDB; Q9V498; -.
DR SMR; Q9V498; -.
DR IntAct; Q9V498; 1.
DR STRING; 7227.FBpp0305853; -.
DR GlyGen; Q9V498; 5 sites.
DR iPTMnet; Q9V498; -.
DR PaxDb; Q9V498; -.
DR PRIDE; Q9V498; -.
DR DNASU; 43824; -.
DR EnsemblMetazoa; FBtr0089207; FBpp0088271; FBgn0039928.
DR EnsemblMetazoa; FBtr0089208; FBpp0088272; FBgn0039928.
DR EnsemblMetazoa; FBtr0345193; FBpp0311392; FBgn0039928.
DR GeneID; 43824; -.
DR KEGG; dme:Dmel_CG11059; -.
DR UCSC; CG11059-RA; d. melanogaster.
DR CTD; 43824; -.
DR FlyBase; FBgn0039928; Cals.
DR VEuPathDB; VectorBase:FBgn0039928; -.
DR eggNOG; KOG1834; Eukaryota.
DR HOGENOM; CLU_008904_0_0_1; -.
DR InParanoid; Q9V498; -.
DR OMA; YTVQCAM; -.
DR OrthoDB; 302557at2759; -.
DR PhylomeDB; Q9V498; -.
DR SignaLink; Q9V498; -.
DR BioGRID-ORCS; 43824; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43824; -.
DR PRO; PR:Q9V498; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0039928; Expressed in antenna and 28 other tissues.
DR ExpressionAtlas; Q9V498; baseline and differential.
DR Genevisible; Q9V498; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; ISM:FlyBase.
DR GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR GO; GO:0042988; F:X11-like protein binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:FlyBase.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISM:FlyBase.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IBA:GO_Central.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR026914; Calsyntenin.
DR InterPro; IPR045588; CLSTN_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR14139; PTHR14139; 1.
DR Pfam; PF19699; CLSTN_C; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 2.
DR SUPFAM; SSF49313; SSF49313; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50268; CADHERIN_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Cell projection;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..978
FT /note="Calsyntenin-1"
FT /id="PRO_0000004029"
FT TOPO_DOM 27..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..143
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 144..249
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 937..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 978 AA; 110493 MW; 0FED6AE787A4299C CRC64;
MTFHKTFGYG CIVLICFELL FAGVETSSEN DDEYLTQKEI ILEKSYHGLI RENETLVEIT
PLIKVNEEKI CNFHILKKPY HEIPFKIELV NNLGILKARR TLNCENRKSY HFEICAIYCD
GTPSNTANVH ITVIDVNEYA PTFLEPSYVI EVDEGRLYNE ILRVEASDKD CTPLFGDVCK
YEILNNDEPF SIDNEGSIKN TEPLSHKASH NHILSVVAYD CAMKESAPIM VSIKVRRVCE
TKFVGMPERI DYTSGSTESL QLFPNARLDL CDISCKNEED LRIHSSIALK TKHISFGCDR
DISNCTSGQK VKDLLPHGAE WTKELSYDEG LEPIFHFDGS TGVVVPATVI DHYDFSSQPF
SILTLFRHNS QVEINKHVKE HIVCSADDHK MNRHHMALFV RNCRLIFLLR KNFNEGDLNI
FSPAEWRWKI PEVCDNEWHH YVLNVEDSSK VDLFIDGVRF ENSIENRHSN PEVIDDWPLH
AAHGVNTSLA IGACYQSLEN RLKHGFNGDI SEVKVSLNSV LTAEDIKCGT TCAEHLLAPK
PLQSNNEKSY SDNSQIKENI EMNEIYISAK NKHDIEQFMR KVQYINTKQK PTVGRRNIEV
LTTLNCKNES SLRLPPIETY IMVNEPIAPL GIDIDVVSAS LETSDLTPPS YSPKIAISGT
SNKLVSYQEI KLGVHILEKT CIDSVSKNNG KLEEKNHIDS CSVVVFPSLN PDHEDIKIDG
DESLSSSMDI KTNINKDGVE MIGKDTISNY INVLRSLVYS NKKPAYYLNR VFKLSCAQQS
SQYKSGEYTL TLTVLHPKQT LFKSTNVLPS SLSKVNFIGN TDNETSFHRN SGSVNGNDNN
QPTESKVYSY SLLHTNNVQE PKSHIHSFIH KAEGSHVTML IILVSVFLAV LLCGVSIARL
KNNQKYIEHH QPCPKISDDG LIWDDSALTI TINPMQADVT SDASSESENS ESEDEEALKD
GFTHINQLEW DNSNIFQQ
