GenomeNet

Database: UniProt
Entry: D2A5Z8_TRICA
LinkDB: D2A5Z8_TRICA
Original site: D2A5Z8_TRICA 
ID   D2A5Z8_TRICA            Unreviewed;       918 AA.
AC   D2A5Z8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=Calsyntenin-1-like Protein {ECO:0000313|EMBL:EFA05740.2};
GN   Name=AUGUSTUS-3.0.2_15622 {ECO:0000313|EMBL:EFA05740.2};
GN   ORFNames=TcasGA2_TC015622 {ECO:0000313|EMBL:EFA05740.2};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA05740.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA05740.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05740.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA05740.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA05740.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- SIMILARITY: Belongs to the calsyntenin family.
CC       {ECO:0000256|ARBA:ARBA00035015}.
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; KQ971345; EFA05740.2; -; Genomic_DNA.
DR   RefSeq; XP_008194752.1; XM_008196530.2.
DR   AlphaFoldDB; D2A5Z8; -.
DR   STRING; 7070.D2A5Z8; -.
DR   EnsemblMetazoa; TC015622_001; TC015622_001; TC015622.
DR   GeneID; 659467; -.
DR   KEGG; tca:659467; -.
DR   eggNOG; KOG1834; Eukaryota.
DR   HOGENOM; CLU_008904_0_0_1; -.
DR   InParanoid; D2A5Z8; -.
DR   OMA; IKVNRVC; -.
DR   OrthoDB; 3615717at2759; -.
DR   Proteomes; UP000007266; Linkage group 6.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR   GO; GO:0042988; F:X11-like protein binding; IEA:InterPro.
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   CDD; cd11304; Cadherin_repeat; 2.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 2.
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; CALSYNTENIN; 1.
DR   PANTHER; PTHR14139:SF2; CALSYNTENIN-1; 1.
DR   Pfam; PF00028; Cadherin; 1.
DR   Pfam; PF19699; CLSTN_C; 2.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS50268; CADHERIN_2; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU00043};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..918
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007310017"
FT   TRANSMEM        795..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..136
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          137..249
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          855..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..909
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   918 AA;  103542 MW;  661297D6A50A05D1 CRC64;
     MFWFAICALL LTPIASSTEP FDEYTAPKLD VDNLENGYHG LVKENETLVE VTPAIRAIGE
     QVCSFRIVNK HHGEAPFEIV SKEDGYAELR ARRVLNCEKR RNYKFDIAAV GCNGKQSVSA
     TVHITVSDVN EYAPTFSEPS YVRQVDEGRI YSEIVRVEAT DRDCTPKFGD VCKYEILTSD
     QPFVIDMDGV IRNTEPLDYE RSHNHILSVV AYDCGMRQSL PVMVTIKVNR VCRLGWRGLP
     ERVDYAPTTG KQELFPSASL ELCDVPCNVR ELRTRVDLAT RHIGKGCDRD TYSVQSQRKL
     CGASPSAIDL LPSPGVGAEW TKPLISDEGH ESDQMFEFDG SSTAVSIPNS VLDHNLPSTF
     TIATWMRHGQ HNGQDKRVKE HILCSADDHK MNRHHYALFV RNCRLILLLR RDFSEGDLNI
     FRPAEWRWKI PQVCDDQWHH YAVNVRFPDI ELYVDGQLFR SEKKNPEVID DWPLHPTKGI
     NTTLTVGACW QGSDNKMKHH LKGYLAGLSV LVGETEKPEV LSCLHQCKES LQVPAMELLQ
     PGMELLTNSD LTEVTVEGDN RTNLETLVRK IGYANSREFP TPGRRNLRLT TTVTCDNGKT
     VKVPDAQTYV MVLRPQTPSI NLNGTGNMAR KYEDFRMGVR VLADIHISGE QKLDKCSLTI
     YPNLNPDHEN LSVPEEMLKR LGMAARVSKD GVTITGSDMV FNYQQVLRQI VYTNRKPAYY
     LNRVFKLTCS ELNGRFTSNE YVQTLTVIHP QPKEPIVAHA TVNKHNVELR PASVVSRDYI
     PSEHLNLVAS GGSHAVTIIV VVCVGFLLFM IVLGVIRIRA AHHRNASEEA QDSEMTWDDS
     ALTITVNPME NAERKLEGHS ADYSESDQSD SDSSSDDDNI DGPCRIPDSS DDEEEQPARS
     RKHDYQNISQ LEWDHSTM
//
DBGET integrated database retrieval system