CSTN3_MOUSE
ID CSTN3_MOUSE Reviewed; 956 AA.
AC Q99JH7; Q544R0;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Calsyntenin-3;
DE AltName: Full=Alcadein-beta;
DE Short=Alc-beta;
DE Flags: Precursor;
GN Name=Clstn3; Synonyms=Cs3, Cstn3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12498782; DOI=10.1006/mcne.2002.1181;
RA Hintsch G., Zurlinden A., Meskenaite V., Steuble M., Fink-Widmer K.,
RA Kinter J., Sonderegger P.;
RT "The calsyntenins - a family of postsynaptic membrane proteins with
RT distinct neuronal expression patterns.";
RL Mol. Cell. Neurosci. 21:393-409(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH KLC1, AND MUTAGENESIS OF PHE-896.
RX PubMed=16760430; DOI=10.1091/mbc.e06-02-0112;
RA Konecna A., Frischknecht R., Kinter J., Ludwig A., Steuble M.,
RA Meskenaite V., Indermuehle M., Engel M., Cen C., Mateos J.-M., Streit P.,
RA Sonderegger P.;
RT "Calsyntenin-1 docks vesicular cargo to kinesin-1.";
RL Mol. Biol. Cell 17:3651-3663(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May modulate calcium-mediated postsynaptic signals. Complex
CC formation with APBA2 and APP, stabilizes APP metabolism and enhances
CC APBA2-mediated suppression of beta-APP40 secretion, due to the
CC retardation of intracellular APP maturation. {ECO:0000250}.
CC -!- SUBUNIT: Directly interacts with APBA2. Forms a tripartite complex with
CC APBA2 and APP (By similarity). Interacts with low affinity with KLC1.
CC {ECO:0000250, ECO:0000269|PubMed:16760430}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12498782}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12498782}. Postsynapse
CC {ECO:0000269|PubMed:12498782}. Cell projection, dendrite
CC {ECO:0000269|PubMed:12498782}. Note=Most prominent in the postsynaptic
CC specializations of asymmetric (type I) synapses with both axodendritic
CC and axospinous localization. {ECO:0000269|PubMed:12498782}.
CC -!- TISSUE SPECIFICITY: Restricted to the brain. In the cerebral cortex,
CC found in the somas and neuropil of all layers. Expressed at highest
CC levels in neurons of cortical layer 5 and, at lower levels, in neurons
CC of the upper layers. Highly expressed in Purkinje cells. Also found in
CC a few scattered interneurons throughout the granule cell layer and
CC occasionally in neurons in the molecular layer (at protein level). In
CC all layers, high levels in a subpopulation of presumptive GABAergic
CC neurons (based on morphology). {ECO:0000269|PubMed:12498782}.
CC -!- DOMAIN: Binds synaptic Ca(2+) with its cytoplasmic domain.
CC {ECO:0000250}.
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; AJ278486; CAC33088.1; -; mRNA.
DR EMBL; AK032336; BAC27821.1; -; mRNA.
DR EMBL; BC055054; AAH55054.1; -; mRNA.
DR CCDS; CCDS20519.1; -.
DR RefSeq; NP_705728.1; NM_153508.4.
DR AlphaFoldDB; Q99JH7; -.
DR SMR; Q99JH7; -.
DR BioGRID; 231248; 1.
DR IntAct; Q99JH7; 1.
DR STRING; 10090.ENSMUSP00000008297; -.
DR GlyConnect; 2177; 3 N-Linked glycans (1 site).
DR GlyGen; Q99JH7; 5 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q99JH7; -.
DR PhosphoSitePlus; Q99JH7; -.
DR MaxQB; Q99JH7; -.
DR PaxDb; Q99JH7; -.
DR PRIDE; Q99JH7; -.
DR ProteomicsDB; 277911; -.
DR Antibodypedia; 42025; 34 antibodies from 14 providers.
DR DNASU; 232370; -.
DR Ensembl; ENSMUST00000008297; ENSMUSP00000008297; ENSMUSG00000008153.
DR GeneID; 232370; -.
DR KEGG; mmu:232370; -.
DR UCSC; uc009dqw.2; mouse.
DR CTD; 9746; -.
DR MGI; MGI:2178323; Clstn3.
DR VEuPathDB; HostDB:ENSMUSG00000008153; -.
DR eggNOG; KOG1834; Eukaryota.
DR GeneTree; ENSGT00950000183086; -.
DR InParanoid; Q99JH7; -.
DR OMA; YTVQCAM; -.
DR OrthoDB; 302557at2759; -.
DR PhylomeDB; Q99JH7; -.
DR TreeFam; TF315946; -.
DR BioGRID-ORCS; 232370; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Clstn3; mouse.
DR PRO; PR:Q99JH7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99JH7; protein.
DR Bgee; ENSMUSG00000008153; Expressed in primary visual cortex and 119 other tissues.
DR ExpressionAtlas; Q99JH7; baseline and differential.
DR Genevisible; Q99JH7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:1902474; P:positive regulation of protein localization to synapse; IDA:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IGI:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0007416; P:synapse assembly; IDA:MGI.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
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; PF00028; Cadherin; 1.
DR Pfam; PF19699; CLSTN_C; 1.
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 Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..956
FT /note="Calsyntenin-3"
FT /id="PRO_0000004027"
FT TOPO_DOM 20..847
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..868
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 869..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..145
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 146..246
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 916..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 896
FT /note="F->D: Increased KLC1-binding."
FT /evidence="ECO:0000269|PubMed:16760430"
SQ SEQUENCE 956 AA; 105872 MW; BF9CB267B1D0B578 CRC64;
MTLLLVSLLL ASLLQISSGN KANKHKPWIE AEYQGIVMEN DNTVLLNPPL FALDKDAPLR
YAGEICGFRL HGSGVPFEAV ILDKATGEGL IRAKEPVDCE AQKEHTFTIQ AYDCGEGPDG
TNTKKSHKAT VHVRVNDVNE FAPVFVERLY RAAVTEGKLY DRILRVEAID GDCSPQYSQI
CYYEILTPNT PFLIDNDGNI ENTEKLQYSG EKLYKFTVTA YDCGKKRAAD DAEVEIQVKP
TCKPSWQGWN KRIEYAPGAG SLALFPGIRL ETCDEPLWNI QATIELQTSH VAKGCDRDNY
SERALRKLCG AATGEVDLLP MPGPNANWTA GLSVHYSQDS SLIYWFNGTQ AVQVPLGGPA
GLGSGPQDGF SDHFTLSFWM KHSVTPSKGK KEEETIVCNT VQNEDGYSHY SLTVHGCRIA
FLYWPLLESA RPVKFLWKLE QVCDDEWHHY ALNLEFPTVT LYTDGISFDP ALIHDNGLIH
PPRREPALMI GACWTEEKNK EKKGGENSTD TASGDPLLIH HYFHGYLAGF SVRSGRLESR
EVIECLYACR EGLDYRDFES LGKGMKVHVN PSQSLLTLEG DDVETFNHAL QHVAYMNTLR
FATPGVRPLR LTTAVKCFSE ESCVSIPEVE GYVVVLQPDA PQILLSGTAH FARPAVDFEG
PEGVPLFPDL QITCSISHQV EAKADESWQG TVTDTRMSDE IVHNLDGCEI SLVGDDLDPE
RESLLLDMAS LQQRGLELTN TSAYLTIAGV ETITVYEEIL RQARYQLRHG AALYARKFRL
SCSEMNGRYS SNEFIVEVNV LHSMNRVAHP SHVLSSQQFL HRGHQPPPEM AGHSLASSHR
NSMVPSAATL IIVVCVGFLV LMVILGLVRI HSLHRRVSGT GGPSGASTDP KDPDLFWDDS
ALTIIVNPME SYQNQQTCVA GVAGGQQEEE DSSDSEAADS PSSDERRIIE SPPHRY
