CSTN3_RAT
ID CSTN3_RAT Reviewed; 957 AA.
AC Q8R553;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Calsyntenin-3;
DE AltName: Full=Alcadein-beta;
DE Short=Alc-beta;
DE Flags: Precursor;
GN Name=Clstn3; Synonyms=Cs3, Cstn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=OFA; 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).
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. Interacts with low affinity with KLC1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99JH7};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99JH7}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q99JH7}. Postsynapse
CC {ECO:0000250|UniProtKB:Q99JH7}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q99JH7}. Note=Most prominent in the postsynaptic
CC specializations of asymmetric (type I) synapses with both axodendritic
CC and axospinous localization. {ECO:0000250|UniProtKB:Q99JH7}.
CC -!- DOMAIN: Binds synaptic Ca(2+) with its cytoplasmic domain.
CC {ECO:0000250}.
CC -!- PTM: Proteolytically processed under normal cellular conditions. A
CC primary zeta-cleavage generates a large extracellular (soluble) N-
CC terminal domain (sAlc) and a short C-terminal transmembrane fragment
CC (CTF1). A secondary cleavage catalyzed by gamma-secretase within the
CC transmembrane domain releases the beta-Alc-beta chain in the
CC extracellular milieu and produces an intracellular fragment (AlcICD).
CC This processing is strongly suppressed in the tripartite complex formed
CC with APBA2 and APP, which seems to prevent the association with gamma-
CC secretase (By similarity). {ECO:0000250}.
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DR EMBL; AJ431642; CAD24292.1; -; mRNA.
DR RefSeq; NP_599203.1; NM_134376.1.
DR AlphaFoldDB; Q8R553; -.
DR SMR; Q8R553; -.
DR STRING; 10116.ENSRNOP00000015570; -.
DR CarbonylDB; Q8R553; -.
DR GlyGen; Q8R553; 5 sites.
DR iPTMnet; Q8R553; -.
DR PhosphoSitePlus; Q8R553; -.
DR PaxDb; Q8R553; -.
DR PRIDE; Q8R553; -.
DR GeneID; 171393; -.
DR KEGG; rno:171393; -.
DR UCSC; RGD:621153; rat.
DR CTD; 9746; -.
DR RGD; 621153; Clstn3.
DR eggNOG; KOG1834; Eukaryota.
DR InParanoid; Q8R553; -.
DR OrthoDB; 302557at2759; -.
DR PhylomeDB; Q8R553; -.
DR PRO; PR:Q8R553; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
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:0007268; P:chemical synaptic transmission; NAS:RGD.
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; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
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 2: Evidence at transcript 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..957
FT /note="Calsyntenin-3"
FT /id="PRO_0000004028"
FT TOPO_DOM 20..848
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 849..869
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 870..957
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..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..957
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 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 957 AA; 105945 MW; 7107EF05F40F9840 CRC64;
MTLLLVSLLL ASLLQISSGN KANKHKPWIE AEYQGIVMEN DNTVLLNPPL FALDKDAPLR
YAGEICGFRL HGSGVPFKAV ILDKATGEGL IRAKEPVDCE AQKEHTFTTQ AYDCVDGPDG
ANTKKSHKAT VHVRVNDVNE FAPVFVERLY RAAVTEGKLY DRILRVEAID GDCSPQYSQI
CYYEILTPNT PFLIDNDGNI ENTEKLQYSG EKLYKFTVTA YDCGKKRAAD DAEVEIQVKP
TCKPSWQGWN KRIEYAPGAG SLALFPGIRL ETCDEPLWNI QATIELQTSH VAKGCDRDNY
SERALRKLCG AATGEVDLLP MPGPNANWTA GLSVHYSQDS SLIYWFNGTQ AVQVPLGGPA
GLGSGPQDGL SDHFTLSFWM KHSVTPSKGK KEEETIVCNT IQNEDGYSHY SLTVHGCRIA
FLYWPLLESA RPVKFLWKLE QVCDDEWHHY ALNLEFPTVT LYTDGISFDP ALIHDNGLIH
PPRREPALMI GACWSEEKNK EKEKGGENST DTTSGDPLPI HHYFHGYLAG FSVRSGRLES
REVIECLYAC REGLDYRDFE SLGKGMKVHV NPSQSLLTLE GDDVETFNHA LQHVAYMNTL
RFATPGVRPL RLTTAVKCFS EESCVSIPEV EGYVVVLQPD APQILLSGTA HFARPAVDFE
GPEGVPLFPD LQITCSISHQ VEAKADESWQ GTVTDTRMSD EIVHNLDGCE ISLVGDDLDP
ERESLLLDMA SLQQRGLELT NRSAYLTIAG VETITVYEEI LRQARYQLRH GAALYARKFR
LSCSEMNGRY SSNEFIVEVN VLHSMNRVAH PSHVLSSQQF LHRGHQPPPE MAGHSLASSH
RNSMVPSAAT LIIVVCVGFL VLMVILGLVR IHSLHRRVSG TGGPSGASAD PKDPDLFWDD
SALTIIVNPM ESYQNQQTGV AGVAGGQQEE EDSSDSEAAD SPSSDERRII ESPPHRY
