CSTN3_BOVIN
ID CSTN3_BOVIN Reviewed; 957 AA.
AC Q0VCN6; Q0V7L7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Calsyntenin-3;
DE AltName: Full=Alcadein-beta;
DE Short=Alc-beta;
DE Flags: Precursor;
GN Name=CLSTN3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 652-957 (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal cerebellum, and Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-499 (ISOFORM 1/2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0VCN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VCN6-2; Sequence=VSP_032038, VSP_032039;
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}.
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; BC120082; AAI20083.1; -; mRNA.
DR EMBL; DV883017; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT026553; ABH06340.1; -; mRNA.
DR RefSeq; NP_001068893.2; NM_001075425.2. [Q0VCN6-1]
DR AlphaFoldDB; Q0VCN6; -.
DR SMR; Q0VCN6; -.
DR STRING; 9913.ENSBTAP00000010687; -.
DR PaxDb; Q0VCN6; -.
DR Ensembl; ENSBTAT00000010689; ENSBTAP00000010689; ENSBTAG00000008129. [Q0VCN6-2]
DR GeneID; 509969; -.
DR KEGG; bta:509969; -.
DR CTD; 9746; -.
DR VEuPathDB; HostDB:ENSBTAG00000008129; -.
DR eggNOG; KOG1834; Eukaryota.
DR GeneTree; ENSGT00950000183086; -.
DR HOGENOM; CLU_008904_0_0_1; -.
DR InParanoid; Q0VCN6; -.
DR OrthoDB; 302557at2759; -.
DR TreeFam; TF315946; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000008129; Expressed in prefrontal cortex and 92 other tissues.
DR ExpressionAtlas; Q0VCN6; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:AgBase.
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: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; 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 Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cell projection; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; 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_0000323604"
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 919..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 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 VAR_SEQ 799..861
FT /note="VSVLHSVNRVAHPSHMLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSAAT
FT LIIVVCVGFLV -> WFPVRRPSSSWCAWASWCSWSSWVSCAFTHCTAASRGPVGLPGP
FT PATPRIPISSGMTQLSPLS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032038"
FT VAR_SEQ 862..957
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032039"
SQ SEQUENCE 957 AA; 105795 MW; 46FB64D3140AA53F CRC64;
MTPLLFPLLL ASLLPSSSCN KANKHKPWIE AEYQGIVMEN DNTVLLNPPL FALDKDAPLR
YAGEICGFRL HGSGVPFEAV ILDKATGEGL IRAKEPVDCE AQKEHTFTIQ AYDCGEGPDG
ANTKKSHKAT VHVRVNDVNE FAPVFVERLY RAAVTEGKLY DRILRVEAID GDCSPQYSQI
CYYEILTPNT PFLIDNDGNI ENTEKLQYSG EKLYKFTVTA YDCGKKRAAD DAEVEIQVKP
TCKPSWQGWN KRIEYAPGAG SLALFPGIRL ETCDEPLWNI QATIELQTSH VAKGCDRDNY
SERALRKLCG AAPGEVDLLP MPGPNANWTA GLSVHYSQDS SLIYWFNGTQ AVQVPLGGAA
GLGSGPPDSL SDHFTLSFWM KHGVTPNKGK KEEETIVCNT VQNEDGFSHY SLTVHGCRIA
FLYWPLLESA RPVKFLWKLE QVCDDEWHHY ALNLEFPTVT LYADGISFDP ALIHDNGLIH
PPRREPALMI GACWAEEKNK EKEKGGDNST DATAGDPLPI HHYFHGYLAG FSVRSGRLES
REVIECLYAC REGLDYRDFE SLGKGMKVHV NPSQSLLTLE GDDVETFNHA LQHVAYMNTL
RFATPGVRPL RLTTAVKCFS EESCVSIPEV EGYVVVLQPD APQILLSGTA HFARPAVDFE
GPEGVPLFPD LQITCSISHQ VEAKKDESWQ GTVTDTRMSD EIVHNLDGCE ISLVGDDLDP
ERESLLLDMA SLQQRGLELT NTSAYLTIAG VESITVYEEI LRQARYRLRH GAALYARKFR
LSCSEMNGRY SSNEFIVEVS VLHSVNRVAH PSHMLSSQQF LHRGHQPPPE MAGHSLASSH
RNSMVPSAAT LIIVVCVGFL VLMVVLGLVR IHSLHRRVSG ASGPPGASSD PKDPDLFWDD
SALTIIVNPM ESYQSRQVCV AGAAGGQQDD EDSSDSEAAD SPSSDERRII ETPPHRY
