CSTN3_PONAB
ID CSTN3_PONAB Reviewed; 956 AA.
AC Q5R9Q9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Calsyntenin-3;
DE AltName: Full=Alcadein-beta;
DE Short=Alc-beta;
DE Flags: Precursor;
GN Name=CLSTN3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859323; CAH91501.1; -; mRNA.
DR RefSeq; NP_001127427.1; NM_001133955.1.
DR AlphaFoldDB; Q5R9Q9; -.
DR STRING; 9601.ENSPPYP00000004814; -.
DR GeneID; 100174497; -.
DR KEGG; pon:100174497; -.
DR CTD; 9746; -.
DR eggNOG; KOG1834; Eukaryota.
DR InParanoid; Q5R9Q9; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
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 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..956
FT /note="Calsyntenin-3"
FT /id="PRO_0000269184"
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 917..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"
SQ SEQUENCE 956 AA; 106095 MW; 9E233AB17BE72110 CRC64;
MTLLLLPLLL ASLLASCSCN KANKHKPWIE AEYQGIVMEN DNTVLLNPPL FALDKDAPLR
YAGEICGFRL HGSGVPFEAV ILDKATGEGR IRAKEPMDCE AQKEHTFTIQ AYDCGEGPDG
ANTKKSHKAT VHVRVNDVNE FAPVFVERLY RAAVTEGKLY DRILRVEAID GDCSPQYSQI
CYYEILTPNT PFLIDNDGNI ENTEKLQYSG ERLYKFTVTA YDCGKKRAAD DAEVEIQVKP
TCKPSWQGWN KRIEYAPGAG SLALFPGIRL ETCDEPLWNI QATIELQTSH VAKGCDRDNY
SERALRKLCG AATGEVDLLP MPGPNANWTA GLSVHYSQDS SQIYWFNGTQ AVQVPLGGPS
GLGSGPQDSL SDHFTLSFWM KHGVTPNKGK KEEETIVCNT VQNEDGFSHY SLTVHGCRIA
FLYWPLLESA RPVKFLWKLE QVCDDEWHHY ALNLEFPTVT LYTDGISFDP ALIHDNGLIH
PPRREPALMI GACWTEGKNK EKEKGDNSTD TTQGDPLSIQ RYFHGYLAGF SVRSGRLESR
EVIECLYACR EGLDYRDFES LGKGMKVHVN PSQSLLTLEG DDVETFNHAL QHVAYMNTLR
FATPGVRPLR LTTAVKCFSE ESCVSIPEVE GYVVVLQPDA PQILLSGTAH FARPAVDFEG
TEGVPLFPDL QITCSISHQV EAKKDESWQG TVTDTRMSDE IVHNLDGCEI SLVGDDLDPE
RESLLLDTTS LQQRGLELTN TSAYLTIAGV ESITVYEEIL RQARYRLRHG AALYARKFRL
SCSEMNGRYS SNEFIVEVNV LHSMNRVAHP SHVLSSQQFL HRGHQPPPEM AGHSLASSHR
NSMIPSAATL IIVVCVGFLV LMVVLGLVRI HSLHRRVSGA GGPPGASSDP KDPDLFWDDS
ALTIIVNPME SYQNRQACVT GAVGGQQEDE DSSDSEVADS PSSDERRIIE TPPHRY
