CSTN2_RAT
ID CSTN2_RAT Reviewed; 965 AA.
AC Q8VDA1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Calsyntenin-2;
DE AltName: Full=Alcadein-gamma;
DE Short=Alc-gamma;
DE Flags: Precursor;
GN Name=Clstn2; Synonyms=Cs2, Cstn2;
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.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ER65};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ER65}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ER65}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9ER65}. Postsynapse
CC {ECO:0000250|UniProtKB:Q9ER65}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9ER65}. Note=Most prominent in the postsynaptic
CC specializations of asymmetric (type I) synapses with both axodendritic
CC and axospinous localization. {ECO:0000250|UniProtKB:Q9ER65}.
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-gamma 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 PSEN1
CC (By similarity). {ECO:0000250}.
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DR EMBL; AJ427342; CAD20352.1; -; mRNA.
DR RefSeq; NP_599204.1; NM_134377.1.
DR AlphaFoldDB; Q8VDA1; -.
DR SMR; Q8VDA1; -.
DR STRING; 10116.ENSRNOP00000060748; -.
DR GlyGen; Q8VDA1; 6 sites.
DR PaxDb; Q8VDA1; -.
DR PRIDE; Q8VDA1; -.
DR GeneID; 171394; -.
DR KEGG; rno:171394; -.
DR UCSC; RGD:621151; rat.
DR CTD; 64084; -.
DR RGD; 621151; Clstn2.
DR eggNOG; KOG1834; Eukaryota.
DR InParanoid; Q8VDA1; -.
DR OrthoDB; 302557at2759; -.
DR PhylomeDB; Q8VDA1; -.
DR PRO; PR:Q8VDA1; -.
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: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: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:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..965
FT /note="Calsyntenin-2"
FT /id="PRO_0000004025"
FT TOPO_DOM 21..835
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..965
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..162
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 163..282
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 891..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 965 AA; 107729 MW; 73F89113E823889E CRC64;
MLPGRLCLVP LLLALGVGSG GGSGDGGDSR RRRLLAAKVN KHKPWIETSY HGVITENNDT
VILDPTIVAL DKDAPVPFAG EICAFKIHGQ ELPFEAVVLN KTSGEGRLRA KSPIDCELQK
EYTFIIQAYD CGAGPQEAAW KKSHKAVVHI QVKDVNEFAP TFKEPAYKAI VTEGKIYDSI
LQVEAIDEDC SPQYSQICNY EIVTTDVPFA IDRNGNIRNT EKLSYDKQRQ YEILVTAYDC
GQKPAAQDTL VQVDVKPVCK PGWQDWTKRI EYQPGSGSMP LFPGIHLETC DGAVSSLQVT
AELQTNYIGK GCDRETYSEK SLQKLCGASS GIIDLLPSPS AATNWTAGLL VDSSEMIFKF
DGRQGAKIPD GIVPKNLTDQ FTITMWMKHG PSPGVRAEKE TILCNSDKTE MNRHHYALYV
HNCRLVFLLR KDFDQADTFR PAEFHWKLDQ ICDKEWHYYV INVEFPVVTL YMDGATYEPY
LVTNDWPIHP SHIAMQLTVG ACWQGGEVAK PRFAQFFHGS LASLTIRPGK MESQKVISCL
QACKEGLDIN SLESLGRGIK YHFNPSQSIL VMEGDDIGNI NQALQKVSYI NSRQFPTAGV
RRLRLSSKVQ CFGEDVCISI PDVDAYIMVL QAIEPQITLQ GTERFWRPAA QFESARGVTL
FPDIKIISTF AKTEASGDLR ATGTAPKSAV LEEMLHNLDF CDILVLGGDL DPRQECLELN
HSELHQRHLD ATNSTAGYSI YGVGSMSRYE QVLHHLRYRN WHPTSLETRR FQIKCSELNG
RYTSNEFNLE VSVLHEVRVS DTEHVNHLIV QPPFLQSVYH PETRSSIQRS SVVPSIATVV
IIISVCMLVF VVAMGVYRVR IAHQHFIQET EAAKEAEMDW DDSALTITVN PMEKHEGPGH
GEDETEGEEE EEAEEGMSSS SSGSDDSEEE EEEGMGRVRH GQSGTSSQRP ERSTWNTAGV
INIWK
