CSTN1_RAT
ID CSTN1_RAT Reviewed; 952 AA.
AC Q6Q0N0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Calsyntenin-1;
DE AltName: Full=Alcadein-alpha;
DE Short=Alc-alpha;
DE Contains:
DE RecName: Full=Soluble Alc-alpha;
DE Short=SAlc-alpha;
DE Contains:
DE RecName: Full=CTF1-alpha;
DE AltName: Full=C-terminal fragment 1-alpha;
DE Flags: Precursor;
GN Name=Clstn1; Synonyms=Cs1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Eye;
RX PubMed=15326124; DOI=10.1167/iovs.04-0302;
RA Ahmed F., Torrado M., Zinovieva R.D., Senatorov V.V., Wistow G.,
RA Tomarev S.I.;
RT "Gene expression profile of the rat eye iridocorneal angle: NEIBank
RT expressed sequence tag analysis.";
RL Invest. Ophthalmol. Vis. Sci. 45:3081-3090(2004).
RN [2]
RP CLEAVAGE AFTER HIS-795, CLEAVAGE AFTER PHE-824, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: Induces KLC1 association with vesicles and functions as a
CC cargo in axonal anterograde transport. Complex formation with APBA2 and
CC APP, stabilizes APP metabolism and enhances APBA2-mediated suppression
CC of beta-APP40 secretion, due to the retardation of intracellular APP
CC maturation. In complex with APBA2 and C99, a C-terminal APP fragment,
CC abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by
CC gamma-secretase, most probably through stabilization of the direct
CC interaction between APBA2 and APP. As intracellular fragment AlcICD,
CC suppresses APBB1-dependent transactivation stimulated by APP C-terminal
CC intracellular fragment (AICD), most probably by competing with AICD for
CC APBB1-binding. May modulate calcium-mediated postsynaptic signals (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Directly interacts with APBA2. Forms a tripartite complex with
CC APBA2 and APP. The CTF1 chain interacts with PSEN1. The intracellular
CC fragment AlcICD interacts with APBB1; this interaction stabilizes
CC AlcICD metabolism. Interacts with KLC1 and APBB1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9EPL2}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9EPL2}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q9EPL2}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9EPL2}. Nucleus {ECO:0000250}. Vesicle
CC {ECO:0000250|UniProtKB:Q9EPL2}. Note=Neurite tips. Localized in the
CC postsynaptic membrane of both excitatory and inhibitory synapses. The
CC AlcICD fragment is translocated to the nucleus upon interaction with
CC APBB1 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the retina and brain.
CC {ECO:0000269|PubMed:15326124}.
CC -!- DOMAIN: The cytoplasmic domain is involved in interaction with APBA2,
CC as well as the binding of synaptic Ca(2+). {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 presenilin gamma-secretase
CC within the transmembrane domain releases the beta-Alc-alpha chain in
CC the extracellular milieu and produces an intracellular fragment
CC (AlcICD). Beta-Alc-alpha secretion is largely dependent upon PSEN1 and
CC PSEN2. This processing is strongly suppressed in the tripartite complex
CC formed with APBA2 and APP, which seems to prevent the association with
CC PSEN1 (By similarity). {ECO:0000250}.
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DR EMBL; AY569014; AAS75317.1; -; mRNA.
DR RefSeq; NP_001007093.1; NM_001007092.1.
DR AlphaFoldDB; Q6Q0N0; -.
DR STRING; 10116.ENSRNOP00000047223; -.
DR GlyGen; Q6Q0N0; 1 site.
DR iPTMnet; Q6Q0N0; -.
DR PhosphoSitePlus; Q6Q0N0; -.
DR PaxDb; Q6Q0N0; -.
DR PRIDE; Q6Q0N0; -.
DR GeneID; 313717; -.
DR KEGG; rno:313717; -.
DR UCSC; RGD:1306458; rat.
DR CTD; 22883; -.
DR RGD; 1306458; Clstn1.
DR VEuPathDB; HostDB:ENSRNOG00000016398; -.
DR eggNOG; KOG1834; Eukaryota.
DR HOGENOM; CLU_008904_0_0_1; -.
DR InParanoid; Q6Q0N0; -.
DR OMA; CWQGSDN; -.
DR OrthoDB; 302557at2759; -.
DR PRO; PR:Q6Q0N0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016398; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; Q6Q0N0; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
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:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099065; C:integral component of spine apparatus membrane; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0098845; C:postsynaptic endosome; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0042988; F:X11-like protein binding; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; 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:0090128; P:regulation of synapse maturation; ISO:RGD.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; 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 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Cell projection;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane; Nucleus;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..952
FT /note="Calsyntenin-1"
FT /id="PRO_0000323601"
FT CHAIN 29..796
FT /note="Soluble Alc-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000323602"
FT CHAIN 797..952
FT /note="CTF1-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000323603"
FT TOPO_DOM 29..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..154
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 155..255
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 886..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..929
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 795..796
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:26479776"
FT SITE 824..825
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:26479776"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 952 AA; 106261 MW; DBE2185AF20F9713 CRC64;
MLRRPAPALA RAVRLLLAGL LYGGGVWAAR VNKHKPWLEP TYHGIVTEND NTVLLDPPLI
ALDKDSPLRF AGEICGFKIH GQNVPFDAVV VDKSTGEGII RSKEKLDCEL QKDYTFTIQA
YDCGKGPDGT GVKKSHKATV HIQVNDVNEY APVFKEKSYK AAVVEGKQHG SILRVEAVDA
DCSPQFSQIC SYEILTPDVP FTVDKDGYIK NTEKLNYGKE HQYKLTVTAY DCGKKRATED
VLVKISVKPT CSPGWQGWSS RIEYEPGTGA LAVFPSIHLE TCDEPVASVQ ATVELETSHI
GKGCDRDTYS EKSLHRLCGA AAGTSELLPS PSSSFNWTVG LPTDNGHDSD QVFEFNGTQA
VRIPDGVVTL DPKEPFTISV WMRHGPFGRK KETILCSSDK TDMNRHHYSL YVHGCRLIFL
LRQDPSEEKK YRPAEFHWKL NQVCDEDWHH FVLNVEVPSV TLYVDGVSHE PFSVTEDYPL
HPTKIETQLV VGACWQGGDL HMTQFFRGNL AGLTVRSGKL ADKKVIDCLY TCKEGLDLQV
PEDGNRGVQI QTSSSQAVLT LEGENVGELD KAMQHISYLN SRQFPTPGIR RLKITSTVKC
FNEAACIEVP PVEGYVMVLQ PEEPKISLSG VHHFARAASE FESPEGVSLF PELKIISTIT
REVEPEADGA EDPTVQESLV SEEIVHDLDT CEVTVEGEEL NAEQESLEVD VARLQQKGIE
VNHSDLGVVF TGVETMASYE EVLHLLRYRN WHTRSLLDRK FKLICSELNG RYLSNEFKVE
VNVIHTANPV EHANHMAAQP QFVHPEHRSF VDLSGHNLAS PHPFAVVPST ATVVIVVCVS
FLVFMIILGV FRIRAAHQRT MRDQDTGKEN EMDWDDSALT ITVNPMETYE DQHSSEEEEE
EEEEEESEDG EEEEDITSAE SESSEEEEGG PGDGQNTTRQ QQLEWDYSTL SY
