CSTN2_MOUSE
ID CSTN2_MOUSE Reviewed; 966 AA.
AC Q9ER65; Q5DTM0; Q6P565; Q8C858;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Calsyntenin-2;
DE AltName: Full=Alcadein-gamma;
DE Short=Alc-gamma;
DE Flags: Precursor;
GN Name=Clstn2; Synonyms=Cs2, Cstn2, Kiaa4134;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 426-966 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: May modulate calcium-mediated postsynaptic signals.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12498782}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12498782}. Postsynapse
CC {ECO:0000269|PubMed:12498782}. Cell projection, dendrite
CC {ECO:0000269|PubMed:12498782}. Note=Most prominent in the postsynaptic
CC specializations of asymmetric (type I) synapses with both axodendritic
CC and axospinous localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ER65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ER65-2; Sequence=VSP_032037;
CC -!- TISSUE SPECIFICITY: Restricted to the brain. In the cerebral cortex,
CC found in the somas and neuropil of all layers. Expressed at highest
CC levels in neurons of cortical layers 5 and 6 and, at lower levels, in
CC neurons of the upper layers. Highly expressed in Purkinje cells. Also
CC found in a few scattered interneurons throughout the granule cell layer
CC and occasionally in neurons in the molecular layer (at protein level).
CC Present throughout all cortical layers, highest levels in GABAergic
CC neurons (based on morphology and distribution pattern).
CC {ECO:0000269|PubMed:12498782}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90297.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ278069; CAC14887.1; -; mRNA.
DR EMBL; AK220500; BAD90297.1; ALT_INIT; mRNA.
DR EMBL; BC063058; AAH63058.1; -; mRNA.
DR EMBL; AK048369; BAC33313.1; -; mRNA.
DR CCDS; CCDS40733.1; -. [Q9ER65-1]
DR RefSeq; NP_071714.2; NM_022319.2. [Q9ER65-1]
DR RefSeq; XP_006511397.1; XM_006511334.3. [Q9ER65-2]
DR AlphaFoldDB; Q9ER65; -.
DR STRING; 10090.ENSMUSP00000035027; -.
DR GlyConnect; 2176; 3 N-Linked glycans (2 sites).
DR GlyGen; Q9ER65; 6 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q9ER65; -.
DR PhosphoSitePlus; Q9ER65; -.
DR MaxQB; Q9ER65; -.
DR PaxDb; Q9ER65; -.
DR PeptideAtlas; Q9ER65; -.
DR PRIDE; Q9ER65; -.
DR ProteomicsDB; 277909; -. [Q9ER65-1]
DR ProteomicsDB; 277910; -. [Q9ER65-2]
DR Antibodypedia; 33471; 136 antibodies from 20 providers.
DR DNASU; 64085; -.
DR Ensembl; ENSMUST00000035027; ENSMUSP00000035027; ENSMUSG00000032452. [Q9ER65-1]
DR Ensembl; ENSMUST00000162295; ENSMUSP00000124081; ENSMUSG00000032452. [Q9ER65-2]
DR GeneID; 64085; -.
DR KEGG; mmu:64085; -.
DR UCSC; uc009rdd.1; mouse. [Q9ER65-1]
DR UCSC; uc009rde.1; mouse. [Q9ER65-2]
DR CTD; 64084; -.
DR MGI; MGI:1929897; Clstn2.
DR VEuPathDB; HostDB:ENSMUSG00000032452; -.
DR eggNOG; KOG1834; Eukaryota.
DR GeneTree; ENSGT00950000183086; -.
DR HOGENOM; CLU_008904_0_0_1; -.
DR InParanoid; Q9ER65; -.
DR OMA; WQDWAKR; -.
DR OrthoDB; 302557at2759; -.
DR PhylomeDB; Q9ER65; -.
DR TreeFam; TF315946; -.
DR BioGRID-ORCS; 64085; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Clstn2; mouse.
DR PRO; PR:Q9ER65; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ER65; protein.
DR Bgee; ENSMUSG00000032452; Expressed in olfactory epithelium and 174 other tissues.
DR Genevisible; Q9ER65; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
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; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
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; IGI:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IGI:MGI.
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 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..966
FT /note="Calsyntenin-2"
FT /id="PRO_0000004024"
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..966
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 890..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..966
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"
FT VAR_SEQ 947..966
FT /note="SSQSPERSTWNTAGVINIWK -> RQAQLEWDDSTLPY (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032037"
FT CONFLICT 342
FT /note="A -> G (in Ref. 2; BAD90297)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="N -> H (in Ref. 1; CAC14887)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="V -> G (in Ref. 1; CAC14887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 966 AA; 107887 MW; 681735771BBBF97E CRC64;
MLPGRLCLVP LLLALGVGSG GGSGDGGDSR RRRLLVAKVN KHKPWIETSY HGVITENNDT
VILDPPLVAL DKDAPVPFAG EICAFKIHGQ ELPFEAVVLN KTSGEGRLRA KSPIDCELQK
EYTFIIQAYD CGAGPREAAW KKSHKAVVHI QVKDVNEFAP TFKEPAYKAI VTEGKIYDSI
LQVEAIDEDC SPQYSQICNY EIVTTDVPFA IDRNGNIRNT EKLSYDKQHQ YEILVTAYDC
GQKPAAQDTL VQVDVKPVCK PGWQDWTKRI EYQPGSGSMP LFPSIHLETC 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 NRALQKVSYI NSRQFPTAGV
RRLRLSSKVQ CFGEDVCISI PDVDAYIMVL QAIEPQITLQ GTERFWRPAA QFESARGVTL
FPDIKIVSTF AKTEASGDMR ATGTAPKSAV LEEMLHNLDF CDILVLGGDL DPRQECLELN
HSELHQRHLD ATNSTAGYSI YGVGSMNRYE QVLHHLRYRN WHPTSLETRR FRIKCSELNG
RYTSNEFNLE VSVLHEVRVS DKEHVNHLIV QPPFLQSVHH PETRSSIQRS SVVPSIATVV
IIISVCMLVF VVAMGVYRVR IAHQHFIQET EAAKEAEMDW DDSALTITVN PMEKHEGPGN
GEDETTEVEE EEEAEEGSSS SSSGSDDSEE EEEEGMGRVR HGQSGTSSQS PERSTWNTAG
VINIWK
