ID CSTN1_HUMAN Reviewed; 981 AA. AC O94985; A8K183; Q5SR52; Q5UE58; Q71MN0; Q8N4K9; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 28-JAN-2026, entry version 200. DE RecName: Full=Calsyntenin-1 {ECO:0000303|PubMed:12498782}; DE AltName: Full=Alcadein-alpha {ECO:0000303|PubMed:12972431}; DE Short=Alc-alpha {ECO:0000303|PubMed:12972431}; DE AltName: Full=Alzheimer-related cadherin-like protein; DE AltName: Full=Non-classical cadherin XB31alpha; DE Contains: DE RecName: Full=Soluble Alc-alpha {ECO:0000305|PubMed:15037614}; DE Short=SAlc-alpha {ECO:0000305|PubMed:15037614}; DE Contains: DE RecName: Full=CTF1-alpha {ECO:0000305|PubMed:15037614}; DE AltName: Full=C-terminal fragment 1-alpha {ECO:0000305|PubMed:15037614}; DE Flags: Precursor; GN Name=CLSTN1 {ECO:0000312|HGNC:HGNC:17447}; GN Synonyms=CS1, KIAA0911 {ECO:0000303|PubMed:10048485}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, RP INTERACTION WITH APBA2, AND MUTAGENESIS OF 913-ASN-PRO-914 AND TYR-918. RC TISSUE=Brain; RX PubMed=12972431; DOI=10.1074/jbc.m306024200; RA Araki Y., Tomita S., Yamaguchi H., Miyagi N., Sumioka A., Kirino Y., RA Suzuki T.; RT "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like RT protein-mediated stabilization of amyloid beta-protein precursor RT metabolism."; RL J. Biol. Chem. 278:49448-49458(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ALA-474; RP CYS-524; ARG-583; HIS-857 AND SER-870. RC TISSUE=Hippocampus; 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 [6] RP PROTEIN SEQUENCE OF 29-33 AND 826-833, FUNCTION (CTF1-ALPHA AND SOLUBLE RP ALC-ALPHA), INTERACTION WITH PSEN1 (CTF1-ALPHA), AND PROTEOLYTIC CLEAVAGE. RX PubMed=15037614; DOI=10.1074/jbc.m401925200; RA Araki Y., Miyagi N., Kato N., Yoshida T., Wada S., Nishimura M., Komano H., RA Yamamoto T., De Strooper B., Yamamoto K., Suzuki T.; RT "Coordinated metabolism of Alcadein and amyloid beta-protein precursor RT regulates FE65-dependent gene transactivation."; RL J. Biol. Chem. 279:24343-24354(2004). RN [7] RP TISSUE SPECIFICITY. 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 [8] RP INTERACTION WITH KLC1, SUBCELLULAR LOCATION, AND GLYCOSYLATION. RX PubMed=17332754; DOI=10.1038/sj.emboj.7601609; RA Araki Y., Kawano T., Taru H., Saito Y., Wada S., Miyamoto K., Kobayashi H., RA Ishikawa H.O., Ohsugi Y., Yamamoto T., Matsuno K., Kinjo M., Suzuki T.; RT "The novel cargo Alcadein induces vesicle association of kinesin-1 motor RT components and activates axonal transport."; RL EMBO J. 26:1475-1486(2007). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KLC1. RX PubMed=21385839; DOI=10.1242/jcs.075168; RA Vagnoni A., Rodriguez L., Manser C., De Vos K.J., Miller C.C.; RT "Phosphorylation of kinesin light chain 1 at serine 460 modulates binding RT and trafficking of calsyntenin-1."; RL J. Cell Sci. 124:1032-1042(2011). CC -!- FUNCTION: Postsynaptic adhesion molecule that binds to presynaptic CC neurexins to mediate both excitatory and inhibitory synapse formation CC (By similarity). Promotes synapse development by acting as a cell CC adhesion molecule at the postsynaptic membrane, which associates with CC neurexin-alpha at the presynaptic membrane (By similarity). Also CC functions as a cargo in axonal anterograde transport by acting as a CC molecular adapter that promotes KLC1 association with vesicles CC (PubMed:21385839). Complex formation with APBA2 and APP, stabilizes APP CC metabolism and enhances APBA2-mediated suppression of beta-APP40 CC secretion, due to the retardation of intracellular APP maturation CC (PubMed:12972431). {ECO:0000250|UniProtKB:Q99JH7, CC ECO:0000250|UniProtKB:Q9EPL2, ECO:0000269|PubMed:12972431, CC ECO:0000269|PubMed:21385839}. CC -!- FUNCTION: [Soluble Alc-alpha]: 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 (PubMed:15037614). {ECO:0000305|PubMed:15037614}. CC -!- FUNCTION: [CTF1-alpha]: In complex with APBA2 and C99, a C-terminal APP CC fragment, abolishes C99 interaction with PSEN1 and thus APP C99 CC cleavage by gamma-secretase, most probably through stabilization of the CC direct interaction between APBA2 and APP (PubMed:15037614). CC {ECO:0000305|PubMed:15037614}. CC -!- SUBUNIT: Directly interacts with APBA2 (PubMed:12972431). Forms a CC tripartite complex with APBA2 and APP (By similarity). Interacts with CC KLC1 (PubMed:17332754, PubMed:21385839). {ECO:0000250|UniProtKB:Q9EPL2, CC ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:17332754, CC ECO:0000269|PubMed:21385839}. CC -!- SUBUNIT: [Soluble Alc-alpha]: Interacts with APBB1; this interaction CC stabilizes AlcICD metabolism. {ECO:0000269|PubMed:15037614}. CC -!- SUBUNIT: [CTF1-alpha]: Interacts with PSEN1. CC {ECO:0000269|PubMed:15037614}. CC -!- INTERACTION: CC O94985; Q99767: APBA2; NbExp=2; IntAct=EBI-522075, EBI-81711; CC O94985; Q8CD76: Klc1; Xeno; NbExp=7; IntAct=EBI-522075, EBI-6271950; CC O94985-2; P05067: APP; NbExp=3; IntAct=EBI-16041593, EBI-77613; CC O94985-2; Q9UK58-5: CCNL1; NbExp=3; IntAct=EBI-16041593, EBI-25873837; CC O94985-2; P09496-2: CLTA; NbExp=3; IntAct=EBI-16041593, EBI-4401010; CC O94985-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-16041593, EBI-743960; CC O94985-2; Q16609: LPAL2; NbExp=3; IntAct=EBI-16041593, EBI-10238012; CC O94985-2; Q9Y6R0: NUMBL; NbExp=3; IntAct=EBI-16041593, EBI-945925; CC O94985-2; O60927: PPP1R11; NbExp=3; IntAct=EBI-16041593, EBI-1048104; CC O94985-2; Q09028: RBBP4; NbExp=3; IntAct=EBI-16041593, EBI-620823; CC O94985-2; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-16041593, EBI-714023; CC O94985-2; Q13573: SNW1; NbExp=3; IntAct=EBI-16041593, EBI-632715; CC O94985-2; Q91YS4: Klc2; Xeno; NbExp=2; IntAct=EBI-16041593, EBI-6272135; CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:Q9EPL2}; Single-pass type I membrane protein CC {ECO:0000255}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:17332754}; Single-pass type I membrane protein CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:17332754, CC ECO:0000269|PubMed:21385839}; Single-pass type I membrane protein CC {ECO:0000255}. Cell projection, neuron projection CC {ECO:0000269|PubMed:17332754}. Note=Localized in the postsynaptic CC membrane of both excitatory and inhibitory synapses. CC {ECO:0000250|UniProtKB:Q9EPL2}. CC -!- SUBCELLULAR LOCATION: [Soluble Alc-alpha]: Nucleus CC {ECO:0000269|PubMed:17332754}. Note=The AlcICD fragment is translocated CC to the nucleus upon interaction with APBB1. CC {ECO:0000269|PubMed:17332754}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Alcalpha2; CC IsoId=O94985-1; Sequence=Displayed; CC Name=2; Synonyms=Alcalpha1; CC IsoId=O94985-2; Sequence=VSP_032035; CC -!- TISSUE SPECIFICITY: Expressed in the brain and, a lower level, in the CC heart, skeletal muscle, kidney and placenta. Accumulates in dystrophic CC neurites around the amyloid core of Alzheimer disease senile plaques CC (at protein level). {ECO:0000269|PubMed:12498782, CC ECO:0000269|PubMed:12972431}. CC -!- DOMAIN: The cytoplasmic domain binds synaptic Ca(2+). CC {ECO:0000250|UniProtKB:Q9EPL2}. CC -!- PTM: Proteolytically processed under normal cellular conditions CC (PubMed:15037614). A primary zeta-cleavage generates a large CC extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal CC transmembrane fragment (CTF1) (PubMed:15037614). A secondary cleavage CC catalyzed by presenilin gamma-secretase within the transmembrane domain CC releases the beta-Alc-alpha chain in the extracellular milieu and CC produces an intracellular fragment (AlcICD) (PubMed:15037614). This CC processing is strongly suppressed in the tripartite complex formed with CC APBA2 and APP, which seems to prevent the association with PSEN1 CC (PubMed:15037614). {ECO:0000269|PubMed:15037614}. CC -!- SIMILARITY: Belongs to the calsyntenin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74934.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AF438482; AAQ04552.1; -; mRNA. DR EMBL; AY753301; AAV30551.1; -; mRNA. DR EMBL; AB020718; BAA74934.2; ALT_INIT; mRNA. DR EMBL; AK289798; BAF82487.1; -; mRNA. DR EMBL; AL691449; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL357140; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC033902; AAH33902.1; -; mRNA. DR CCDS; CCDS105.1; -. [O94985-2] DR CCDS; CCDS30580.1; -. [O94985-1] DR RefSeq; NP_001009566.1; NM_001009566.3. [O94985-1] DR RefSeq; NP_001289812.1; NM_001302883.1. DR RefSeq; NP_055759.3; NM_014944.4. [O94985-2] DR AlphaFoldDB; O94985; -. DR BioGRID; 116550; 152. DR DIP; DIP-31694N; -. DR ELM; O94985; -. DR FunCoup; O94985; 633. DR IntAct; O94985; 129. DR MINT; O94985; -. DR STRING; 9606.ENSP00000366513; -. DR GlyCosmos; O94985; 4 sites, 1 glycan. DR GlyGen; O94985; 7 sites, 3 O-linked glycans (3 sites). DR iPTMnet; O94985; -. DR PhosphoSitePlus; O94985; -. DR BioMuta; CLSTN1; -. DR jPOST; O94985; -. DR MassIVE; O94985; -. DR PaxDb; 9606-ENSP00000366513; -. DR PeptideAtlas; O94985; -. DR ProteomicsDB; 50608; -. [O94985-1] DR ProteomicsDB; 50609; -. [O94985-2] DR Pumba; O94985; -. DR Antibodypedia; 2632; 180 antibodies from 28 providers. DR DNASU; 22883; -. DR Ensembl; ENST00000361311.4; ENSP00000354997.4; ENSG00000171603.19. [O94985-2] DR Ensembl; ENST00000377298.9; ENSP00000366513.4; ENSG00000171603.19. [O94985-1] DR GeneID; 22883; -. DR KEGG; hsa:22883; -. DR MANE-Select; ENST00000377298.9; ENSP00000366513.4; NM_001009566.3; NP_001009566.1. DR UCSC; uc001aqh.4; human. [O94985-1] DR AGR; HGNC:17447; -. DR ClinPGx; PA38238; -. DR CTD; 22883; -. DR DisGeNET; 22883; -. DR GeneCards; CLSTN1; -. DR HGNC; HGNC:17447; CLSTN1. DR HPA; ENSG00000171603; Low tissue specificity. DR MIM; 611321; gene. DR OpenTargets; ENSG00000171603; -. DR VEuPathDB; HostDB:ENSG00000171603; -. DR eggNOG; KOG1834; Eukaryota. DR GeneTree; ENSGT00950000183086; -. DR HOGENOM; CLU_008904_0_0_1; -. DR InParanoid; O94985; -. DR OMA; CWQGSDN; -. DR OrthoDB; 10012272at2759; -. DR PAN-GO; O94985; 4 GO annotations based on evolutionary models. DR PhylomeDB; O94985; -. DR PathwayCommons; O94985; -. DR SignaLink; O94985; -. DR Agora; ENSG00000171603; -. DR BioGRID-ORCS; 22883; 16 hits in 1159 CRISPR screens. DR ChiTaRS; CLSTN1; human. DR GeneWiki; CLSTN1; -. DR GenomeRNAi; 22883; -. DR Pharos; O94985; Tbio. DR PRO; PR:O94985; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O94985; protein. DR Bgee; ENSG00000171603; Expressed in frontal pole and 205 other cell types or tissues. DR ExpressionAtlas; O94985; baseline and differential. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0098845; C:postsynaptic endosome; IEA:Ensembl. DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central. DR GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB. DR GO; GO:0042988; F:X11-like protein binding; IPI:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB. 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; IEA:Ensembl. 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 GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl. DR GO; GO:0090128; P:regulation of synapse maturation; IEA:Ensembl. DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IEA:Ensembl. DR CDD; cd11304; Cadherin_repeat; 2. DR FunFam; 2.60.120.200:FF:000036; Calsyntenin 1; 1. DR FunFam; 2.60.40.60:FF:000025; Calsyntenin 1; 1. DR FunFam; 2.60.40.60:FF:000062; Calsyntenin 3; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.60.40.60; Cadherins; 2. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR045588; CLSTN_C. DR InterPro; IPR013320; ConA-like_dom_sf. DR PANTHER; PTHR14139; CALSYNTENIN; 1. DR PANTHER; PTHR14139:SF4; CALSYNTENIN-1; 1. DR Pfam; PF00028; Cadherin; 1. DR Pfam; PF19699; CLSTN_C; 1. DR Pfam; PF13385; Laminin_G_3; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 2. DR SUPFAM; SSF49313; Cadherin-like; 2. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS50268; CADHERIN_2; 2. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; KW Cell projection; Direct protein sequencing; Endoplasmic reticulum; KW Glycoprotein; Golgi apparatus; Membrane; Nucleus; KW Postsynaptic cell membrane; Proteomics identification; Reference proteome; KW Repeat; Signal; Synapse; Transmembrane; Transmembrane helix. FT SIGNAL 1..28 FT /evidence="ECO:0000269|PubMed:15037614" FT CHAIN 29..981 FT /note="Calsyntenin-1" FT /id="PRO_0000004021" FT CHAIN 29..825 FT /note="Soluble Alc-alpha" FT /evidence="ECO:0000305|PubMed:15037614" FT /id="PRO_0000323597" FT CHAIN 826..981 FT /note="CTF1-alpha" FT /evidence="ECO:0000305|PubMed:15037614" FT /id="PRO_0000323598" FT TOPO_DOM 29..859 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 860..880 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 881..981 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 38..164 FT /note="Cadherin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 165..265 FT /note="Cadherin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT REGION 915..981 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 925..960 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 962..981 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 824..825 FT /note="Cleavage" FT /evidence="ECO:0000250|UniProtKB:Q6Q0N0" FT SITE 853..854 FT /note="Cleavage" FT /evidence="ECO:0000250|UniProtKB:Q6Q0N0" FT CARBOHYD 346 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 366 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 515 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 72..81 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12972431, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_032035" FT VARIANT 332 FT /note="A -> T (in dbSNP:rs7550295)" FT /id="VAR_048582" FT VARIANT 474 FT /note="V -> A (in dbSNP:rs17853245)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_039552" FT VARIANT 524 FT /note="S -> C (in dbSNP:rs17853244)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_039553" FT VARIANT 583 FT /note="P -> R (in dbSNP:rs17853243)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_039554" FT VARIANT 857 FT /note="P -> H (in dbSNP:rs17855572)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_039555" FT VARIANT 870 FT /note="F -> S (in dbSNP:rs17855573)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_039556" FT MUTAGEN 913..914 FT /note="NP->AA: Abolishes interaction with APBA2." FT /evidence="ECO:0000269|PubMed:12972431" FT MUTAGEN 918 FT /note="Y->A: No effect on APBA2-binding." FT /evidence="ECO:0000269|PubMed:12972431" FT CONFLICT 102 FT /note="D -> G (in Ref. 3; BAF82487)" FT /evidence="ECO:0000305" FT CONFLICT 553 FT /note="K -> R (in Ref. 3; BAF82487)" FT /evidence="ECO:0000305" FT CONFLICT 886..887 FT /note="HR -> ST (in Ref. 1; AAQ04552)" FT /evidence="ECO:0000305" SQ SEQUENCE 981 AA; 109793 MW; 01856284DEC3FC73 CRC64; MLRRPAPALA PAARLLLAGL LCGGGVWAAR VNKHKPWLEP TYHGIVTEND NTVLLDPPLI ALDKDAPLRF AESFEVTVTK EGEICGFKIH GQNVPFDAVV VDKSTGEGVI RSKEKLDCEL QKDYSFTIQA YDCGKGPDGT NVKKSHKATV HIQVNDVNEY APVFKEKSYK ATVIEGKQYD SILRVEAVDA DCSPQFSQIC SYEIITPDVP FTVDKDGYIK NTEKLNYGKE HQYKLTVTAY DCGKKRATED VLVKISIKPT CTPGWQGWNN RIEYEPGTGA LAVFPNIHLE TCDEPVASVQ ATVELETSHI GKGCDRDTYS EKSLHRLCGA AAGTAELLPS PSGSLNWTMG LPTDNGHDSD QVFEFNGTQA VRIPDGVVSV SPKEPFTISV WMRHGPFGRK KETILCSSDK TDMNRHHYSL YVHGCRLIFL FRQDPSEEKK YRPAEFHWKL NQVCDEEWHH YVLNVEFPSV TLYVDGTSHE PFSVTEDYPL HPSKIETQLV VGACWQEFSG VENDNETEPV TVASAGGDLH MTQFFRGNLA GLTLRSGKLA DKKVIDCLYT CKEGLDLQVL EDSGRGVQIQ AHPSQLVLTL EGEDLGELDK AMQHISYLNS RQFPTPGIRR LKITSTIKCF NEATCISVPP VDGYVMVLQP EEPKISLSGV HHFARAASEF ESSEGVFLFP ELRIISTITR EVEPEGDGAE DPTVQESLVS EEIVHDLDTC EVTVEGEELN HEQESLEVDM ARLQQKGIEV SSSELGMTFT GVDTMASYEE VLHLLRYRNW HARSLLDRKF KLICSELNGR YISNEFKVEV NVIHTANPME HANHMAAQPQ FVHPEHRSFV DLSGHNLANP HPFAVVPSTA TVVIVVCVSF LVFMIILGVF RIRAAHRRTM RDQDTGKENE MDWDDSALTI TVNPMETYED QHSSEEEEEE EEEEESEDGE EEDDITSAES ESSEEEEGEQ GDPQNATRQQ QLEWDDSTLS Y //