CSTN1_HUMAN
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 03-AUG-2022, entry version 183.
DE RecName: Full=Calsyntenin-1;
DE AltName: Full=Alcadein-alpha;
DE Short=Alc-alpha;
DE AltName: Full=Alzheimer-related cadherin-like protein;
DE AltName: Full=Non-classical cadherin XB31alpha;
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, KIAA0911;
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, 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).
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. The 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, ECO:0000269|PubMed:12972431}.
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 -!- 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: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17332754}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:17332754}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:17332754}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:17332754}. Postsynaptic cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Nucleus {ECO:0000269|PubMed:17332754}. Note=Neurite tips. Localized in
CC the postsynaptic membrane of both excitatory and inhibitory synapses
CC (By similarity). The AlcICD fragment is translocated to the nucleus
CC upon interaction with APBB1. {ECO:0000250}.
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 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). This processing is strongly suppressed in the tripartite
CC complex formed with APBA2 and APP, which seems to prevent the
CC association with PSEN1. {ECO:0000269|PubMed:15037614}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74934.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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_001009566.2. [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; 134.
DR DIP; DIP-31694N; -.
DR ELM; O94985; -.
DR IntAct; O94985; 42.
DR MINT; O94985; -.
DR STRING; 9606.ENSP00000366513; -.
DR GlyGen; O94985; 5 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; O94985; -.
DR PhosphoSitePlus; O94985; -.
DR BioMuta; CLSTN1; -.
DR EPD; O94985; -.
DR jPOST; O94985; -.
DR MassIVE; O94985; -.
DR MaxQB; O94985; -.
DR PaxDb; O94985; -.
DR PeptideAtlas; O94985; -.
DR PRIDE; O94985; -.
DR ProteomicsDB; 50608; -. [O94985-1]
DR ProteomicsDB; 50609; -. [O94985-2]
DR Antibodypedia; 2632; 178 antibodies from 27 providers.
DR DNASU; 22883; -.
DR Ensembl; ENST00000361311.4; ENSP00000354997.4; ENSG00000171603.18. [O94985-2]
DR Ensembl; ENST00000377298.9; ENSP00000366513.4; ENSG00000171603.18. [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 CTD; 22883; -.
DR DisGeNET; 22883; -.
DR GeneCards; CLSTN1; -.
DR HGNC; HGNC:17447; CLSTN1.
DR HPA; ENSG00000171603; Low tissue specificity.
DR MIM; 611321; gene.
DR neXtProt; NX_O94985; -.
DR OpenTargets; ENSG00000171603; -.
DR PharmGKB; PA38238; -.
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; 302557at2759; -.
DR PhylomeDB; O94985; -.
DR TreeFam; TF315946; -.
DR PathwayCommons; O94985; -.
DR SignaLink; O94985; -.
DR BioGRID-ORCS; 22883; 14 hits in 1080 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 203 other tissues.
DR ExpressionAtlas; O94985; baseline and differential.
DR Genevisible; O94985; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; Direct protein sequencing; Endoplasmic reticulum;
KW 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: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 /id="PRO_0000323597"
FT CHAIN 826..981
FT /note="CTF1-alpha"
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 921..960
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..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
