CALY_HUMAN
ID CALY_HUMAN Reviewed; 217 AA.
AC Q9NYX4; Q5VWX3; Q5VWY5; Q5VWY6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Neuron-specific vesicular protein calcyon;
GN Name=CALY; Synonyms=DRD1IP;
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].
RX PubMed=10698743; DOI=10.1126/science.287.5458.1660;
RA Lezcano N., Mrzljak L., Eubanks S., Levenson R., Goldman-Rakic P.,
RA Bergson C.;
RT "Dual signaling regulated by calcyon, a D1 dopamine receptor interacting
RT protein.";
RL Science 287:1660-1664(2000).
RN [2]
RP ERRATUM OF PUBMED:10698743, AND RETRACTION NOTICE OF PUBMED:10698743.
RX PubMed=17170272; DOI=10.1126/science.314.5806.1681b;
RA Lezcano N., Mrzljak L., Levenson R., Bergson C.;
RL Science 314:1681-1681(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12622665; DOI=10.1001/archpsyc.60.3.311;
RA Koh P.O., Bergson C., Undie A.S., Goldman-Rakic P.S., Lidow M.S.;
RT "Up-regulation of the D1 dopamine receptor-interacting protein, calcyon, in
RT patients with schizophrenia.";
RL Arch. Gen. Psychiatry 60:311-319(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14534309; DOI=10.1074/jbc.m305803200;
RA Ali M.K., Bergson C.;
RT "Elevated intracellular calcium triggers recruitment of the receptor cross-
RT talk accessory protein calcyon to the plasma membrane.";
RL J. Biol. Chem. 278:51654-51663(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLTA.
RX PubMed=16595675; DOI=10.1074/jbc.m600265200;
RA Xiao J., Dai R., Negyessy L., Bergson C.;
RT "Calcyon, a novel partner of clathrin light chain, stimulates clathrin-
RT mediated endocytosis.";
RL J. Biol. Chem. 281:15182-15193(2006).
RN [9]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [10]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
CC -!- FUNCTION: Interacts with clathrin light chain A and stimulates clathrin
CC self-assembly and clathrin-mediated endocytosis.
CC {ECO:0000269|PubMed:16595675}.
CC -!- SUBUNIT: Interacts with CLTA. {ECO:0000269|PubMed:16595675}.
CC -!- INTERACTION:
CC Q9NYX4; P09496: CLTA; NbExp=4; IntAct=EBI-10904725, EBI-1171169;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass
CC membrane protein. Cell membrane; Single-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NYX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYX4-2; Sequence=VSP_034474, VSP_034475;
CC Name=3;
CC IsoId=Q9NYX4-3; Sequence=VSP_034473;
CC -!- TISSUE SPECIFICITY: Expressed in the pyramidal cells of the prefrontal
CC cortex, in hippothalamus and in caudate nucleus. No expression in
CC spleen. Up-regulated in the prefrontal cortex of schizophrenic patients
CC with nearly twice the levels of non-schizophrenics.
CC {ECO:0000269|PubMed:12622665}.
CC -!- PTM: Glycosylated. {ECO:0000305|PubMed:19838169,
CC ECO:0000305|PubMed:23234360}.
CC -!- SIMILARITY: Belongs to the NSG family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to interact with the D1 dopamine
CC receptor (DRD1) and to play a role in potentiating calcium ion-
CC dependent signaling but this work was later retracted.
CC {ECO:0000305|PubMed:10698743}.
CC -!- CAUTION: In cerebrospinal fluid (CSF), found to be O-glycosylated in
CC the predicted intracellular region at Thr-180 and Thr-189
CC (PubMed:19838169). This glycosylation has been confirmed by a separate
CC mass spectrometry (MS) method (PubMed:23234360). Glycosylation in this
CC region of the protein is unexplained as yet.
CC {ECO:0000305|PubMed:19838169, ECO:0000305|PubMed:23234360}.
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DR EMBL; AF225903; AAF34714.1; -; mRNA.
DR EMBL; AL360181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471211; EAW61334.1; -; Genomic_DNA.
DR EMBL; BC038978; AAH38978.1; -; mRNA.
DR CCDS; CCDS7678.1; -. [Q9NYX4-1]
DR RefSeq; NP_056537.1; NM_015722.3. [Q9NYX4-1]
DR AlphaFoldDB; Q9NYX4; -.
DR BioGRID; 119105; 3.
DR IntAct; Q9NYX4; 5.
DR STRING; 9606.ENSP00000252939; -.
DR DrugBank; DB05419; ADX-10061.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB05432; DAS-431 IV.
DR DrugBank; DB00831; Trifluoperazine.
DR GlyGen; Q9NYX4; 1 site.
DR iPTMnet; Q9NYX4; -.
DR PhosphoSitePlus; Q9NYX4; -.
DR BioMuta; CALY; -.
DR DMDM; 17374622; -.
DR MassIVE; Q9NYX4; -.
DR PaxDb; Q9NYX4; -.
DR PeptideAtlas; Q9NYX4; -.
DR PRIDE; Q9NYX4; -.
DR ProteomicsDB; 83295; -. [Q9NYX4-1]
DR ProteomicsDB; 83296; -. [Q9NYX4-2]
DR Antibodypedia; 32650; 99 antibodies from 27 providers.
DR DNASU; 50632; -.
DR Ensembl; ENST00000252939.9; ENSP00000252939.4; ENSG00000130643.9. [Q9NYX4-1]
DR Ensembl; ENST00000368555.3; ENSP00000357543.3; ENSG00000130643.9. [Q9NYX4-3]
DR Ensembl; ENST00000368558.1; ENSP00000357546.1; ENSG00000130643.9. [Q9NYX4-2]
DR GeneID; 50632; -.
DR KEGG; hsa:50632; -.
DR MANE-Select; ENST00000252939.9; ENSP00000252939.4; NM_015722.4; NP_056537.1.
DR UCSC; uc001lmo.3; human. [Q9NYX4-1]
DR CTD; 50632; -.
DR DisGeNET; 50632; -.
DR GeneCards; CALY; -.
DR HGNC; HGNC:17938; CALY.
DR HPA; ENSG00000130643; Group enriched (brain, pituitary gland).
DR MIM; 604647; gene.
DR neXtProt; NX_Q9NYX4; -.
DR OpenTargets; ENSG00000130643; -.
DR PharmGKB; PA162380987; -.
DR VEuPathDB; HostDB:ENSG00000130643; -.
DR eggNOG; ENOG502QW2S; Eukaryota.
DR GeneTree; ENSGT00390000000483; -.
DR HOGENOM; CLU_112085_1_0_1; -.
DR InParanoid; Q9NYX4; -.
DR OMA; ILKQKHC; -.
DR OrthoDB; 1262422at2759; -.
DR PhylomeDB; Q9NYX4; -.
DR TreeFam; TF332232; -.
DR PathwayCommons; Q9NYX4; -.
DR SignaLink; Q9NYX4; -.
DR BioGRID-ORCS; 50632; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; CALY; human.
DR GeneWiki; DRD1IP; -.
DR GenomeRNAi; 50632; -.
DR Pharos; Q9NYX4; Tbio.
DR PRO; PR:Q9NYX4; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NYX4; protein.
DR Bgee; ENSG00000130643; Expressed in nucleus accumbens and 124 other tissues.
DR Genevisible; Q9NYX4; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0098843; C:postsynaptic endocytic zone; IDA:SynGO.
DR GO; GO:0032051; F:clathrin light chain binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR GO; GO:0048268; P:clathrin coat assembly; IDA:UniProtKB.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; IEA:Ensembl.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:2001019; P:positive regulation of retrograde axon cargo transport; IEA:Ensembl.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR InterPro; IPR009431; NSG.
DR PANTHER; PTHR28546; PTHR28546; 1.
DR Pfam; PF06387; Calcyon; 1.
DR PIRSF; PIRSF002383; Calcyon; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasmic vesicle; Endocytosis;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..217
FT /note="Neuron-specific vesicular protein calcyon"
FT /id="PRO_0000164368"
FT TOPO_DOM 1..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT VAR_SEQ 83..217
FT /note="LPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYT
FT EMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPG
FT KPSAKAEKEAARKAAGSAAPPPAQ -> VTTPTPPTVGTQDRRRRWKAAGGAWVPSRPV
FT WGPLALREERVAVSHPAQSWPHRLPCTHQAPSRGCRCRLTKQWRS (in isoform
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034473"
FT VAR_SEQ 121..124
FT /note="HKIC -> GPEF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034474"
FT VAR_SEQ 125..217
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034475"
SQ SEQUENCE 217 AA; 23434 MW; 7B3ACA9042819F58 CRC64;
MVKLGCSFSG KPGKDPGDQD GAAMDSVPLI SPLDISQLQP PLPDQVVIKT QTEYQLSSPD
QQNFPDLEGQ RLNCSHPEEG RRLPTARMIA FAMALLGCVL IMYKAIWYDQ FTCPDGFLLR
HKICTPLTLE MYYTEMDPER HRSILAAIGA YPLSRKHGTE TPAAWGDGYR AAKEERKGPT
QAGAAAAATE PPGKPSAKAE KEAARKAAGS AAPPPAQ
