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CALY_RAT
ID   CALY_RAT                Reviewed;         226 AA.
AC   P58821;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Neuron-specific vesicular protein calcyon;
GN   Name=Caly; Synonyms=Drd1ip;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=11920718; DOI=10.1002/cne.10198;
RA   Zelenin S., Aperia A., Diaz Heijtz R.;
RT   "Calcyon in the rat brain: cloning of cDNA and expression of mRNA.";
RL   J. Comp. Neurol. 446:37-45(2002).
RN   [2]
RP   FUNCTION.
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   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17623072; DOI=10.1186/1744-9081-3-33;
RA   Heijtz R.D., Alexeyenko A., Castellanos F.X.;
RT   "Calcyon mRNA expression in the frontal-striatal circuitry and its
RT   relationship to vesicular processes and ADHD.";
RL   Behav. Brain Funct. 3:33-33(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17885599; DOI=10.1097/wnr.0b013e3282f03f51;
RA   Kruusmagi M., Zelenin S., Brismar H., Scott L.;
RT   "Intracellular dynamics of calcyon, a neuron-specific vesicular protein.";
RL   NeuroReport 18:1547-1551(2007).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:17885599}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:17885599}. Cell membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in neurons (at protein
CC       level). In all age groups, expressed at significantly higher levels in
CC       the medial prefrontal and orbital frontal cortices of spontaneously
CC       hypertensive rats (SHR), a model of attention deficit-hyperactivity
CC       disorder, than Wistar Kyoto (WKY) animals. In the motor cortex, dorsal
CC       striatum and nucleus accumbens, expression is significantly elevated in
CC       SHR only in younger animals. {ECO:0000269|PubMed:17623072,
CC       ECO:0000269|PubMed:17885599}.
CC   -!- DEVELOPMENTAL STAGE: Levels decrease significantly with age.
CC       {ECO:0000269|PubMed:17623072}.
CC   -!- SIMILARITY: Belongs to the NSG family. {ECO:0000305}.
CC   -!- CAUTION: The human ortholog was originally thought to interact with the
CC       D1 dopamine receptor (DRD1) and to play a role in potentiating calcium
CC       ion-dependent signaling but this work was later retracted.
CC       {ECO:0000305}.
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DR   EMBL; AF303658; AAL09318.1; -; mRNA.
DR   RefSeq; NP_001177328.1; NM_001190399.1.
DR   RefSeq; NP_620270.1; NM_138915.1.
DR   AlphaFoldDB; P58821; -.
DR   BioGRID; 251406; 1.
DR   STRING; 10116.ENSRNOP00000024766; -.
DR   iPTMnet; P58821; -.
DR   PhosphoSitePlus; P58821; -.
DR   PaxDb; P58821; -.
DR   PRIDE; P58821; -.
DR   Ensembl; ENSRNOT00000089729; ENSRNOP00000069564; ENSRNOG00000018337.
DR   GeneID; 192349; -.
DR   KEGG; rno:192349; -.
DR   UCSC; RGD:621719; rat.
DR   CTD; 50632; -.
DR   RGD; 621719; Caly.
DR   eggNOG; ENOG502QW2S; Eukaryota.
DR   GeneTree; ENSGT00390000000483; -.
DR   HOGENOM; CLU_112085_1_0_1; -.
DR   InParanoid; P58821; -.
DR   OMA; ILKQKHC; -.
DR   OrthoDB; 1262422at2759; -.
DR   PhylomeDB; P58821; -.
DR   TreeFam; TF332232; -.
DR   PRO; PR:P58821; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018337; Expressed in cerebellum and 12 other tissues.
DR   Genevisible; P58821; RN.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS: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; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098843; C:postsynaptic endocytic zone; ISO:RGD.
DR   GO; GO:0032051; F:clathrin light chain binding; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0008089; P:anterograde axonal transport; IMP:RGD.
DR   GO; GO:0048268; P:clathrin coat assembly; ISS: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; IDA:RGD.
DR   GO; GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB.
DR   GO; GO:2001019; P:positive regulation of retrograde axon cargo transport; IMP:RGD.
DR   GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; ISO:RGD.
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   Cell membrane; Cytoplasmic vesicle; Endocytosis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..226
FT                   /note="Neuron-specific vesicular protein calcyon"
FT                   /id="PRO_0000164370"
FT   TOPO_DOM        1..88
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   226 AA;  24718 MW;  CF575AC37A3EF6B5 CRC64;
     MVKLGCSFSG KPGKETGDQD GAAMDSVPLI SPLDVSQLQP SFPDQVVIKT QTEYQLTSAD
     QPKKFADLEG QRLACSHPEE GRRLPTARMI AFAMALLGCV LIMYKAIWYD QFTCPDGFLL
     RHKICTPLTL EMYYTEMDPE RHRSILAAIG AYPLSRKHGT EMPAIWGNSY RAGKEEHKGT
     TPAAMTVSTA AAAAAAEGNE PSGKPLDMRE KEDPQKAEDV PSQSPK
 
 
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