CART_RAT
ID CART_RAT Reviewed; 129 AA.
AC P49192;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cocaine- and amphetamine-regulated transcript protein;
DE Contains:
DE RecName: Full=CART(1-52);
DE Contains:
DE RecName: Full=CART(55-102);
DE Contains:
DE RecName: Full=CART(62-102);
DE Flags: Precursor;
GN Name=Cartpt; Synonyms=Cart;
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] (ISOFORMS LONG AND SHORT).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7891182; DOI=10.1523/jneurosci.15-03-02471.1995;
RA Douglass J.O., McKinzie A.A., Couceyro P.;
RT "PCR differential display identifies a rat brain mRNA that is
RT transcriptionally regulated by cocaine and amphetamine.";
RL J. Neurosci. 15:2471-2481(1995).
RN [2]
RP PROTEIN SEQUENCE OF 81-97, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DISULFIDE BONDS.
RX PubMed=9654146; DOI=10.1016/s0014-5793(98)00543-2;
RA Thim L., Nielsen P.F., Judge M.E., Andersen A.S., Diers I., Egel-Mitani M.,
RA Hastrup S.;
RT "Purification and characterisation of a new hypothalamic satiety peptide,
RT cocaine and amphetamine regulated transcript (CART), produced in yeast.";
RL FEBS Lett. 428:263-268(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41 AND SER-48,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 (ISOFORM SHORT), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Satiety factor closely associated with the actions of leptin
CC and neuropeptide y; this anorectic peptide inhibits both normal and
CC starvation-induced feeding and completely blocks the feeding response
CC induced by neuropeptide Y and regulated by leptin in the hypothalamus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P49192-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P49192-2; Sequence=VSP_000794;
CC -!- TISSUE SPECIFICITY: Neuroendocrine tissues. Predominantly expressed in
CC the hypothalamus, pituitary, and longitudinal muscle-myenteric plexus.
CC Abundant expression is also seen in the midbrain/thalamus and eye. A
CC lower level expression is seen in the other brain regions and adrenal.
CC -!- INDUCTION: By cocaine and amphetamine.
CC -!- SIMILARITY: Belongs to the CART family. {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; U10071; AAA87897.1; -; mRNA.
DR RefSeq; NP_058806.1; NM_017110.1. [P49192-1]
DR RefSeq; XP_006231905.1; XM_006231843.3. [P49192-2]
DR AlphaFoldDB; P49192; -.
DR SMR; P49192; -.
DR STRING; 10116.ENSRNOP00000023869; -.
DR iPTMnet; P49192; -.
DR PhosphoSitePlus; P49192; -.
DR PaxDb; P49192; -.
DR Ensembl; ENSRNOT00000023869; ENSRNOP00000023869; ENSRNOG00000017712. [P49192-2]
DR GeneID; 29131; -.
DR KEGG; rno:29131; -.
DR UCSC; RGD:2272; rat. [P49192-1]
DR CTD; 9607; -.
DR RGD; 2272; Cartpt.
DR VEuPathDB; HostDB:ENSRNOG00000017712; -.
DR eggNOG; ENOG502S2YU; Eukaryota.
DR GeneTree; ENSGT00390000018319; -.
DR HOGENOM; CLU_157363_1_0_1; -.
DR InParanoid; P49192; -.
DR OMA; PRTGTMQ; -.
DR OrthoDB; 1562917at2759; -.
DR PhylomeDB; P49192; -.
DR TreeFam; TF332948; -.
DR PRO; PR:P49192; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000017712; Expressed in duodenum and 10 other tissues.
DR Genevisible; P49192; RN.
DR GO; GO:0005615; C:extracellular space; IDA:HGNC-UCL.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR GO; GO:0008343; P:adult feeding behavior; IDA:HGNC-UCL.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISS:HGNC-UCL.
DR GO; GO:0009267; P:cellular response to starvation; IDA:HGNC-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:HGNC-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0001696; P:gastric acid secretion; TAS:RGD.
DR GO; GO:0032099; P:negative regulation of appetite; IDA:HGNC-UCL.
DR GO; GO:0045779; P:negative regulation of bone resorption; ISO:RGD.
DR GO; GO:0070093; P:negative regulation of glucagon secretion; IDA:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISS:HGNC-UCL.
DR GO; GO:0032812; P:positive regulation of epinephrine secretion; ISS:HGNC-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:HGNC-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:HGNC-UCL.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISS:HGNC-UCL.
DR GO; GO:0046850; P:regulation of bone remodeling; ISO:RGD.
DR GO; GO:0050796; P:regulation of insulin secretion; IDA:RGD.
DR GO; GO:0070253; P:somatostatin secretion; IDA:RGD.
DR Gene3D; 4.10.40.30; -; 1.
DR InterPro; IPR009106; CART.
DR InterPro; IPR036722; CART_C_sf.
DR PANTHER; PTHR16655; PTHR16655; 1.
DR Pfam; PF06373; CART; 1.
DR SUPFAM; SSF64546; SSF64546; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Neuropeptide; Neurotransmitter;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..129
FT /note="Cocaine- and amphetamine-regulated transcript
FT protein"
FT /id="PRO_0000004442"
FT PEPTIDE 28..79
FT /note="CART(1-52)"
FT /id="PRO_0000004443"
FT PEPTIDE 82..129
FT /note="CART(55-102)"
FT /id="PRO_0000004444"
FT PEPTIDE 89..129
FT /note="CART(62-102)"
FT /evidence="ECO:0000255"
FT /id="PRO_0000004445"
FT MOD_RES 41
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 95..113
FT /evidence="ECO:0000269|PubMed:9654146"
FT DISULFID 101..121
FT /evidence="ECO:0000269|PubMed:9654146"
FT DISULFID 115..128
FT /evidence="ECO:0000269|PubMed:9654146"
FT VAR_SEQ 54..66
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7891182"
FT /id="VSP_000794"
FT MOD_RES P49192-2:48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 129 AA; 14140 MW; 0FDE28B705BB2728 CRC64;
MESSRLRLLP VLGAALLLLL PLLGAGAQED AELQPRALDI YSAVDDASHE KELPRRQLRA
PGAVLQIEAL QEVLKKLKSK RIPIYEKKYG QVPMCDAGEQ CAVRKGARIG KLCDCPRGTS
CNSFLLKCL
