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 24-JAN-2024, entry version 141. 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; 10116-ENSRNOP00000023869; -. DR Ensembl; ENSRNOT00000023869.3; ENSRNOP00000023869.2; ENSRNOG00000017712.3. [P49192-2] DR GeneID; 29131; -. DR KEGG; rno:29131; -. DR UCSC; RGD:2272; rat. [P49192-1] DR AGR; RGD:2272; -. 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; CNCPRGA; -. DR OrthoDB; 3971848at2759; -. DR PhylomeDB; P49192; -. DR TreeFam; TF332948; -. DR PRO; PR:P49192; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000017712; Expressed in duodenum and 10 other cell types or tissues. 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: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:0001678; P:intracellular glucose homeostasis; ISS:HGNC-UCL. 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 CDD; cd22741; CART_CTD-like; 1. DR Gene3D; 4.10.40.30; CART, C-terminal domain; 1. DR InterPro; IPR009106; CART. DR InterPro; IPR036722; CART_C_sf. DR PANTHER; PTHR16655; COCAINE AND AMPHETAMINE REGULATED TRANSCRIPT PROTEIN; 1. DR PANTHER; PTHR16655:SF0; COCAINE- AND AMPHETAMINE-REGULATED TRANSCRIPT PROTEIN; 1. DR Pfam; PF06373; CART; 1. DR SUPFAM; SSF64546; Satiety factor CART (cocaine and amphetamine regulated transcript); 1. DR Genevisible; P49192; RN. 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 //