CART_BOVIN
ID CART_BOVIN Reviewed; 116 AA.
AC Q68RJ9; A4FUF3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Cocaine- and amphetamine-regulated transcript protein;
DE Contains:
DE RecName: Full=CART(1-39);
DE Contains:
DE RecName: Full=CART(42-89);
DE Flags: Precursor;
GN Name=CARTPT; Synonyms=CART;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15670137; DOI=10.1111/j.1365-2052.2004.01218.x;
RA Valle E., Moore S.S., Jann O., Williams J.L., Crews D.H., Benkel B.F.;
RT "The bovine cocaine and amphetamine-regulated transcript locus: gene
RT characterization and SNP discovery.";
RL Anim. Genet. 36:74-75(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the CART family. {ECO:0000305}.
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DR EMBL; AY603972; AAT99018.1; -; Genomic_DNA.
DR EMBL; BC114792; AAI14793.1; -; mRNA.
DR RefSeq; NP_001007821.1; NM_001007820.3.
DR AlphaFoldDB; Q68RJ9; -.
DR SMR; Q68RJ9; -.
DR STRING; 9913.ENSBTAP00000055162; -.
DR PaxDb; Q68RJ9; -.
DR PRIDE; Q68RJ9; -.
DR Ensembl; ENSBTAT00000064119; ENSBTAP00000055162; ENSBTAG00000047486.
DR GeneID; 493726; -.
DR KEGG; bta:493726; -.
DR CTD; 9607; -.
DR VEuPathDB; HostDB:ENSBTAG00000047486; -.
DR VGNC; VGNC:26774; CARTPT.
DR eggNOG; ENOG502S2YU; Eukaryota.
DR GeneTree; ENSGT00390000018319; -.
DR HOGENOM; CLU_157363_1_0_1; -.
DR InParanoid; Q68RJ9; -.
DR OMA; PRTGTMQ; -.
DR OrthoDB; 1562917at2759; -.
DR TreeFam; TF332948; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000047486; Expressed in Ammon's horn and 44 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:HGNC-UCL.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
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; ISS:HGNC-UCL.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISS:HGNC-UCL.
DR GO; GO:0009267; P:cellular response to starvation; ISS:HGNC-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:HGNC-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:HGNC-UCL.
DR GO; GO:0032099; P:negative regulation of appetite; ISS:HGNC-UCL.
DR GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:HGNC-UCL.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISS:HGNC-UCL.
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 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond; Neuropeptide;
KW Neurotransmitter; Obesity; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..116
FT /note="Cocaine- and amphetamine-regulated transcript
FT protein"
FT /id="PRO_0000256516"
FT PEPTIDE 28..66
FT /note="CART(1-39)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000256517"
FT PEPTIDE 69..116
FT /note="CART(42-89)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000256518"
FT MOD_RES 41
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49192"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56388"
FT DISULFID 82..100
FT /evidence="ECO:0000250"
FT DISULFID 88..108
FT /evidence="ECO:0000250"
FT DISULFID 102..115
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 12790 MW; 3664F4DBBE77106E CRC64;
MESPRLRLLP LLGAALLLLL PLLGALAQED AELQPRALDI YSAVEDASHE KELIEALQEV
LKKLKSKRIP IYEKKYGQVP MCDAGEQCAV RKGARIGKLC DCPRGTSCNS FLLKCL
