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Q16568 (CART_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cocaine- and amphetamine-regulated transcript protein

Cleaved into the following 2 chains:

  1. CART(1-39)
  2. CART(42-89)
Gene names
Name:CARTPT
Synonyms:CART
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length116 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Satiety factor closely associated with the actions of leptin and neuropeptide y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. It promotes neuronal development and survival in vitro. Ref.6

Subcellular location

Secreted Potential.

Tissue specificity

Hypothalamus. Found in neurons of the ventrolateral part of the arcuate nucleus, in the external zone of the median eminence, and also found in terminals in the periventricular part of the paraventricular nucleus.

Induction

By leptin.

Sequence similarities

Belongs to the CART family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseObesity
   DomainSignal
   Molecular functionNeuropeptide
Neurotransmitter
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity PubMed 15908120. Source: HGNC

activation of MAPKK activity

Inferred from sequence or structural similarity PubMed 15908120. Source: HGNC

adult feeding behavior

Inferred from sequence or structural similarity. Source: HGNC

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

cellular glucose homeostasis

Inferred from direct assay PubMed 11711504. Source: HGNC

cellular response to starvation

Inferred from sequence or structural similarity PubMed 15680948. Source: HGNC

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of appetite

Inferred from sequence or structural similarity. Source: HGNC

negative regulation of bone resorption

Inferred from mutant phenotype PubMed 16614075. Source: HGNC

negative regulation of glucagon secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of osteoclast differentiation

Traceable author statement PubMed 16614075. Source: HGNC

neuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of blood pressure

Inferred from direct assay PubMed 11711504. Source: HGNC

positive regulation of epinephrine secretion

Inferred from direct assay PubMed 11711504. Source: HGNC

positive regulation of transmission of nerve impulse

Inferred from direct assay PubMed 11711504. Source: HGNC

regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

somatostatin secretion

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from direct assay PubMed 11711504. Source: HGNC

secretory granule

Inferred from direct assay PubMed 21624661. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CEACAM1P136883EBI-4314526,EBI-4314481
CEACAM6P401993EBI-4314526,EBI-4314501

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.5
Chain28 – 11689Cocaine- and amphetamine-regulated transcript protein
PRO_0000004433
Peptide28 – 6639CART(1-39)
PRO_0000004434
Peptide69 – 11648CART(42-89)
PRO_0000004435

Amino acid modifications

Disulfide bond82 ↔ 100
Disulfide bond88 ↔ 108
Disulfide bond102 ↔ 115

Natural variations

Natural variant611L → F Cosegregates with obesity phenotype in a large family. Ref.9
VAR_012199
Natural variant661S → T. Ref.8
Corresponds to variant rs78242624 [ dbSNP | Ensembl ].
VAR_012200
Natural variant1131L → M.
Corresponds to variant rs12517689 [ dbSNP | Ensembl ].
VAR_053022

Secondary structure

......... 116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16568 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FC396CA2C032AA83

FASTA11612,829
        10         20         30         40         50         60 
MESSRVRLLP LLGAALLLML PLLGTRAQED AELQPRALDI YSAVDDASHE KELIEALQEV 

        70         80         90        100        110 
LKKLKSKRVP IYEKKYGQVP MCDAGEQCAV RKGARIGKLC DCPRGTSCNS FLLKCL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the human cDNA and genomic DNA encoding CART: a cocaine- and amphetamine-regulated transcript."
Douglass J.O., Daoud S.
Gene 169:241-245(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-42.
[6]"Hypothalamic CART is a new anorectic peptide regulated by leptin."
Kristensen P., Judge M.E., Thim L., Ribel U., Christjansen K.N., Wulff B.S., Clausen J.T., Jensen P.B., Madsen O.D., Vrang N., Larsen P.J., Hastrup S.
Nature 393:72-76(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Solution structure of the satiety factor, CART, reveals new functionality of a well-known fold."
Ludvigsen S., Thim L., Blom A.M., Wulff B.S.
Biochemistry 40:9082-9088(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 75-116.
[8]"The CART gene and human obesity: mutational analysis and population genetics."
Challis B.G., Yeo G.S.H., Farooqi I.S., Luan J., Aminian S., Halsall D.J., Keogh J.M., Wareham N.J., O'Rahilly S.
Diabetes 49:872-875(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-66.
[9]"Mutational screening of the CART gene in obese children: identifying a mutation (Leu34Phe) associated with reduced resting energy expenditure and cosegregating with obesity phenotype in a large family."
del Giudice E.M., Santoro N., Cirillo G., D'Urso L., Di Toro R., Perrone L.
Diabetes 50:2157-2160(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PHE-61.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16826 mRNA. Translation: AAB08010.1.
U20325 Genomic DNA. Translation: AAB08011.1.
CR542216 mRNA. Translation: CAG47012.1.
CH471084 Genomic DNA. Translation: EAW95694.1.
BC029882 mRNA. Translation: AAH29882.1.
PIRJC4669.
RefSeqNP_004282.1. NM_004291.3.
UniGeneHs.1707.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HY9NMR-A76-116[»]
ProteinModelPortalQ16568.
SMRQ16568. Positions 76-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114970. 2 interactions.
IntActQ16568. 2 interactions.
STRING9606.ENSP00000296777.

Chemistry

DrugBankDB00182. Amphetamine.

PTM databases

PhosphoSiteQ16568.

Polymorphism databases

DMDM2833274.

Proteomic databases

PaxDbQ16568.
PRIDEQ16568.

Protocols and materials databases

DNASU9607.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296777; ENSP00000296777; ENSG00000164326.
GeneID9607.
KEGGhsa:9607.
UCSCuc003kbv.2. human.

Organism-specific databases

CTD9607.
GeneCardsGC05P071051.
HGNCHGNC:24323. CARTPT.
HPAHPA046278.
MIM602606. gene.
neXtProtNX_Q16568.
PharmGKBPA162381084.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47455.
HOGENOMHOG000111306.
HOVERGENHBG018929.
InParanoidQ16568.
OMASHEKELP.
OrthoDBEOG7JDR0T.
PhylomeDBQ16568.
TreeFamTF332948.

Gene expression databases

BgeeQ16568.
CleanExHS_CARTPT.
GenevestigatorQ16568.

Family and domain databases

Gene3D4.10.40.30. 1 hit.
InterProIPR009106. CART.
[Graphical view]
PANTHERPTHR16655. PTHR16655. 1 hit.
PfamPF06373. CART. 1 hit.
[Graphical view]
SUPFAMSSF64546. SSF64546. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ16568.
GenomeRNAi9607.
NextBio36043.
PROQ16568.
SOURCESearch...

Entry information

Entry nameCART_HUMAN
AccessionPrimary (citable) accession number: Q16568
Secondary accession number(s): Q6FG92
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM