ID CORT_HUMAN Reviewed; 105 AA. AC O00230; Q5T6G0; Q6UX11; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 13-FEB-2019, entry version 128. DE RecName: Full=Cortistatin; DE Contains: DE RecName: Full=Cortistatin-29; DE Contains: DE RecName: Full=Cortistatin-17; DE Flags: Precursor; GN Name=CORT; ORFNames=UNQ307/PRO350; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=9125122; DOI=10.1006/bbrc.1997.6252; RA Fukusumi S., Kitada C., Takekawa S., Kizawa H., Sakamoto J., RA Miyamoto M., Hinuma S., Kitano K., Fujino M.; RT "Identification and characterization of a novel human cortistatin-like RT peptide."; RL Biochem. Biophys. Res. Commun. 232:157-163(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9205124; DOI=10.1006/geno.1997.4763; RA de Lecea L., Ruiz-Lozano P., Danielson P.E., Peelle-Kirley J., RA Foye P.E., Frankel W.N., Sutcliffe J.G.; RT "Cloning, mRNA expression, and chromosomal mapping of mouse and human RT preprocortistatin."; RL Genomics 42:499-506(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-104. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). CC -!- FUNCTION: Binds to all human somatostatin receptor (SSTR) CC subtypes. It also inhibits cAMP production induced by forskolin CC through SSTRs. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed in a subset of GABAergic cells in CC the cortex and hippocampus. CC -!- SIMILARITY: Belongs to the somatostatin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI19725.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAI19726.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAQ89950.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=EAW71650.1; Type=Erroneous initiation; Evidence={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; AB000263; BAA19770.1; -; mRNA. DR EMBL; AF013252; AAB66895.1; -; mRNA. DR EMBL; AL354956; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471130; EAW71650.1; ALT_INIT; Genomic_DNA. DR EMBL; BC119724; AAI19725.1; ALT_INIT; mRNA. DR EMBL; BC119725; AAI19726.1; ALT_INIT; mRNA. DR EMBL; AY358561; AAQ89950.1; ALT_INIT; mRNA. DR CCDS; CCDS117.2; -. DR PIR; JC5414; JC5414. DR RefSeq; NP_001293.3; NM_001302.4. DR UniGene; Hs.412311; -. DR ProteinModelPortal; O00230; -. DR BioGrid; 107718; 7. DR STRING; 9606.ENSP00000366248; -. DR iPTMnet; O00230; -. DR PhosphoSitePlus; O00230; -. DR BioMuta; CORT; -. DR jPOST; O00230; -. DR PaxDb; O00230; -. DR PeptideAtlas; O00230; -. DR PRIDE; O00230; -. DR ProteomicsDB; 47795; -. DR Ensembl; ENST00000377049; ENSP00000366248; ENSG00000241563. DR GeneID; 1325; -. DR KEGG; hsa:1325; -. DR UCSC; uc001ari.5; human. DR CTD; 1325; -. DR DisGeNET; 1325; -. DR EuPathDB; HostDB:ENSG00000241563.3; -. DR GeneCards; CORT; -. DR HGNC; HGNC:2257; CORT. DR MIM; 602784; gene. DR neXtProt; NX_O00230; -. DR OpenTargets; ENSG00000241563; -. DR PharmGKB; PA26773; -. DR eggNOG; ENOG410J3SG; Eukaryota. DR eggNOG; ENOG411196C; LUCA. DR GeneTree; ENSGT00730000111752; -. DR HOVERGEN; HBG017816; -. DR InParanoid; O00230; -. DR KO; K05238; -. DR OMA; RMPLPLC; -. DR OrthoDB; 1614009at2759; -. DR PhylomeDB; O00230; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SIGNOR; O00230; -. DR GeneWiki; Cortistatin_(neuropeptide); -. DR GenomeRNAi; 1325; -. DR PRO; PR:O00230; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000241563; Expressed in 83 organ(s), highest expression level in putamen. DR Genevisible; O00230; HS. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB. DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB. DR GO; GO:0005184; F:neuropeptide hormone activity; IDA:UniProtKB. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007268; P:chemical synaptic transmission; NAS:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR InterPro; IPR004250; Somatostatin. DR InterPro; IPR018142; Somatostatin/Cortistatin_C. DR Pfam; PF03002; Somatostatin; 1. DR PIRSF; PIRSF001814; Somatostatin; 1. PE 2: Evidence at transcript level; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW Hormone; Reference proteome; Secreted; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT PROPEP 19 74 {ECO:0000255}. FT /FTId=PRO_0000033154. FT PEPTIDE 77 105 Cortistatin-29. {ECO:0000255}. FT /FTId=PRO_0000033155. FT PEPTIDE 89 105 Cortistatin-17. FT /FTId=PRO_0000033156. FT DISULFID 93 104 {ECO:0000250}. SQ SEQUENCE 105 AA; 11532 MW; 09578F4520201551 CRC64; MPLSPGLLLL LLSGATATAA LPLEGGPTGR DSEHMQEAAG IRKSSLLTFL AWWFEWTSQA SAGPLIGEEA REVARRQEGA PPQQSARRDR MPCRNFFWKT FSSCK //