ID UTS2_HUMAN Reviewed; 124 AA. AC O95399; Q5H8X7; Q6UXF6; Q9UKP7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-FEB-2019, entry version 148. DE RecName: Full=Urotensin-2; DE AltName: Full=Urotensin II; DE Short=U-II; DE Short=UII; DE Flags: Precursor; GN Name=UTS2; ORFNames=UNQ525/PRO1068; 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] (ISOFORM 1). RC TISSUE=Spinal cord; RX PubMed=9861051; DOI=10.1073/pnas.95.26.15803; RA Coulouarn Y., Lihrmann I., Jegou S., Anouar Y., Tostivint H., RA Beauvillain J.-C., Conlon J.M., Bern H.A., Vaudry H.; RT "Cloning of the cDNA encoding the urotensin II precursor in frog and RT human reveals intense expression of the urotensin II gene in RT motoneurons of the spinal cord."; RL Proc. Natl. Acad. Sci. U.S.A. 95:15803-15808(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10499587; DOI=10.1038/45809; RA Ames R.S., Sarau H.M., Chambers J.K., Willette R.N., Aiyar N.V., RA Romanic A.M., Louden C.S., Foley J.J., Sauermelch C.F., Coatney R.W., RA Ao Z., Disa J., Holmes S.D., Stadel J.M., Martin J.D., Liu W.-S., RA Glover G.I., Wilson S., McNulty D.E., Ellis C.E., Elshourbagy N.A., RA Shabon U., Trill J.J., Hay D.W.P., Ohlstein E.H., Bergsma D.J., RA Douglas S.A.; RT "Human urotensin-II is a potent vasoconstrictor and agonist for the RT orphan receptor GPR14."; RL Nature 401:282-286(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP THR-12. 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). RN [4] 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 [5] RP PROTEIN SEQUENCE OF 21-35 (ISOFORM 1). RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). CC -!- FUNCTION: Highly potent vasoconstrictor. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95399-1; Sequence=Displayed; CC Name=2; CC IsoId=O95399-2; Sequence=VSP_013638; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Brain specific. CC -!- SIMILARITY: Belongs to the urotensin-2 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; AF104118; AAD13070.1; -; mRNA. DR EMBL; AF140630; AAD55577.1; -; mRNA. DR EMBL; AY358375; AAQ88741.1; -; mRNA. DR EMBL; Z98884; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS90.1; -. [O95399-2] DR CCDS; CCDS91.1; -. [O95399-1] DR RefSeq; NP_006777.1; NM_006786.3. [O95399-1] DR RefSeq; NP_068835.1; NM_021995.2. [O95399-2] DR RefSeq; XP_011538839.1; XM_011540537.2. [O95399-2] DR RefSeq; XP_011538840.1; XM_011540538.1. [O95399-1] DR UniGene; Hs.715862; -. DR ProteinModelPortal; O95399; -. DR SMR; O95399; -. DR BioGrid; 116116; 2. DR IntAct; O95399; 2. DR BindingDB; O95399; -. DR BioMuta; UTS2; -. DR EPD; O95399; -. DR jPOST; O95399; -. DR MaxQB; O95399; -. DR PeptideAtlas; O95399; -. DR PRIDE; O95399; -. DR ProteomicsDB; 50851; -. DR ProteomicsDB; 50852; -. [O95399-2] DR DNASU; 10911; -. DR Ensembl; ENST00000054668; ENSP00000054668; ENSG00000049247. [O95399-2] DR Ensembl; ENST00000361696; ENSP00000355163; ENSG00000049247. [O95399-1] DR GeneID; 10911; -. DR KEGG; hsa:10911; -. DR UCSC; uc001aor.4; human. [O95399-1] DR CTD; 10911; -. DR DisGeNET; 10911; -. DR EuPathDB; HostDB:ENSG00000049247.13; -. DR GeneCards; UTS2; -. DR HGNC; HGNC:12636; UTS2. DR HPA; HPA017000; -. DR MIM; 604097; gene. DR neXtProt; NX_O95399; -. DR OpenTargets; ENSG00000049247; -. DR PharmGKB; PA37261; -. DR GeneTree; ENSGT00510000049583; -. DR HOGENOM; HOG000136847; -. DR HOVERGEN; HBG065793; -. DR InParanoid; O95399; -. DR KO; K05248; -. DR OMA; RKFQAFS; -. DR OrthoDB; 1506988at2759; -. DR PhylomeDB; O95399; -. DR TreeFam; TF330799; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR ChiTaRS; UTS2; human. DR GeneWiki; UTS2; -. DR GenomeRNAi; 10911; -. DR PRO; PR:O95399; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000049247; Expressed in 91 organ(s), highest expression level in adrenal tissue. DR ExpressionAtlas; O95399; baseline and differential. DR Genevisible; O95399; HS. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005179; F:hormone activity; TAS:ProtInc. DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc. DR GO; GO:0097746; P:regulation of blood vessel diameter; IEA:InterPro. DR InterPro; IPR001483; Urotensin_II. DR Pfam; PF02083; Urotensin_II; 1. DR PROSITE; PS00984; UROTENSIN_II; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cleavage on pair of basic residues; KW Complete proteome; Direct protein sequencing; Disulfide bond; Hormone; KW Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 20 FT PROPEP 21 110 FT /FTId=PRO_0000036346. FT PEPTIDE 114 124 Urotensin-2. FT /FTId=PRO_0000036347. FT DISULFID 118 123 {ECO:0000250}. FT VAR_SEQ 1 27 MYKLASCCLLFIGFLNPLLSLPLLDSR -> METNVFHLML FT CVTSARTHKSTSLCFGHFNSYPSLPLIHDLLL (in FT isoform 2). FT {ECO:0000303|PubMed:10499587}. FT /FTId=VSP_013638. FT VARIANT 12 12 I -> T (in dbSNP:rs34305100). FT {ECO:0000269|PubMed:12975309}. FT /FTId=VAR_053734. FT VARIANT 74 74 S -> N (in dbSNP:rs2890565). FT /FTId=VAR_029313. SQ SEQUENCE 124 AA; 14296 MW; C7A5FC7EFE00D312 CRC64; MYKLASCCLL FIGFLNPLLS LPLLDSREIS FQLSAPHEDA RLTPEELERA SLLQILPEML GAERGDILRK ADSSTNIFNP RGNLRKFQDF SGQDPNILLS HLLARIWKPY KKRETPDCFW KYCV //