ID CER1_HUMAN Reviewed; 267 AA. AC O95813; Q6ISJ1; Q6ISJ6; Q6ISQ2; Q6ISS1; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-FEB-2019, entry version 131. DE RecName: Full=Cerberus; DE AltName: Full=Cerberus-related protein; DE AltName: Full=DAN domain family member 4; DE Flags: Precursor; GN Name=CER1; Synonyms=DAND4; 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=Blood; RX PubMed=10049596; DOI=10.1006/geno.1998.5671; RA Lah M., Brodnicki T., Maccarone P., Nash A., Stanley E., Harvey R.P.; RT "Human cerberus related gene CER1 maps to chromosome 9."; RL Genomics 55:364-366(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Feng Z., Zhang B., Peng X., Yuan J., Qiang B.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TRP-19; GLY-65 RP AND ILE-179. 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 [5] RP PROTEIN SEQUENCE OF 18-32. 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: Cytokine that may play a role in anterior neural CC induction and somite formation during embryogenesis in part CC through a BMP-inhibitory mechanism. Can regulate Nodal signaling CC during gastrulation as well as the formation and patterning of the CC primitive streak (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Forms monomers and predominantly dimers. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DAN family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH69503.1; Type=Erroneous termination; Positions=266; Note=Translated as Ser.; 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; AF090189; AAD19879.1; -; Genomic_DNA. DR EMBL; AF400435; AAK92484.1; -; mRNA. DR EMBL; AL390732; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069371; AAH69371.1; -; mRNA. DR EMBL; BC069405; AAH69405.1; -; mRNA. DR EMBL; BC069491; AAH69491.1; -; mRNA. DR EMBL; BC069503; AAH69503.1; ALT_SEQ; mRNA. DR CCDS; CCDS6476.1; -. DR RefSeq; NP_005445.1; NM_005454.2. DR UniGene; Hs.248204; -. DR ProteinModelPortal; O95813; -. DR SMR; O95813; -. DR BioGrid; 114753; 14. DR STRING; 9606.ENSP00000370297; -. DR iPTMnet; O95813; -. DR PhosphoSitePlus; O95813; -. DR BioMuta; CER1; -. DR PaxDb; O95813; -. DR PeptideAtlas; O95813; -. DR PRIDE; O95813; -. DR ProteomicsDB; 51063; -. DR DNASU; 9350; -. DR Ensembl; ENST00000380911; ENSP00000370297; ENSG00000147869. DR GeneID; 9350; -. DR KEGG; hsa:9350; -. DR UCSC; uc003zlj.4; human. DR CTD; 9350; -. DR DisGeNET; 9350; -. DR EuPathDB; HostDB:ENSG00000147869.4; -. DR GeneCards; CER1; -. DR H-InvDB; HIX0034784; -. DR HGNC; HGNC:1862; CER1. DR HPA; HPA019917; -. DR MIM; 603777; gene. DR neXtProt; NX_O95813; -. DR OpenTargets; ENSG00000147869; -. DR PharmGKB; PA26417; -. DR eggNOG; ENOG410IGR5; Eukaryota. DR eggNOG; ENOG410YX4Y; LUCA. DR GeneTree; ENSGT00530000063926; -. DR HOGENOM; HOG000231309; -. DR HOVERGEN; HBG050902; -. DR InParanoid; O95813; -. DR KO; K01645; -. DR OMA; CFGKCGS; -. DR OrthoDB; 1134947at2759; -. DR PhylomeDB; O95813; -. DR TreeFam; TF106445; -. DR Reactome; R-HSA-1181150; Signaling by NODAL. DR Reactome; R-HSA-1433617; Regulation of signaling by NODAL. DR Reactome; R-HSA-201451; Signaling by BMP. DR GeneWiki; Cerberus_(protein); -. DR GenomeRNAi; 9350; -. DR PRO; PR:O95813; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; ENSG00000147869; Expressed in 24 organ(s), highest expression level in right hemisphere of cerebellum. DR Genevisible; O95813; HS. DR GO; GO:0005576; C:extracellular region; ISS:BHF-UCL. DR GO; GO:0005615; C:extracellular space; ISS:BHF-UCL. DR GO; GO:0036122; F:BMP binding; IDA:BHF-UCL. DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW. DR GO; GO:0016015; F:morphogen activity; IDA:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL. DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:BHF-UCL. DR GO; GO:0009952; P:anterior/posterior pattern specification; ISS:BHF-UCL. DR GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome. DR GO; GO:0030282; P:bone mineralization; IMP:BHF-UCL. DR GO; GO:0042074; P:cell migration involved in gastrulation; ISS:BHF-UCL. DR GO; GO:0071773; P:cellular response to BMP stimulus; ISS:BHF-UCL. DR GO; GO:0048263; P:determination of dorsal identity; IMP:BHF-UCL. DR GO; GO:0061371; P:determination of heart left/right asymmetry; IBA:GO_Central. DR GO; GO:0007369; P:gastrulation; ISS:BHF-UCL. DR GO; GO:0003419; P:growth plate cartilage chondrocyte proliferation; ISS:BHF-UCL. DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:BHF-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:BHF-UCL. DR GO; GO:2000381; P:negative regulation of mesoderm development; IMP:BHF-UCL. DR GO; GO:1900176; P:negative regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; IMP:BHF-UCL. DR GO; GO:0035582; P:sequestering of BMP in extracellular matrix; IDA:BHF-UCL. DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISS:BHF-UCL. DR GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB. DR Gene3D; 2.10.90.10; -; 1. DR InterPro; IPR016860; Cerberus. DR InterPro; IPR006207; Cys_knot_C. DR InterPro; IPR029034; Cystine-knot_cytokine. DR InterPro; IPR004133; DAN. DR PANTHER; PTHR15273; PTHR15273; 1. DR Pfam; PF03045; DAN; 1. DR PIRSF; PIRSF027807; Cerberus; 1. DR SMART; SM00041; CT; 1. DR PROSITE; PS01225; CTCK_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytokine; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Polymorphism; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 17 {ECO:0000269|PubMed:15340161}. FT CHAIN 18 267 Cerberus. FT /FTId=PRO_0000006711. FT DOMAIN 162 246 CTCK. {ECO:0000255|PROSITE- FT ProRule:PRU00039}. FT CARBOHYD 26 26 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 222 222 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 162 209 {ECO:0000255|PROSITE-ProRule:PRU00039}. FT DISULFID 176 223 {ECO:0000255|PROSITE-ProRule:PRU00039}. FT DISULFID 186 239 {ECO:0000255|PROSITE-ProRule:PRU00039}. FT DISULFID 190 241 {ECO:0000255|PROSITE-ProRule:PRU00039}. FT VARIANT 19 19 R -> W (in dbSNP:rs10115703). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_021591. FT VARIANT 65 65 A -> G (in dbSNP:rs3747532). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_021592. FT VARIANT 179 179 V -> I (in dbSNP:rs7036635). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_021593. FT CONFLICT 57 57 F -> L (in Ref. 4; AAH69503). FT {ECO:0000305}. FT CONFLICT 221 221 L -> V (in Ref. 4; AAH69405). FT {ECO:0000305}. SQ SEQUENCE 267 AA; 30084 MW; C9FB048CD8558ED7 CRC64; MHLLLFQLLV LLPLGKTTRH QDGRQNQSSL SPVLLPRNQR ELPTGNHEEA EEKPDLFVAV PHLVATSPAG EGQRQREKML SRFGRFWKKP EREMHPSRDS DSEPFPPGTQ SLIQPIDGMK MEKSPLREEA KKFWHHFMFR KTPASQGVIL PIKSHEVHWE TCRTVPFSQT ITHEGCEKVV VQNNLCFGKC GSVHFPGAAQ HSHTSCSHCL PAKFTTMHLP LNCTELSSVI KVVMLVEECQ CKVKTEHEDG HILHAGSQDS FIPGVSA //