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   24-JAN-2024, entry version 156.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., 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., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., 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., Rogers J.,
RA   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 AND
RP   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 project:
RT   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 verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
CC   -!- FUNCTION: Cytokine that may play a role in anterior neural induction
CC       and somite formation during embryogenesis in part through a BMP-
CC       inhibitory mechanism. Can regulate Nodal signaling during gastrulation
CC       as well as the formation and patterning of the primitive streak (By
CC       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; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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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   AlphaFoldDB; O95813; -.
DR   BioGRID; 114753; 17.
DR   IntAct; O95813; 6.
DR   STRING; 9606.ENSP00000370297; -.
DR   GlyCosmos; O95813; 2 sites, No reported glycans.
DR   GlyGen; O95813; 2 sites.
DR   iPTMnet; O95813; -.
DR   PhosphoSitePlus; O95813; -.
DR   BioMuta; CER1; -.
DR   jPOST; O95813; -.
DR   MassIVE; O95813; -.
DR   PaxDb; 9606-ENSP00000370297; -.
DR   PeptideAtlas; O95813; -.
DR   ProteomicsDB; 51063; -.
DR   Antibodypedia; 10019; 279 antibodies from 31 providers.
DR   DNASU; 9350; -.
DR   Ensembl; ENST00000380911.4; ENSP00000370297.3; ENSG00000147869.5.
DR   GeneID; 9350; -.
DR   KEGG; hsa:9350; -.
DR   MANE-Select; ENST00000380911.4; ENSP00000370297.3; NM_005454.3; NP_005445.1.
DR   UCSC; uc003zlj.4; human.
DR   AGR; HGNC:1862; -.
DR   CTD; 9350; -.
DR   DisGeNET; 9350; -.
DR   GeneCards; CER1; -.
DR   HGNC; HGNC:1862; CER1.
DR   HPA; ENSG00000147869; Tissue enhanced (epididymis).
DR   MIM; 603777; gene.
DR   neXtProt; NX_O95813; -.
DR   OpenTargets; ENSG00000147869; -.
DR   PharmGKB; PA26417; -.
DR   VEuPathDB; HostDB:ENSG00000147869; -.
DR   eggNOG; ENOG502S2G4; Eukaryota.
DR   GeneTree; ENSGT00530000063926; -.
DR   HOGENOM; CLU_104447_0_0_1; -.
DR   InParanoid; O95813; -.
DR   OMA; FCSHCSP; -.
DR   OrthoDB; 5347549at2759; -.
DR   PhylomeDB; O95813; -.
DR   TreeFam; TF106445; -.
DR   PathwayCommons; O95813; -.
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   SignaLink; O95813; -.
DR   BioGRID-ORCS; 9350; 12 hits in 1132 CRISPR screens.
DR   GeneWiki; Cerberus_(protein); -.
DR   GenomeRNAi; 9350; -.
DR   Pharos; O95813; Tbio.
DR   PRO; PR:O95813; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; O95813; Protein.
DR   Bgee; ENSG00000147869; Expressed in primordial germ cell in gonad and 39 other cell types or tissues.
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:0030282; P:bone mineralization; IMP:BHF-UCL.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; ISS:BHF-UCL.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
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: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; Cystine-knot cytokines; 1.
DR   InterPro; IPR016860; Cerberus.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR004133; DAN.
DR   PANTHER; PTHR15273:SF4; CERBERUS; 1.
DR   PANTHER; PTHR15273; DAN DOMAIN FAMILY MEMBER 5; 1.
DR   Pfam; PF03045; DAN; 1.
DR   PIRSF; PIRSF027807; Cerberus; 1.
DR   SMART; SM00041; CT; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   Genevisible; O95813; HS.
PE   1: Evidence at protein level;
KW   Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           18..267
FT                   /note="Cerberus"
FT                   /id="PRO_0000006711"
FT   DOMAIN          162..246
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   REGION          19..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        162..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        176..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        186..239
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        190..241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   VARIANT         19
FT                   /note="R -> W (in dbSNP:rs10115703)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_021591"
FT   VARIANT         65
FT                   /note="A -> G (in dbSNP:rs3747532)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_021592"
FT   VARIANT         179
FT                   /note="V -> I (in dbSNP:rs7036635)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_021593"
FT   CONFLICT        57
FT                   /note="F -> L (in Ref. 4; AAH69503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="L -> V (in Ref. 4; AAH69405)"
FT                   /evidence="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
//