ID   CFC1_MOUSE              Reviewed;         202 AA.
AC   P97766; Q496U5; Q9JIB7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   04-NOV-2026, entry version 150.
DE   RecName: Full=Cryptic protein;
DE   Flags: Precursor;
GN   Name=Cfc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND GLYCOSYLATION.
RC   STRAIN=129/Sv;
RX   PubMed=9053319; DOI=10.1242/dev.124.2.429;
RA   Shen M.M., Wang H., Leder P.;
RT   "A differential display strategy identifies Cryptic, a novel EGF-related
RT   gene expressed in the axial and lateral mesoderm during mouse
RT   gastrulation.";
RL   Development 124:429-442(1997).
RN   [2]
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154.
RX   PubMed=11024280; DOI=10.1016/s0378-1119(00)00337-1;
RA   Colas J.-F., Schoenwolf G.C.;
RT   "Subtractive hybridization identifies chick-cripto, a novel EGF-CFC
RT   ortholog expressed during gastrulation, neurulation and early
RT   cardiogenesis.";
RL   Gene 255:205-217(2000).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10574770; DOI=10.1016/s0960-9822(00)80059-7;
RA   Gaio U., Schweickert A., Fischer A., Garratt A.N., Mueller T., Oezcelik C.,
RA   Lankes W., Strehle M., Britsch S., Blum M., Birchmeier C.;
RT   "A role of the cryptic gene in the correct establishment of the left-right
RT   axis.";
RL   Curr. Biol. 9:1339-1342(1999).
CC   -!- FUNCTION: Nodal coreceptor involved in the correct establishment of the
CC       left-right axis. May play a role in mesoderm and/or neural patterning
CC       during gastrulation. {ECO:0000269|PubMed:10574770,
CC       ECO:0000269|PubMed:9053319}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}. Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: No expressed in adult tissues.
CC       {ECO:0000269|PubMed:9053319}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during gastrulation (from 6.5 dpc to 11
CC       dpc) in two spatial domains that correspond to the axial and lateral
CC       mesoderm. In the first domain expression is progressively localized to
CC       the anterior primitive streak, the head process, and the node and
CC       notochordal. In the second domain, expression is initially concentrated
CC       in the lateral region of the egg cylinder, and is later found
CC       circumferentially in the intermediate and lateral plate mesoderm.
CC       Furthermore, the expression can also be detected at the early head-fold
CC       stage in the midline neuroectoderm, and consequently is an early marker
CC       for the prospective floor plate of the neural tube. Expression ceases
CC       at the end of gastrulation, and has not been observed in later
CC       embryonic stages. {ECO:0000269|PubMed:9053319}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9053319}.
CC   -!- DISRUPTION PHENOTYPE: Positional defects in internal organs. The lung
CC       presents a right pulmonary isomerism. The stomach is located on either
CC       the left or the right and the spleen is small and has an abnormal
CC       shape. The apex of the heart pointed to the right or left. In addition
CC       malpositioning of heart outflow tracts is observed, the aorta is
CC       connected to the right ventricle and emerged from the heart in a
CC       ventral position and to the right of the pulmonary artery. This one is
CC       connected to either the left or the right ventricle.
CC       {ECO:0000269|PubMed:10574770}.
CC   -!- SIMILARITY: Belongs to the EGF-CFC (Cripto-1/FRL1/Cryptic) family.
CC       {ECO:0000305}.
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DR   EMBL; U57720; AAC53042.1; -; mRNA.
DR   EMBL; BC100705; AAI00706.1; -; mRNA.
DR   EMBL; BC100706; AAI00707.1; -; mRNA.
DR   EMBL; BC100708; AAI00709.1; -; mRNA.
DR   EMBL; BC100711; AAI00712.1; -; mRNA.
DR   EMBL; AF242430; AAF76323.1; -; Genomic_DNA.
DR   CCDS; CCDS14869.1; -.
DR   RefSeq; NP_031711.1; NM_007685.3.
DR   BioGRID; 198681; 3.
DR   STRING; 10090.ENSMUSP00000027298; -.
DR   GlyCosmos; P97766; 1 site, No reported glycans.
DR   GlyGen; P97766; 1 site.
DR   PhosphoSitePlus; P97766; -.
DR   PaxDb; 10090-ENSMUSP00000027298; -.
DR   DNASU; 12627; -.
DR   Ensembl; ENSMUST00000027298.5; ENSMUSP00000027298.4; ENSMUSG00000026124.5.
DR   GeneID; 12627; -.
DR   KEGG; mmu:12627; -.
DR   UCSC; uc007aow.1; mouse.
DR   CTD; 55997; -.
DR   VEuPathDB; HostDB:ENSMUSG00000026124; -.
DR   AGR; MGI:109448; -.
DR   MGI; MGI:109448; Cfc1.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00940000162302; -.
DR   HOGENOM; CLU_092661_0_0_1; -.
DR   InParanoid; P97766; -.
DR   OMA; AWTLQSC; -.
DR   OrthoDB; 9893603at2759; -.
DR   PhylomeDB; P97766; -.
DR   PRO; PR:P97766; -.
DR   Bgee; ENSMUSG00000026124; Expressed in mesodermal cell in embryo and 26 other cell types or tissues.
DR   CDD; cd00054; EGF_CA; 1.
DR   FunFam; 2.10.25.10:FF:000421; Teratocarcinoma-derived growth factor; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR019011; Cryptic/Cripto_CFC-dom.
DR   InterPro; IPR000742; EGF.
DR   PANTHER; PTHR14949:SF25; CRYPTIC FAMILY PROTEIN 1B-RELATED; 1.
DR   PANTHER; PTHR14949; EGF-LIKE-DOMAIN, MULTIPLE 7, 8; 1.
DR   Pfam; PF09443; CFC; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0070697; F:activin receptor binding; IPI:UniProtKB.
DR   GO; GO:0038100; F:nodal binding; ISO:GO_Central.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR   GO; GO:0060413; P:atrial septum morphogenesis; IMP:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
DR   GO; GO:0007492; P:endoderm development; IGI:MGI.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0060460; P:left lung morphogenesis; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0038092; P:nodal signaling pathway; IMP:UniProtKB.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0060541; P:respiratory system development; IMP:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IBA:GO_Central.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P97766; protein.
DR   BioGRID-ORCS; 12627; 2 hits in 75 CRISPR screens.
DR   AlphaFoldDB; P97766; -.
DR   FunCoup; P97766; 73.
PE   1: Evidence at protein level;
KW   Cell membrane; Developmental protein; Disulfide bond; EGF-like domain;
KW   Gastrulation; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..166
FT                   /note="Cryptic protein"
FT                   /id="PRO_0000044631"
FT   PROPEP          167..202
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000395409"
FT   DOMAIN          94..123
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   LIPID           166
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        98..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        99..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        113..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CONFLICT        83
FT                   /note="P -> T (in Ref. 2; AAI00707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  21792 MW;  57035AD339A16FD7 CRC64;
     MRANSPTQGI SLKMHQARPL FLVTVALQLI GLGYSYQSEG DGAREVSNIL SPVIPGTTLD
     RTLSNSSRKN DIPEGARLWD SLPDSSTLGE SAVPVSRCCH NGGTCVLGSF CVCPAYFTGR
     YCEHDQRRRD CGALGHGAWT LHSCRLCRCI FSALYCLPHQ TFSHCDLKSF LSSGARGSRE
     CSIPSLLLLV LCLLLQGVAG KG
//