CFC1_CHICK
ID CFC1_CHICK Reviewed; 193 AA.
AC Q9I8Q3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cryptic protein;
DE AltName: Full=Cripto-related factor 1;
DE Flags: Precursor;
GN Name=CFC1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND DEVELOPMENTAL
RP STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schlange T., Schnipkoweit I., Andree B., Ebert A., Zile M.H., Arnold H.-H.,
RA Brand T.;
RT "Dual function of chicken cryptic in the determination of left-right
RT asymmetry: control of midline barrier formation and lateralization of the
RT lateral plate mesoderm.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in mesoderm and/or neural patterning during
CC gastrulation. {ECO:0000269|PubMed:11024280}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: First detected in the early streak embryo,
CC specifically in the epiblast layer. At the late streak stage,
CC expression is condensed in the rostral half of the primitive streak. At
CC HH stage 4 expression appeared for the first time in the mesendodermal
CC layer of the presumptive prechordal plate rostrally and in the
CC expanding mesoderm laterally. At HH stage 6, labeling in mesendodermal
CC progenitors underlying the future forebrain level of the neuraxis
CC reached its maximum, whereas mesoderm expression, which was restricted
CC to the lateral plate, was accompanied by an underlying endodermal
CC expression at the level of the heart-forming regions. Later
CC gastrulation (HH stage 5-7) was marked by strong expression in the
CC notochord, beneath the future floor plate of the neural tube. Expressed
CC in Hensen node, within its mesenchymal core beneath the epiblast, and
CC at a time when it is morphologically asymmetric.
CC {ECO:0000269|PubMed:11024280}.
CC -!- SIMILARITY: Belongs to the EGF-CFC (Cripto-1/FRL1/Cryptic) family.
CC {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; AF228760; AAF97868.1; -; mRNA.
DR EMBL; AF228762; AAF97869.1; -; Genomic_DNA.
DR EMBL; AF228761; AAF97869.1; JOINED; Genomic_DNA.
DR EMBL; AF282984; AAK07089.1; -; mRNA.
DR RefSeq; NP_990031.1; NM_204700.2.
DR AlphaFoldDB; Q9I8Q3; -.
DR SMR; Q9I8Q3; -.
DR STRING; 9031.ENSGALP00000020578; -.
DR PaxDb; Q9I8Q3; -.
DR Ensembl; ENSGALT00000020607; ENSGALP00000020578; ENSGALG00000012623.
DR GeneID; 395437; -.
DR KEGG; gga:395437; -.
DR CTD; 55997; -.
DR VEuPathDB; HostDB:geneid_395437; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000162302; -.
DR HOGENOM; CLU_092661_0_0_1; -.
DR InParanoid; Q9I8Q3; -.
DR OMA; VFGALHC; -.
DR OrthoDB; 1387592at2759; -.
DR PhylomeDB; Q9I8Q3; -.
DR TreeFam; TF333187; -.
DR PRO; PR:Q9I8Q3; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000012623; Expressed in spermatocyte and 7 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0070697; F:activin receptor binding; IBA:GO_Central.
DR GO; GO:0038100; F:nodal binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0038092; P:nodal signaling pathway; IBA:GO_Central.
DR InterPro; IPR019011; Cryptic/Cripto_CFC-dom.
DR InterPro; IPR000742; EGF-like_dom.
DR Pfam; PF09443; CFC; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 2: Evidence at transcript 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..193
FT /note="Cryptic protein"
FT /id="PRO_0000044632"
FT DOMAIN 91..115
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 105..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 193 AA; 22332 MW; E859A98F2DE6325F CRC64;
MFWRKHVRIL FTVTLIWQAI HLGKGREKEH EKDVKNFNDT AQKQSPKNSV TIIDAFSDMN
QSYQSRKQQN SREFVPFTGI TESKNLNRNC CQNGGTCILG AFCACPKHFS GRHCELRKCG
SIIHGDWVMK GCWLCRCLYG TLKCLSQNTQ DGCELRREEE IIRLYSNGLR LQQTMSALIC
LLTFLLELCC WQL