EGIP_HELCR
ID EGIP_HELCR Reviewed; 325 AA.
AC P15217; P15218; P15219;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Exogastrula-inducing polypeptide;
DE Short=EGIP;
DE Contains:
DE RecName: Full=Exogastrula-inducing peptide C;
DE Short=EGIP-C;
DE Contains:
DE RecName: Full=Exogastrula-inducing peptide D;
DE Short=EGIP-D;
DE Contains:
DE RecName: Full=Exogastrula-inducing peptide A;
DE Short=EGIP-A;
DE Contains:
DE RecName: Full=EGIP-X;
DE Flags: Precursor;
OS Heliocidaris crassispina (Sea urchin) (Anthocidaris crassispina).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinometridae;
OC Heliocidaris.
OX NCBI_TaxID=1043166;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=7705369; DOI=10.1111/j.1432-1033.1995.tb20291.x;
RA Yamasu K., Watanabe H., Kohchi C., Soma G., Mizuno D., Akasaka K.,
RA Shimada H., Suyemitsu T., Ishihara K.;
RT "Molecular cloning of a cDNA that encodes the precursor to several
RT exogastrula-inducing peptides, epidermal-growth-factor-related polypeptides
RT of the sea urchin Anthocidaris crassispina.";
RL Eur. J. Biochem. 228:515-523(1995).
RN [2]
RP PROTEIN SEQUENCE OF 106-158 AND 179-230.
RC TISSUE=Embryo;
RX PubMed=2713739; DOI=10.1016/0922-3371(89)90783-1;
RA Suyemitsu T., Asami-Yoshizumi T., Noguchi S., Tonegawa Y., Ishihara K.;
RT "The exogastrula-inducing peptides in embryos of the sea urchin,
RT Anthocidaris crassispina -- isolation and determination of the primary
RT structure.";
RL Cell Differ. Dev. 26:53-66(1989).
RN [3]
RP PROTEIN SEQUENCE OF 47-104.
RC TISSUE=Embryo;
RX PubMed=2804137; DOI=10.1016/0167-4838(89)90024-1;
RA Suyemitsu T., Tonegawa Y., Ishihara K.;
RT "Amino acid sequence of exogastrula-inducing peptide C from the sea urchin,
RT Anthocidaris crassispina.";
RL Biochim. Biophys. Acta 999:24-28(1989).
CC -!- FUNCTION: The EGIP peptides are factors effective to extrude the
CC archenteron toward outside of embryos. May have a role in the induction
CC of gastrulation.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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DR EMBL; Z48184; CAA88234.1; -; mRNA.
DR PIR; S68985; S68985.
DR AlphaFoldDB; P15217; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR InterPro; IPR000742; EGF-like_dom.
DR SMART; SM00181; EGF; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Developmental protein;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Gastrulation; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..45
FT /id="PRO_0000007548"
FT PEPTIDE 47..104
FT /note="Exogastrula-inducing peptide C"
FT /id="PRO_0000007549"
FT PEPTIDE 106..158
FT /note="Exogastrula-inducing peptide D"
FT /id="PRO_0000007550"
FT PROPEP 160..177
FT /id="PRO_0000007551"
FT PEPTIDE 179..230
FT /note="Exogastrula-inducing peptide A"
FT /id="PRO_0000007552"
FT PROPEP 232..249
FT /id="PRO_0000007553"
FT PEPTIDE 251..310
FT /note="EGIP-X"
FT /evidence="ECO:0000305"
FT /id="PRO_0000007554"
FT PROPEP 313..325
FT /id="PRO_0000007555"
FT DOMAIN 48..91
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 107..154
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 180..226
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 252..298
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 52..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 59..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 77..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 111..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 118..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 140..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 184..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 191..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 213..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 256..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 263..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 285..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 325 AA; 36462 MW; 1FD2577B3617306A CRC64;
MKVSLVLLIA VFGLAMVAAE ETLESKLQMA LKSLLQENEE LNLEGRDTKG GCERATNNCN
GHGDCVQGRW GQYYCKCTLP YRVGGSESSC YMPKDKEEDV EIETKDTVAR CERDTKNCDG
HGTCQLSTFG RRTGQYICFC DAGYRKPNSY GGCSPSSARE LEYLSYVARD VEMEMLARDS
VYQCNRDTNS CDGFGKCEKS TFGRTTGQYI CNCDDGYRNN AYGGCSPRTE REIEYLSMIA
RDQELEMQAR DSLPQCNRDT NYCDGFGQCV KSTFGRTTGQ YICSCNDGYE NNLYGGCSPK
DNEDEEVDTD RKMEILRSLA NLLEE
