GenomeNet

Database: UniProt
Entry: P15217
LinkDB: P15217
Original site: P15217 
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   20-JUN-2018, entry version 73.
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;
OC   Echinoidea; Euechinoidea; Echinacea; Echinoida; 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
RT   polypeptides 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.,
RA   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
RT   urchin, 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
CC       induction of gastrulation.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
DR   EMBL; Z48184; CAA88234.1; -; mRNA.
DR   PIR; S68985; S68985.
DR   ProteinModelPortal; P15217; -.
DR   PRIDE; P15217; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR   InterPro; IPR013032; EGF-like_CS.
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       {ECO:0000255}.
FT   PROPEP       20     45
FT                                /FTId=PRO_0000007548.
FT   PEPTIDE      47    104       Exogastrula-inducing peptide C.
FT                                /FTId=PRO_0000007549.
FT   PEPTIDE     106    158       Exogastrula-inducing peptide D.
FT                                /FTId=PRO_0000007550.
FT   PROPEP      160    177
FT                                /FTId=PRO_0000007551.
FT   PEPTIDE     179    230       Exogastrula-inducing peptide A.
FT                                /FTId=PRO_0000007552.
FT   PROPEP      232    249
FT                                /FTId=PRO_0000007553.
FT   PEPTIDE     251    310       EGIP-X. {ECO:0000305}.
FT                                /FTId=PRO_0000007554.
FT   PROPEP      313    325
FT                                /FTId=PRO_0000007555.
FT   DOMAIN       48     91       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      107    154       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      180    226       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      252    298       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID     52     65       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     59     75       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     77     90       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    111    124       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    118    138       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    140    153       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    184    197       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    191    211       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    213    225       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    256    269       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    263    283       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    285    297       {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
//
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