ID GIGA2_CRAGI Reviewed; 340 AA. AC P86785; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 1. DT 16-OCT-2019, entry version 11. DE RecName: Full=Gigasin-2 {ECO:0000303|Ref.2}; DE Flags: Precursor; OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia; OC Ostreoida; Ostreoidea; Ostreidae; Crassostrea. OX NCBI_TaxID=29159; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=18054177; DOI=10.1016/j.gene.2007.10.021; RA Tanguy A., Bierne N., Saavedra C., Pina B., Bachere E., Kube M., RA Bazin E., Bonhomme F., Boudry P., Boulo V., Boutet I., Cancela L., RA Dossat C., Favrel P., Huvet A., Jarque S., Jollivet D., Klages S., RA Lapegue S., Leite R., Moal J., Moraga D., Reinhardt R., Samain J.F., RA Zouros E., Canario A.; RT "Increasing genomic information in bivalves through new EST RT collections in four species: development of new genetic markers for RT environmental studies and genome evolution."; RL Gene 408:27-36(2008). RN [2] {ECO:0000305} RP PROTEIN SEQUENCE OF 50-59; 137-143; 212-221 AND 287-297, AND TISSUE RP SPECIFICITY. RC TISSUE=Shell {ECO:0000269|Ref.2}; RA Marie B., Zanella-Cleon I., Becchi M., Marin F.; RT "Proteomic identification of novel proteins from the calcifying shell RT matrix of the Pacific oyster Crassostrea gigas."; RL FEBS Lett. 0:0-0(2010). CC -!- TISSUE SPECIFICITY: Component of the organic matrix of calcified CC shell layers. {ECO:0000269|Ref.2}. CC -!- SEQUENCE CAUTION: CC Sequence=AM868448; Type=Frameshift; Evidence={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; AM864770; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AM868448; -; NOT_ANNOTATED_CDS; mRNA. DR PRIDE; P86785; -. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR SMART; SM00181; EGF; 2. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 2. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; EGF-like domain; Repeat; KW Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 340 Gigasin-2. {ECO:0000255}. FT /FTId=PRO_0000403307. FT DOMAIN 22 57 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 65 97 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DISULFID 25 39 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 33 45 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 47 56 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 69 79 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 73 85 {ECO:0000255|PROSITE-ProRule:PRU00076}. FT DISULFID 87 96 {ECO:0000255|PROSITE-ProRule:PRU00076}. SQ SEQUENCE 340 AA; 37687 MW; DD9CEFB9FB186EF1 CRC64; MNKMSPLYVL ALCCLATTVF AKYDCTNNGG YGCKYGGTCH FYGFCICPKG FQGEDCGLKT ELISTAANCT AECKNGGTCY ESDRCYCPHG FIGDMCEIPD TVARCAPDRM IIEAYRPLGF VGEVYMFQNR KSCALKQVPS DIRDMMKLER VVLHSDKTEC ALTRTPDTPK LGDVTMKTTV VSTHNYNQFG PRDSIMDVSC VHTNSFQGST KEITETAFPF RMVALDMNGE PVQALAANES IILQFEPVGI PDVRGVMVEY LEVYSINANS NEVVSKTIIE NGCVLRTAQQ HLEIPIRNYS EMXRQGTSWV ARSAMRAFIL LPGDHCYSSL DYASVPEVPR //