ID A0A2G8KHC8_STIJA Unreviewed; 415 AA.
AC A0A2G8KHC8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Putative follistatin isoform X2 {ECO:0000313|EMBL:PIK47396.1};
GN ORFNames=BSL78_15730 {ECO:0000313|EMBL:PIK47396.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK47396.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK47396.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK47396.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK47396.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIK47396.1}.
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DR EMBL; MRZV01000582; PIK47396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8KHC8; -.
DR STRING; 307972.A0A2G8KHC8; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR CDD; cd00104; KAZAL_FS; 3.
DR Gene3D; 3.30.60.30; -; 3.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 1.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR13866:SF29; FOLLISTATIN; 1.
DR PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR Pfam; PF21333; FST_N; 1.
DR Pfam; PF07648; Kazal_2; 3.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 3.
DR PROSITE; PS51465; KAZAL_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..415
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013587148"
FT DOMAIN 111..167
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 190..240
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 257..314
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT REGION 355..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..408
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 46198 MW; B24A91AC4B9F7C3B CRC64;
MKIIMNSSPF IMIVMMWGTS SVLPLTEGGS CWANYDTLSG QCVALIHRRV SYEDCCRISG
FSFIERDMST EDIFRSLIMH GGVSDCLPCS SFGKDVCEGI TCNRDEVCVA RNGQPLCNCD
PDCSDVDLDQ PVCGSDRQTY TNECTFKMNR CQERRDVELA YYGQCQDSCD TVTCAHGTCL
VDQMGVPHCV NCSPECKDKE VQGSVCGTDK NTYESICHLR LTSCNIGKAI IKNHNGRCVG
STNCSSFLCM EGNICSMGTK PHCSTCPQAG CGRYALRALC GSDDVTYANL CAMKRAICDT
RVYVKRQHFG PCARDMSHIP PQDREAYFRY YLSFFHHEQV SEPATTALIR RLTTNTEESL
TRTGDNDDTT NDENNQGVEE ENQGEEEDVI GVETEEEPEE EEVAEEMVQE ESPNL
//