SSP1_BOMMO
ID SSP1_BOMMO Reviewed; 747 AA.
AC P09179;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Sex-specific storage-protein 1;
DE Short=SP 1;
DE AltName: Full=Methionine-rich storage protein;
DE Flags: Precursor;
GN Name=SP1;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tokai X Asahi; TISSUE=Fat body;
RX PubMed=3412900; DOI=10.1093/nar/16.15.7717;
RA Sakurai H., Fujii T., Izumi S., Tomino S.;
RT "Complete nucleotide sequence of gene for sex-specific storage protein of
RT Bombyx mori.";
RL Nucleic Acids Res. 16:7717-7718(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
RX PubMed=2836399; DOI=10.1016/s0021-9258(18)68579-5;
RA Sakurai H., Fujii T., Izumi S., Tomino S.;
RT "Structure and expression of gene coding for sex-specific storage protein
RT of Bombyx mori.";
RL J. Biol. Chem. 263:7876-7880(1988).
CC -!- FUNCTION: Larval storage protein (LSP) which may serve as a store of
CC amino acids for synthesis of adult proteins.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Fat body.
CC -!- SIMILARITY: Belongs to the hemocyanin family. {ECO:0000305}.
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DR EMBL; X12978; CAA31417.1; -; Genomic_DNA.
DR PIR; S01918; S01918.
DR AlphaFoldDB; P09179; -.
DR SMR; P09179; -.
DR STRING; 7091.BGIBMGA011266-TA; -.
DR eggNOG; ENOG502QR98; Eukaryota.
DR HOGENOM; CLU_012213_1_0_1; -.
DR InParanoid; P09179; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 1.
DR Gene3D; 1.20.1370.10; -; 1.
DR Gene3D; 2.60.40.1520; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
DR InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR InterPro; IPR005203; Hemocyanin_C.
DR InterPro; IPR037020; Hemocyanin_C_sf.
DR InterPro; IPR005204; Hemocyanin_N.
DR InterPro; IPR036697; Hemocyanin_N_sf.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11511; PTHR11511; 1.
DR Pfam; PF03723; Hemocyanin_C; 1.
DR Pfam; PF00372; Hemocyanin_M; 1.
DR Pfam; PF03722; Hemocyanin_N; 1.
DR PRINTS; PR00187; HAEMOCYANIN.
DR SUPFAM; SSF48050; SSF48050; 1.
DR SUPFAM; SSF48056; SSF48056; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00209; HEMOCYANIN_1; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal; Storage protein.
FT SIGNAL 1..15
FT CHAIN 16..747
FT /note="Sex-specific storage-protein 1"
FT /id="PRO_0000013340"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 87242 MW; 08DD368BDAC99F92 CRC64;
MRVLVLLACL AAASASAISG GYGTMVFTKE PMVNLDMKMK ELCIMKLLDH ILQPTMFEDI
KEIAKEYNIE KSCDKYMNVD VVKQFMEMYK MGMLPRGETF VHTNELQMEE AVKVFRVLYY
AKDFDVFMRT ACWMRERING GMFVYAFTAA CFHRTDCKGL YLPAPYEIYP YFFVDSHVIS
KAFMMKMTKA AKDPVLWKYY GITVTDDNLV VIDWRKGVRR SLSQNDVMSY FMEDVDLNTY
MYYLHMNYPF WMTDDAYGIN KERRGEIMMY ANQQLLARMR LERLSHKMCD VKPMMWNEPL
ETGYWPKIRL PSGDEMPVRQ NNMVVATKDN LKMKQMMDDV EMMIREGILT GKIERRDGTV
ISLKKSEDIE NLARLVLGGL EIVGDDAKVI HLTNLMKKML SYGQYNMDKY TYVPTSLDMY
TTCLRDPVFW MIMKRVCNIF TVFKNMLPKY TREQFSFPGV KVEKITTDEL VTFVDEYDMD
ISNAMYLDAT EMQNKTSDMT FMARMRRLNH HPFQVSIDVM SDKTVDAVVR IFLGPKYDCM
GRLMSVNDKR LDMFELDSFM YKLVNGKNTI VRSSMDMQGF IPEYLSTRRV MESEMMPSGD
GQTMVKDWWC KSRNGFPQRL MLPLGTIGGL EMQMYVIVSP VRTGMLLPTL DMTMMKDRCA
CRWSSCISTM PLGYPFDRPI DMASFFTSNM KFADVMIYRK DLGMSNTSKT VDTSEMVMMK
DDLTYLDSDM LVKRTYKDVM MMSSMMN