ID   SSP2_BOMMO              Reviewed;         704 AA.
AC   P20613; Q9TYA2;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Sex-specific storage-protein 2;
DE            Short=SP 2;
DE   AltName: Full=Arylphorin;
DE   Flags: Precursor;
GN   Name=SP2;
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].
RX   PubMed=2544581; DOI=10.1016/s0021-9258(18)60421-1;
RA   Fujii T., Sakurai H., Izumi S., Tomino S.;
RT   "Structure of the gene for the arylphorin-type storage protein SP 2 of
RT   Bombyx mori.";
RL   J. Biol. Chem. 264:11020-11025(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-359.
RC   STRAIN=R53; TISSUE=Posterior silk gland;
RX   PubMed=8845960; DOI=10.1006/mpev.1995.1021;
RA   Shimada T., Kurimoto Y., Kobayashi M.;
RT   "Phylogenetic relationship of silkmoths inferred from sequence data of the
RT   arylphorin gene.";
RL   Mol. Phylogenet. Evol. 4:223-234(1995).
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; M24370; AAA27848.1; -; Genomic_DNA.
DR   EMBL; M24371; AAA27848.1; JOINED; Genomic_DNA.
DR   EMBL; AB019209; BAA34090.1; -; Genomic_DNA.
DR   PIR; A34287; A34287.
DR   AlphaFoldDB; P20613; -.
DR   SMR; P20613; -.
DR   STRING; 7091.BGIBMGA009028-TA; -.
DR   GlyConnect; 563; 3 N-Linked glycans.
DR   PRIDE; P20613; -.
DR   eggNOG; ENOG502QR98; Eukaryota.
DR   HOGENOM; CLU_012213_1_0_1; -.
DR   InParanoid; P20613; -.
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..16
FT   CHAIN           17..704
FT                   /note="Sex-specific storage-protein 2"
FT                   /id="PRO_0000013341"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        681
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   704 AA;  83467 MW;  365E7DFB707137EB CRC64;
     MKSVLILAGL VAVALSSAVP KPSTIKSKNV DAVFVEKQKK ILSFFQDVSQ LNTDDEYYKI
     GKDYDIEMNM DNYTNKKAVE EFLKMYRTGF MPKNLEFSVF YDKMRDEAIA LLDLFYYAKD
     FETFYKSACF ARVHLNQGQF LYAFYIAVIQ RPDCHGFVVP APYEVYPKMF MNMEVLQKIY
     VTKMQHGLIN PEAAAKYGIH KENDYFVYKA NYSNAVLYNN EEQRLTYFTE DIGMNAYYYY
     FHSHLPFWWT SEKYGALKER RGEVYFYFYQ QLLARYYFER LTNGLGKIPE FSWYSPIKTG
     YYPLMLTKFT PFAQRPDYYN LHTEENYERV RFLDTYEKTF VQFLQKDHFE AFGQKIDFHD
     PKAINFVGNY WQDNADLYGE EVTKDYQRSY EVFARRVLGA APMPFDKYTF MPSAMDFYQT
     SLRDPAFYQL YNRIVEYIVE FKQYLKPYTQ DKLYFDGVKI TDVKVDKLTT FFENFEFDAS
     NSVYFSKEEI KNNHVHELRC ATRLNHSPFN VNIEVDSNVA SDAVVKMLLA PKYDDNGIPL
     TLEDNWMKFF ELDWFTTKLT AGQNKIIRNS NEFVIFKEDS VPMTEIMKML DEGKVPFDMS
     EEFCYMPKRL MLPRGTEGGF PFQLFVFVYP FDNKGKDLAP FESFVLDNNL LASLWIAPLL
     MHYSRFLTCI SRIFSFTTRV NGSLTNSIFL RMTHMIMLFQ KIKF