ID   VIT2_CERCA              Reviewed;         422 AA.
AC   P27587;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Vitellogenin-2;
DE   AltName: Full=Vitellogenin II;
DE   AltName: Full=Yolk protein 2;
DE   Flags: Precursor;
GN   Name=VG2-delta;
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Benakeion;
RX   PubMed=1903120; DOI=10.1093/genetics/127.4.769;
RA   Rina M., Savakis C.;
RT   "A cluster of vitellogenin genes in the Mediterranean fruit fly Ceratitis
RT   capitata: sequence and structural conservation in dipteran yolk proteins
RT   and their genes.";
RL   Genetics 127:769-780(1991).
CC   -!- FUNCTION: Vitellogenin is the major yolk protein of eggs where it is
CC       used as a food source during embryogenesis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized in the fat body and ovarian follicle
CC       cells and accumulate in the oocyte.
CC   -!- INDUCTION: By beta-ecdysone; in males.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; X54662; CAA38473.1; -; Genomic_DNA.
DR   PIR; S22888; S22888.
DR   ESTHER; cerca-2vite; Yolk-Protein_dipter.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; PTHR11610; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..422
FT                   /note="Vitellogenin-2"
FT                   /id="PRO_0000017818"
FT   REGION          158..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  45546 MW;  C46F876B538894F3 CRC64;
     MNPLTIFCLV AVLLSAATAH RGSNAIRNNL QPSGXLSPRE LEDMPAINEI TFEKLQEMPA
     EEAADLVNKI YHLSQMSRNI EPSYAPSPNQ IPAYTYTPTG QRVNFNLNQL VATAQQQPNF
     GKQEVTVFIT GLPNKSSAML TANQKLVQAY LQAYNGRVQV QGEQGDDSNQ DTSSSEESSN
     RPNGQQPKPN GNLVVIDLGA VIRNFEDLVL LDINRVGAAI GNSLVQLTAQ ADVPQEVINI
     VAQGIAAHVA GAAARQYTRQ TGNTLRRITA MDPSKIYARK PNTLVGLARG NADFVDAIHT
     SAYGLGTTTR AGDVDFYPNG PSVNMPGTDD IIEASLRATR YLAETVLPGN DRNFPAVAAE
     SLQQYKNNNG NGRRAYMGIA ADYDLEGDYI LQVNAKSPFG KSAPAQKQNS YHGIHQGAGR
     PN