ID   VIT_ANAPL               Reviewed;          46 AA.
AC   P56530;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   02-JUN-2021, entry version 40.
DE   RecName: Full=Phosvitin;
DE            Short=PV;
DE   Flags: Fragment;
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4065410; DOI=10.1016/0020-711x(85)90243-5;
RA   Clark R.C.;
RT   "The primary structure of avian phosvitins. Contributions through the Edman
RT   degradation of methylmercaptovitins prepared from the constituent
RT   phosphoproteins.";
RL   Int. J. Biochem. 17:983-988(1985).
CC   -!- FUNCTION: Phosvitin is believed to be of importance in sequestering
CC       calcium, iron and other cations for the developing embryo.
CC   -!- PTM: Phosvitin, an egg yolk storage protein, is one of the most highly
CC       phosphorylated (10%) proteins in nature.
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DR   PIR; B29184; B29184.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Phosphoprotein; Storage protein.
FT   CHAIN           <1..>46
FT                   /note="Phosvitin"
FT                   /id="PRO_0000134399"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         46
SQ   SEQUENCE   46 AA;  4640 MW;  4990F41700CCB033 CRC64;
     TELGTDPNAK TPSSSSSASS ALSSSSSSSA SSPBHRKPMD EDDNQV