ID   VIT3_CHICK              Reviewed;         347 AA.
AC   Q91025; Q91028;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Vitellogenin-3;
DE   AltName: Full=Minor vitellogenin;
DE   AltName: Full=VYGIII;
DE   AltName: Full=Vitellogenin III;
DE   Contains:
DE     RecName: Full=Phosvitin;
DE              Short=PV;
DE   Flags: Precursor; Fragments;
GN   Name=VTG3; Synonyms=VTGIII;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RX   PubMed=2796998; DOI=10.1128/mcb.9.8.3557-3562.1989;
RA   Silva R., Fischer A.H., Burch J.B.E.;
RT   "The major and minor chicken vitellogenin genes are each adjacent to
RT   partially deleted pseudogene copies of the other.";
RL   Mol. Cell. Biol. 9:3557-3562(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-347.
RC   TISSUE=Liver;
RX   PubMed=2701940; DOI=10.1021/bi00432a034;
RA   Byrne B.M., de Jong H., Fouchier R.A.M., Williams D.L., Gruber M., Ab G.;
RT   "Rudimentary phosvitin domain in a minor chicken vitellogenin gene.";
RL   Biochemistry 28:2572-2577(1989).
CC   -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC       nutrients during early development of oviparous organisms.
CC   -!- FUNCTION: Phosvitin is believed to be of importance in sequestering
CC       calcium, iron and other cations for the developing embryo.
CC   -!- TISSUE SPECIFICITY: Produced by the liver, secreted into the blood and
CC       then sequestered by receptor mediated endocytosis into growing oocytes,
CC       where it is generally cleaved, giving rise to the respective yolk
CC       components.
CC   -!- INDUCTION: By steroids (estrogen).
CC   -!- PTM: Phosvitin, an egg yolk storage protein, is one of the most highly
CC       phosphorylated (10%) proteins in nature.
CC   -!- PTM: Cathepsin D is responsible for intraoocytic processing of
CC       vitellogenin.
CC   -!- PTM: May contain intrachain disulfide bonds.
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DR   EMBL; L36662; AAA21878.1; -; Genomic_DNA.
DR   EMBL; M28125; AAA21878.1; JOINED; Genomic_DNA.
DR   EMBL; L36661; AAA21878.1; JOINED; Genomic_DNA.
DR   EMBL; M25483; AAA49143.1; -; Genomic_DNA.
DR   PIR; A31864; A31864.
DR   PIR; I50439; I50439.
DR   AlphaFoldDB; Q91025; -.
DR   SMR; Q91025; -.
DR   STRING; 9031.ENSGALP00000002886; -.
DR   PaxDb; Q91025; -.
DR   VEuPathDB; HostDB:geneid_424534; -.
DR   eggNOG; KOG4338; Eukaryota.
DR   InParanoid; Q91025; -.
DR   OrthoDB; 36651at2759; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; IBA:GO_Central.
DR   GO; GO:0032355; P:response to estradiol; IBA:GO_Central.
DR   Gene3D; 2.20.90.10; -; 1.
DR   Gene3D; 2.30.230.10; -; 1.
DR   InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR   InterPro; IPR015816; Vitellinogen_b-sht_N.
DR   InterPro; IPR015258; Vitellinogen_b-sht_shell.
DR   InterPro; IPR037088; Vitellinogen_b-sht_shell_sf.
DR   InterPro; IPR001747; Vitellogenin_N.
DR   Pfam; PF09175; DUF1944; 1.
DR   Pfam; PF01347; Vitellogenin_N; 1.
DR   SMART; SM01170; DUF1944; 1.
DR   SUPFAM; SSF56968; SSF56968; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Phosphoprotein; Reference proteome; Signal;
KW   Storage protein.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..>347
FT                   /note="Vitellogenin-3"
FT                   /id="PRO_0000041562"
FT   CHAIN           98..191
FT                   /note="Phosvitin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000041563"
FT   REGION          104..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_CONS        71..72
FT                   /evidence="ECO:0000305"
FT   NON_TER         347
SQ   SEQUENCE   347 AA;  38151 MW;  6A5A32FE8ED9F138 CRC64;
     MRGFILALVL ALVGAQKHDL EPVFSTGKTY LYDYKGLILH GLPGKGLAAA GLKLTCRLEI
     SRVSRSDHLL QIENVFKVAN KTRHHKKWIH SRVKAAVTDL WEEPSATPLS SSSSTDSSAE
     GEEPGNKRDK DEIWQFGKKY GADSSSSSSS SSTGSGSSKT CSSSREDSSR DKHCSVDSEY
     FNQQADLPIY QFWFKPADEQ DPRRKVQNSS ISSSSSSSSD EGISTPVSQP MFLGDSKPPV
     LAAVLRAIRR NEQPTGYQLV LYTDRQASRL RVQVFVSSIT ESDRWKLCAD ASVVNSHKAS
     GTLKWGKDCQ DYQVATQIAT GQFAAHPAIQ VKLEWSEVPS SVRKTAR