ID   VIT_APIME               Reviewed;        1770 AA.
AC   Q868N5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Vitellogenin;
DE   Flags: Precursor;
GN   Name=Vg;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Fat body;
RX   PubMed=12650694; DOI=10.1016/s0965-1748(03)00021-3;
RA   Piulachs M.D., Guidugli K.R., Barchuk A.R., Cruz J., Simoes Z.L.P.,
RA   Belles X.;
RT   "The vitellogenin of the honey bee, Apis mellifera: structural analysis of
RT   the cDNA and expression studies.";
RL   Insect Biochem. Mol. Biol. 33:459-465(2003).
RN   [2]
RP   FUNCTION, AND INDUCTION BY MRJP1.
RX   PubMed=21516106; DOI=10.1038/nature10093;
RA   Kamakura M.;
RT   "Royalactin induces queen differentiation in honeybees.";
RL   Nature 473:478-483(2011).
CC   -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC       nutrients during embryonic development (By similarity). Involved in the
CC       differentiation of honeybee larvae into queens. {ECO:0000250,
CC       ECO:0000269|PubMed:21516106}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Accumulates in the hemolymph. Represents up to 70%
CC       of the queen's hemolymph proteins. During the first week of the worker
CC       adult life, when it becomes a nurse bee and performs brood-rearing
CC       tasks, the vitellogenin titer increases and may account for up to 40%
CC       of the total hemolymph proteins. {ECO:0000269|PubMed:12650694}.
CC   -!- DEVELOPMENTAL STAGE: In queens, first expressed in mid-late pupal stage
CC       and a high production is maintained throughout adult life. In workers,
CC       observed in late pupal stage and expressed at low levels in adults.
CC       Levels can increase in some young workers if an egg-laying queen is
CC       missing to the colony. Also detected in drones, but in freshly molted
CC       adults and not in pupae. {ECO:0000269|PubMed:12650694}.
CC   -!- INDUCTION: By MRJP1 during the differentiation of honeybee larvae into
CC       queens. {ECO:0000269|PubMed:21516106}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ517411; CAD56944.1; -; mRNA.
DR   RefSeq; NP_001011578.1; NM_001011578.1.
DR   PDB; 2LIC; NMR; -; A=358-392.
DR   PDBsum; 2LIC; -.
DR   AlphaFoldDB; Q868N5; -.
DR   SMR; Q868N5; -.
DR   STRING; 7460.GB49544-PA; -.
DR   Allergome; 10030; Api m 12.
DR   Allergome; 10031; Api m 12.0101.
DR   PaxDb; Q868N5; -.
DR   EnsemblMetazoa; NM_001011578; NP_001011578; GeneID_406088.
DR   GeneID; 406088; -.
DR   KEGG; ame:406088; -.
DR   CTD; 36421; -.
DR   eggNOG; KOG4338; Eukaryota.
DR   InParanoid; Q868N5; -.
DR   OrthoDB; 36651at2759; -.
DR   PhylomeDB; Q868N5; -.
DR   Proteomes; UP000005203; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   DisProt; DP01582; -.
DR   Gene3D; 1.25.10.20; -; 1.
DR   Gene3D; 2.30.230.10; -; 1.
DR   InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR   InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR   InterPro; IPR015816; Vitellinogen_b-sht_N.
DR   InterPro; IPR015255; Vitellinogen_open_b-sht.
DR   InterPro; IPR001747; Vitellogenin_N.
DR   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF09172; DUF1943; 1.
DR   Pfam; PF01347; Vitellogenin_N; 1.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM01169; DUF1943; 1.
DR   SMART; SM00638; LPD_N; 1.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF48431; SSF48431; 1.
DR   SUPFAM; SSF56968; SSF56968; 2.
DR   PROSITE; PS51211; VITELLOGENIN; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal; Storage protein.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..1770
FT                   /note="Vitellogenin"
FT                   /id="PRO_5000070065"
FT   DOMAIN          22..809
FT                   /note="Vitellogenin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT   DOMAIN          1442..1635
FT                   /note="VWFD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   REGION          373..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1067
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        178..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT                   ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1444..1598
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1466..1634
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:2LIC"
FT   STRAND          368..371
FT                   /evidence="ECO:0007829|PDB:2LIC"
SQ   SEQUENCE   1770 AA;  201048 MW;  FF42F06CC053ABBF CRC64;
     MLLLLTLLLF AGTVAADFQH NWQVGNEYTY LVRSRTLTSL GDLSDVHTGI LIKALLTVQA
     KDSNVLAAKV WNGQYARVQQ SMPDGWETEI SDQMLELRDL PISGKPFQIR MKHGLIRDLI
     VDRDVPTWEV NILKSIVGQL QVDTQGENAV KVNSVQVPTD DEPYASFKAM EDSVGGKCEV
     LYDIAPLSDF VIHRSPELVP MPTLKGDGRH MEVIKIKNFD NCDQRINYHF GMTDNSRLEP
     GTNKNGKFFS RSSTSRIVIS ESLKHFTIQS SVTTSKMMVS PRLYDRQNGL VLSRMNLTLA
     KMEKTSKPLP MVDNPESTGN LVYIYNNPFS DVEERRVSKT AMNSNQIVSD NSLSSSEEKL
     KQDILNLRTD ISSSSSSISS SEENDFWQPK PTLEDAPQNS LLPNFVGYKG KHIGKSGKVD
     VINAAKELIF QIANELEDAS NIPVHATLEK FMILCNLMRT MNRKQISELE SNMQISPNEL
     KPNDKSQVIK QNTWTVFRDA ITQTGTGPAF LTIKEWIERG TTKSMEAANI MSKLPKTVRT
     PTDSYIRSFF ELLQNPKVSN EQFLNTAATL SFCEMIHNAQ VNKRSIHNNY PVHTFGRLTS
     KHDNSLYDEY IPFLERELRK AHQEKDSPRI QTYIMALGMI GEPKILSVFE PYLEGKQQMT
     VFQRTLMVGS LGKLTETNPK LARSVLYKIY LNTMESHEVR CTAVFLLMKT NPPLSMLQRM
     AEFTKLDTNR QVNSAVKSTI QSLMKLKSPE WKDLAKKARS VNHLLTHHEY DYELSRGYID
     EKILENQNII THMILNYVGS EDSVIPRILY LTWYSSNGDI KVPSTKVLAM ISSVKSFMEL
     SLRSVKDRET IISAAEKIAE ELKIVPEELV PLEGNLMINN KYALKFFPFD KHILDKLPTL
     ISNYIEAVKE GKFMNVNMLD TYESVHSFPT ETGLPFVYTF NVIKLTKTSG TVQAQINPDF
     AFIVNSNLRL TFSKNVQGRV GFVTPFEHRH FISGIDSNLH VYAPLKISLD VNTPKGNMQW
     KIWPMKGEEK SRLFHYSVVP FVSNHDILNL RPLSMEKGTR PMIPDDNTSL ALPKNEGPFR
     LNVETAKTNE EMWELIDTEK LTDRLPYPWT MDNERYVKVD MYMNLEGEQK DPVIFSTSFD
     SKVMTRPDTD SENWTPKMMA VEPTDKQANS KTRRQEMMRE AGRGIESAKS YVVDVRVHVP
     GESESETVLT LAWSESNVES KGRLLGFWRV EMPRSNADYE VCIGSQIMVS PETLLSYDEK
     MDQKPKMDFN VDIRYGKNCG KGERIDMNGK LRQSPRLKEL VGATSIIKDC VEDMKRGNKI
     LRTCQKAVVL SMLLDEVDIS MEVPSDALIA LYSQGLFSLS EIDNLDVSLD VSNPKNAGKK
     KIDVRAKLNE YLDKADVIVN TPIMDAHFKD VKLSDFGFST EDILDTADED LLINNVFYED
     ETSCMLDKTR AQTFDGKDYP LRLGPCWHAV MTTYPRINPD NHNEKLHIPK DKSVSVLSRE
     NEAGQKEVKV LLGSDKIKFV PGTTSQPEVF VNGEKIVVSR NKAYQKVEEN EIIFEIYKMG
     DRFIGLTSDK FDVSLALDGE RVMLKASEDY RYSVRGLCGN FDHDSTNDFV GPKNCLFRKP
     EHFVASYALI SNQCEGDSLN VAKSLQDHDC IRQERTQQRN VISDSESGRL DTEMSTWGYH
     HNVNKHCTIH RTQVKETDDK ICFTMRPVVS CASGCTAVET KSKPYKFHCM EKNEAAMKLK
     KRIEKGANPD LSQKPVSTTE ELTVPFVCKA