VIT1_AEDAE
ID VIT1_AEDAE Reviewed; 2169 AA.
AC Q16927; Q16892; Q16T05;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Vitellogenin-A1;
DE Short=VG;
DE AltName: Full=PVG1;
DE Contains:
DE RecName: Full=Vitellin light chain;
DE Short=VL;
DE Contains:
DE RecName: Full=Vitellin heavy chain;
DE Short=VH;
DE Flags: Precursor;
GN Name=VGA1; ORFNames=AAEL010434;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 47-61 AND
RP 490-504.
RC STRAIN=Rockefeller;
RX PubMed=7550249; DOI=10.1016/0965-1748(95)00037-v;
RA Romans P., Tu Z.J., Ke Z., Hagedorn H.H.;
RT "Analysis of a vitellogenin gene of the mosquito, Aedes aegypti and
RT comparisons to vitellogenins from other organisms.";
RL Insect Biochem. Mol. Biol. 25:939-958(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-2169, AND PROTEIN SEQUENCE OF 47-54 AND
RP 490-498.
RC STRAIN=UGALS; TISSUE=Fat body;
RX PubMed=8158643; DOI=10.1006/jmbi.1994.1261;
RA Chen J.-S., Cho W.-L., Raikhel A.S.;
RT "Analysis of mosquito vitellogenin cDNA. Similarity with vertebrate
RT phosvitins and arthropod serum proteins.";
RL J. Mol. Biol. 237:641-647(1994).
RN [4]
RP SULFATION.
RC TISSUE=Fat body;
RX PubMed=2351682; DOI=10.1016/s0021-9258(19)38760-5;
RA Dhadialla T.S., Raikhel A.S.;
RT "Biosynthesis of mosquito vitellogenin.";
RL J. Biol. Chem. 265:9924-9933(1990).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development. May supply aromatic amino acids
CC to the cuticle of rapidly developing embryos.
CC -!- TISSUE SPECIFICITY: Produced by the fat body, where it is cleaved in
CC the rough endoplasmic reticulum or cis-Golgi before being secreted into
CC hemolymph. It is then sequestered by a single class of receptor
CC mediated endocytosis in the ovary.
CC -!- INDUCTION: Synthesized only by sexually mature female after ingestion
CC of blood.
CC -!- PTM: Glycosylated, phosphorylated and sulfated. The large subunit is
CC sulfated more extensively than the small one.
CC {ECO:0000269|PubMed:2351682}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA18221.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA99486.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L41842; AAA99486.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH477662; EAT37585.1; -; Genomic_DNA.
DR EMBL; U02548; AAA18221.1; ALT_INIT; mRNA.
DR PIR; S46404; S46404.
DR RefSeq; XP_001660818.1; XM_001660768.1.
DR AlphaFoldDB; Q16927; -.
DR STRING; 7159.AAEL010434-PA; -.
DR GeneID; 5573342; -.
DR KEGG; aag:5573342; -.
DR VEuPathDB; VectorBase:AAEL010434; -.
DR eggNOG; KOG4338; Eukaryota.
DR HOGENOM; CLU_002645_0_0_1; -.
DR InParanoid; Q16927; -.
DR OMA; WIASKTY; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; Q16927; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
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; 2.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 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 Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Phosphoprotein; Reference proteome; Signal;
KW Storage protein; Sulfation.
FT SIGNAL 1..46
FT /evidence="ECO:0000269|PubMed:7550249,
FT ECO:0000269|PubMed:8158643"
FT CHAIN 47..2169
FT /note="Vitellogenin-A1"
FT /id="PRO_0000041539"
FT CHAIN 47..485
FT /note="Vitellin light chain"
FT /id="PRO_0000041540"
FT CHAIN 490..2169
FT /note="Vitellin heavy chain"
FT /id="PRO_0000041541"
FT DOMAIN 116..1008
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1770..1979
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 426..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2026..2081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2026..2064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2065..2081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 163
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1067
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1070
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1074
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1563
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1564
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1570
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1737
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1806
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1809
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1822
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1824
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1888
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1772..1942
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1794..1978
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CONFLICT 52
FT /note="S -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="G -> GYDAGYKGYG (in Ref. 1; AAA99486)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="Y -> H (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="G -> D (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="D -> N (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="S -> A (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="S -> R (in Ref. 1; AAA99486)"
FT /evidence="ECO:0000305"
FT CONFLICT 955
FT /note="I -> L (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 1375
FT /note="V -> I (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 1415
FT /note="Y -> F (in Ref. 1; AAA99486)"
FT /evidence="ECO:0000305"
FT CONFLICT 1597
FT /note="Y -> C (in Ref. 1; AAA99486)"
FT /evidence="ECO:0000305"
FT CONFLICT 1743
FT /note="A -> S (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 1762
FT /note="V -> I (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 1778
FT /note="Y -> N (in Ref. 1; AAA99486)"
FT /evidence="ECO:0000305"
FT CONFLICT 1866
FT /note="I -> V (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 1956
FT /note="P -> A (in Ref. 1; AAA99486)"
FT /evidence="ECO:0000305"
FT CONFLICT 2048
FT /note="S -> F (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 2051
FT /note="R -> L (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 2052
FT /note="S -> G (in Ref. 1; AAA99486)"
FT /evidence="ECO:0000305"
FT CONFLICT 2096
FT /note="T -> I (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 2111
FT /note="V -> A (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 2138
FT /note="D -> E (in Ref. 1; AAA99486 and 3; AAA18221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2169 AA; 252892 MW; C5D7983DCD1CD403 CRC64;
MATDGITSRF GFNERRRTHN RNSCRILEDK MLAKLLLLAL AGLTAAYQYE NSFKGYNPGY
KGYDAGYKGY GYDAGYKYNN QGYSYKNGFE YGYQNAYQAA FYKHRPNVTE FEFSSWMPNY
EYVYNVTSKT MTALAELDDQ WTGVFTRAYL VIRPKSRDYV VAYVKQPEYA VFNERLPYGY
ATKFYHDMFK FQPMPMSSKP FGIRYHKGAI KGLYVEKTIP NNEVNILKAW ISQLQVDTRG
ANLMHSSKPI HPSKNEWNGH YKVMEPLVTG ECETHYDVNL IPAYMIQAHK QWVPQGQLRG
EDGQFIQVTK TQNFDRCDQR MGYHFGFTGY SDFRPNTNQM GNVASKSLVS YMYLTGNWYN
FTIQSSSMIN KVAIAPSLVN KEPALVYAQV NMTLNDVHPY DKVPMGPAED LKVFVDLVYS
YNMPSDKKNY VRPGNETSSS SSSSSSSSSS SSESSSSSSE SVENPKISPV EQYKPLLDKV
EKRGNRYRRD LNAIKEKKYY EAYKMDQYRL HRLNDTSSDS SSSDSSSSSS SESKEHRNGT
SSYSSSSSSS SSSSSSESSS YSSSSSSSSE SYSISSEEYY YQPTPANFSY APEAPFLPFF
TGYKGYNIFY ARNVDAIRSV GKLVEEIASD LENPSDLPKS NTMSKFNILT RAIRAMGYED
IYELAQKYFV SQKERQVAQF SDKKFSKRVD AWVTLRDAVA EAGTPSAFKL IFDFIKEKKL
RGYEAATVIA SLAQSIRYPT EHLLHEFFLL VTSDVVLHQE YLNATALFAY SNFVNQAHVS
NRSAYNYYPV FSFGRLADAD YKIIEHKIVP WFAHQLREAV NEGDSVKIQV YIRSLGNLGH
PQILSVFEPY LEGTIQITDF QRLAIMVALD NLVIYYPSLA RSVLYRAYQN TADVHEVRCA
AVHLLMRTDP PADMLQRMAE FTHHDPSLYV RAAVKSAIET AALADDYDED SKLAINAKAA
INFLNPEDVS IQYSFNHIRD YALENLELSY RLHYGEIASN DHRYPSGLFY HLRQNFGGFK
KYTSFYYLVS SMEAFFDIFK KQYNTKYFAD YYKSADYSTN YYNFDKYSKY YKQYYYSKDS
EYYQKFYGQK KDYYNDKEPF KFTAPRIAKL LNIDAEEAEQ LEGQLLFKLF NGYFFTAFDN
QTIENLPHKM RHLFENLEDG YAFDVTKFYQ QQDVVLAWPL ATGFPFIYTL KAPTVFKFEV
DASAKTHPQV YKMPAGHPET ENDDFFYMPQ SINGSVDVNL LYHRMVDAKV GFVTPFDHQR
YIAGYQKKLH GYLPFNVELG LDFVKDEYEF EFKFLEPKDD HLLFHMSSWP YTGYKDITDM
RPIAENPNAK IVHDDNQSTK TMEHTFGQDM TGVALRFHAK YDFDLINFQQ FWSLVQKNDF
VSAVNYPFAY QPYEYHQFNL FYDSQRTHAK SFKFYAYQKF GAPSFEETGP KHPANRHSYS
GNYYESNYAQ PFVYSPGSQR RYEQFFRNAA SGIRNSFVRY YDFGFEFYAP QYKSEFTFTT
AFADSPVDKT SRQLYYFYAS PMFPSQSYFK DIPFSGKQFQ FCATATSEFP RVPYLKFSDF
DKYYGDASQY FDFLYGESCQ GGAHIAVKGK QKQTGKYREY LRFSDVAKAC KEQMANGYYQ
FEECQQAIDQ AYYYDFYDYA IEYKDVGSVA KNLTNKFYNY FQYAFYPYFE SNFFYHGKSN
YIKAEFEFAP YGDYYNASFF GPSYAFQVQN YPVFNDYSTY FPYFFKYTFF PRYQPYYMHR
LPAHKPRNRP YYELSNYEQF AVFDRKPQYP SCSFSNDYFY TFDNKKYFYD MGECWHAVMY
TVKPDYDFYA QQSHFYNSDF EYKYKNGFEE YEQFAALARR GSDNQLYFKF LFGDNYIEVF
PNNGGIPFVK YNGRPYDISK SNIAHFEYKE GYPSFPFFYA FAYPNKDLEV SFFGGKLKFA
TDGYRARFFS DYSFYNNFVG LCGTNNGEYF DEFVTPDQCY MRKPEFFAAS YAITGQNCTG
PAKAFNYAYQ QKAKQECVKR EVYYGDIIYN QEYYHPRYRY YNHNVEESSS SSSSSSSDSS
SSSSSSESSS RSRSGSSSSS SSSEEQKEFH PHKQEHSMKE CPVQHQHQFF EQGDRTCFSL
RPLPVCHSKC VATEKISKYF DVHCFEKDST QAKKYKSDIG RGYTPDFKSF APHKTYKFNY
PKSCVYKAY
