VIT_ANTGR
ID VIT_ANTGR Reviewed; 1790 AA.
AC Q05808;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Vitellogenin;
DE Contains:
DE RecName: Full=YP47;
DE Contains:
DE RecName: Full=YP160;
DE Flags: Precursor;
GN Name=VTG;
OS Anthonomus grandis (Mexican cotton boll weevil) (Anthonomus thurberiae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Curculioninae; Anthonomini; Anthonomus.
OX NCBI_TaxID=7044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1593641; DOI=10.1007/bf00160462;
RA Trewitt P.M., Heilmann L.J., Degrugillier S.S., Kumaran A.K.;
RT "The boll weevil vitellogenin gene: nucleotide sequence, structure, and
RT evolutionary relationship to nematode and vertebrate vitellogenin genes.";
RL J. Mol. Evol. 34:478-492(1992).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; M72980; AAA27740.1; -; Genomic_DNA.
DR PIR; S27772; S27772.
DR AlphaFoldDB; Q05808; -.
DR SMR; Q05808; -.
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 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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Secreted; Signal; Storage protein.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1790
FT /note="Vitellogenin"
FT /id="PRO_0000041542"
FT CHAIN 20..?
FT /note="YP47"
FT /id="PRO_0000041543"
FT CHAIN ?..1790
FT /note="YP160"
FT /id="PRO_0000041544"
FT DOMAIN 23..799
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1466..1675
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 342..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1468..1638
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1790 AA; 205858 MW; E0B07A5B1E70D0DA CRC64;
MWSTVALCLL VGLSYVSSSS PAWKDNTEYV YSVNGRTLTG LEETADQYSG VFLEAKLHLS
IRPDGKLQGR ISEPKFAQIL SQLPDGWKSE IPDSQISYKQ LQLSQKPFQL VLENGLIKRL
IVEKDTLNWE ANIIKSIVSQ FQMDLQGENA LQNPTSSFPT NEYMDAVFKT MEETVTGKTE
TIYDIHRLPE YLVQSQPWIA PQYKLKGEGD LIEVIKSKNY TNARDRPSYH YGFGEIEESE
PTANKMGQFF IRQSNSRAIL TGKPSRYIIQ STYTVNKIMV NPILKNKEMG SITSMVNVTL
LEINNQQQQP EELSNPLDIG NLVYTYGQPK NNQVHSKLNE NLMEDSSSEE SSEQEMTHRR
FRRSANSLTK QWRESSEEWN QQQQQPRPQL TRAPHSPLLP SMVGYHGKSI KENKDFDIRQ
NVENLVTEIS DEIKQSEKTI SKHTLDKYTI LNTLVRLMDE DDIQFVAEQM YSQMKNGQQR
YTWSIFRDSV AEAGTGPALL NIKKWIETKK IQKTEAAQVI GTLAQSTRFP TEEYMRKFFE
LATETQVRQQ ETLNQTCILS YTNLVHKVYI NRNESHNQFP VHAFGSFYTK KGREFVKTTV
IPHLKQELEK AISNADNNKI HVMIRALGNI GHKSILNVFQ PYFEGEKQVS QFQRLMMVAC
MDRLADCYPH IARSVFYKIY QNTAELPEIR VVAVHQLIRA NPPVEMLQRM AQYTNTDSQE
EVNAAVKSVI ESSCKLESSK HAELRKAAQS ARPLLTKKQY GMEQSYINLR DYVAEQMGLE
LHVQRTSHSS AESSFPKIMK FQLHQHNHGM KQHILSTGGM ISSIRELLNV LYRQTEVFQQ
EKSQRSQEQG KDNEWSSANI ARLMNYERDE REQLEAIIYA QVEDVQKLWS FDNQTLEHLP
EVIRQQEEIY RQGKDFSYVK LKQLNEMALS FPTEMGLPFL YTYDVPVLMK VEGKIRALAN
PAISRNNKLT KPEQISTEIK ARVTCTGKTQ SHLSFVTPFD HQIYMAGYDK NMYVSIPVNA
RLEMDVKSKE AKIEFEVEQQ QQDSRLVHIT STPYTSRSDV MAISPVALRP NTYVIKSHRN
NHRYFDFNFG KKETGLTFRG WGHHPEQSIG FNDLVSMWQS RGVAGVWEQL WDKCSTEYSE
ATISFIPSQS TTRKATFRIN VDQKYQKQPE TQSPEDLLTL NQLSSKLQKD EPKQRQQEIK
KHVGSGINSA LLSCSDISLE FEGDKKYEHV VGFAVAKSNA DPKSRVMFYY KNKNENKQGA
LEIRSEIPNT NGLNLDDSLD TEPSTKYNMR LQYGNSENDA FEISAQAQLS RSQERKQYLI
NQDPLYHVCK EQMQQKNFQL PACQNMTIKA NFLDHIKYQV QYQKLNWKLV ETLEGMFKGL
RVLYYPMTEI KSISSVGQNV VEGEVQFQPE DFRQVNVTVR NTDEETVFFN ISLNNELLRT
LLVPHPVFHA KCRFAGLMQG QQNYRPTCVI DQTTAQTFSN KTYSVNLDKE PTVVMQYVPK
DARVNGQQSK SVEQLLRESI ENYVVLVRQV AANQKEVIIN LNHPRTQGKT VKIEMKPSED
RQKSARNPAA KVTIDGQEMH FDDKQIADKC DGYVQVYALP NGEVKLEVED AFYLIYDGQR
VKVTATGNKL RDSVYGLCGR FSQDKHEDFT VPSNCVTRDT RKFVESYQVE KGQQWRNSPS
EQCIKKVLPL YTNVISNQNG SQMRTKLASG TVMKHRYIEE NGEICFTIRP LPVCNTSVKQ
VVTKNVPVHC IQGTKTAYYY KSLIDQGGNP DFSRKSETRT ARMEVAAQCN
