VIT_BOMMO
ID VIT_BOMMO Reviewed; 1782 AA.
AC Q27309;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Vitellogenin;
DE Contains:
DE RecName: Full=Vitellin light chain;
DE Short=VL;
DE Contains:
DE RecName: Full=Vitellin light chain rare isoform;
DE Contains:
DE RecName: Full=Vitellin heavy chain rare isoform;
DE Contains:
DE RecName: Full=Vitellin heavy chain;
DE Short=VH;
DE Flags: Precursor;
GN Name=VG;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 16-25 AND 367-380.
RC STRAIN=Kinshu X Showa; TISSUE=Fat body;
RX PubMed=8193154; DOI=10.1016/0167-4781(94)90094-9;
RA Yano K., Sakurai M.T., Watabe S., Izumi S., Tomino S.;
RT "Structure and expression of mRNA for vitellogenin in Bombyx mori.";
RL Biochim. Biophys. Acta 1218:1-10(1994).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development.
CC -!- SUBUNIT: Heterotetramer of two heavy and two light chains.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Produced by the fat body, where it is cleaved
CC before being secreted into hemolymph. Sequestered then by a single
CC class of receptor mediated endocytosis in the ovary.
CC -!- DEVELOPMENTAL STAGE: First detected in the female fat body on day-2 of
CC spinning stage, reaching maximal levels at larval-pupal ecdysis and
CC declining thereafter. Not found in the male tissues.
CC -!- INDUCTION: By ecdysteroid and juvenile hormone.
CC -!- PTM: Glycosylated and phosphorylated.
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DR EMBL; D13160; BAA02444.1; -; mRNA.
DR EMBL; D30733; BAA06397.1; -; Genomic_DNA.
DR PIR; S45289; S45289.
DR RefSeq; NP_001037309.1; NM_001043844.1.
DR AlphaFoldDB; Q27309; -.
DR SMR; Q27309; -.
DR STRING; 7091.BGIBMGA004585-TA; -.
DR PRIDE; Q27309; -.
DR GeneID; 692741; -.
DR KEGG; bmor:692741; -.
DR CTD; 36421; -.
DR eggNOG; KOG4338; Eukaryota.
DR HOGENOM; CLU_002645_0_0_1; -.
DR InParanoid; Q27309; -.
DR OrthoDB; 36651at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:8193154"
FT CHAIN 16..1782
FT /note="Vitellogenin"
FT /id="PRO_0000041545"
FT CHAIN 16..370
FT /note="Vitellin light chain"
FT /id="PRO_0000041546"
FT CHAIN 16..366
FT /note="Vitellin light chain rare isoform"
FT /id="PRO_0000041547"
FT CHAIN 367..1782
FT /note="Vitellin heavy chain rare isoform"
FT /id="PRO_0000041548"
FT CHAIN 371..1782
FT /note="Vitellin heavy chain"
FT /id="PRO_0000041549"
FT DOMAIN 34..812
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1449..1638
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 333..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 569
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 1357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1451..1602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1782 AA; 203054 MW; 9EABC2F731E108DB CRC64;
MKLFVLAAII AAVSSDRFSS QSQSTGGQTY PSPWQVGKQY RYEVTSRTLA HLQEGPSSGS
AFKAQFTIRV KSPGRLQAKL ENPQHGNFNE QLPDPRELPV DLKYQPTPNI DKVFEIEIDG
GRIVSLDFPT SVPVPQENLI KGLISALQLD TSAHRVIHDS QNNYDREQQQ GLFRKMETDV
TGDCETLYTV SPVASEWRRE LPKFANEQDP VEVTKSTNYG HCHHRVAYHF GVPVGAEWTG
TAHKTQEQQL IGRATYSRIL TGKEGPIYKA ETTSTVHVHP HLYGKQKAEV YSHVHMELIS
VDQDSGAEWP RAGAMRPAQS ILYSLSTKQM TKHYESSSSS SSSESHEFNF PEQHEHPHQS
NQRSRRSYMR SKLVTVHKVL KKRNSESSSG SSSSSADSSS TYINDDIPDI DEPAYAALYM
SPQPHADKKQ NAMNAQKILQ DIAQQLQNPN NMPKSDFLSK FNILVRLIAS MSTEQLSQTS
RSIETAKTSN NIIKSDMWMI FRDGVTQAGT LPAFKQIQSW IENKKIQEEE AAQVVVALPR
TLRYPTKQIM TQFFNFARSP AVKDQMFLNS SALMAATKLI NLGQVNNYTA HSYYPTHMYG
RLTHKHDAFV LEEILPTLAA DLKATVEYKD STKAQVYIQA IGNLGHREIL KVFAPYLEGK
VEISTYLRTH IVKNLKTLAK LRDRHVRAVL FSILRNTAEP YPVRVAAIQS IFISHPTGEM
MQAMAEMTHN DPSVEVRAVL KSAILSAAEL QHPRNFYLSR TAQAARYLVT NEEFGYQHSF
KFIDDSYDED NDIGTFVISH IGSEDSLLPK DFKIVTNSKG GAWERNTIEA SFSSAERFLD
YLRDSVFAPH PKFDRAHKYS AEKIAKLLNI KNDEEEPLEA SFYVDFMNNQ RLFSFSESDL
QQLSQYISEY MKKVESGAEK HYTKVYNQDQ VSIMFPVASG MPFIFKYKEP AVIHFQSKLK
GKFSFPSKDN KYYEANMIKD VQFTYAINID GNVGFMDTLS NQYSSVGVVN KLQFNIPFKF
GIEIKSGLIK FRVEPLHPDQ DQTLVHYSVW PYSASQKKDS LVAISQDPAT KIVERRSKVF
SVDSKYGQST HAVIYAQGYT YSSDWRNFGA KFTSRDYFTN LASLLTQEDI ALTHFNLKHL
CKQSQSKALT ITAYYDEYYN QQNSGILTDA TDRNDLSPNS ETRRAEMVKL VSAGINKARV
RVVDLSASFE GSQDQNYVLT GTWGDSPVDS KVQGMLFAGT KSATQGNQQI NAVFATTKPE
IHSLSFSKPL QSDLRAPFGM HFKYGQSGEI RVSGSFDRTK KYTTELENHP LAKQCSQQTT
LNNFYQDSCH KAIVMAHAPD HVEFSVSFQD MSPQYRNFSY HTYRLYEYLG YWYTEANPLK
LTQNGKMDFK IDFSYFDRTY TVDIASPSGE ARMRDMPIAT MAPGALSFYQ PLKAYELVAN
YFTGHQYQPY CSIDGTRIHT FSNRSYEYPL SRSWHVVMQD ESTQRGNWHE LAILSRRQQR
DQQEIYISYK SESGQDLEIE IQPASGDSAY QVKVTTNTKK ITDDDLTMYW DDVKEQPFLQ
YHTHKDGVLV INIEDDRIRA IYDGQRFVVF TQDYRNSTRG ICGRMSGEQR DDYLTPEGLV
DKPELYAAAY SLNEENSDPK TQELKALATQ QAYYPEYKYT SILRSDPTWQ EESQSCGEDQ
WQSETVYKSR SYDKHKGACE VRQQVQFYEN HGDICITTSR VPSCQSHCRA GDYKIQHVQV
TCKSKLDHDF RMYKEQIKKG QNPEVSGIPS VKQFKVPVTC QP
