VIT_ONCMY
ID VIT_ONCMY Reviewed; 1659 AA.
AC Q92093; P79882; Q91190; Q92092;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Vitellogenin;
DE Short=VTG;
DE Contains:
DE RecName: Full=Lipovitellin I;
DE Short=LVI;
DE Contains:
DE RecName: Full=Phosvitin;
DE Short=PV;
DE Contains:
DE RecName: Full=Lipovitellin II;
DE Short=LVII;
DE Flags: Precursor;
GN Name=vtg1;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8863729; DOI=10.1016/0378-1119(96)00336-8;
RA Mouchel N., Trichet V., Betz A., le Pennec J.-P., Wolff J.;
RT "Characterization of vitellogenin from rainbow trout (Oncorhynchus
RT mykiss).";
RL Gene 174:59-64(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1208-1659.
RC TISSUE=Liver;
RX PubMed=3192063; DOI=10.1016/0016-6480(88)90264-x;
RA le Guellec K., Lawless K., Valotaire Y., Kress M., Tenniswood M.;
RT "Vitellogenin gene expression in male rainbow trout (Salmo gairdneri).";
RL Gen. Comp. Endocrinol. 71:359-371(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1331-1603.
RX PubMed=8599856; DOI=10.1016/0009-2797(95)03686-5;
RA Ren L., Lewis S.K., Lech J.J.;
RT "Effects of estrogen and nonylphenol on the post-transcriptional regulation
RT of vitellogenin gene expression.";
RL Chem. Biol. Interact. 100:67-76(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 894-1301, AND PROTEIN SEQUENCE OF 1089-1093.
RC TISSUE=Liver;
RX PubMed=8756342; DOI=10.1089/dna.1996.15.605;
RA Goulas A., Triplett E.L., Taborsky G.;
RT "Isolation and characterization of a vitellogenin cDNA from rainbow trout
RT (Oncorhynchus mykiss) and the complete sequence of a phosvitin coding
RT segment.";
RL DNA Cell Biol. 15:605-616(1996).
CC -!- FUNCTION: Precursor of the major egg-yolk proteins that are sources of
CC nutrients during early development of oviparous organisms.
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 lipovitellin-I, phosvitin, lipovitellin-II.
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 ---------------------------------------------------------------------------
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; X92804; CAA63421.1; -; Genomic_DNA.
DR EMBL; M27651; AAA81577.1; -; mRNA.
DR EMBL; U26703; AAB02176.1; -; Genomic_DNA.
DR EMBL; S82450; AAB37720.1; -; mRNA.
DR PIR; JC4956; JC4956.
DR AlphaFoldDB; Q92093; -.
DR SMR; Q92093; -.
DR Allergome; 7654; Onc m 5.
DR PRIDE; Q92093; -.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0060417; C:yolk; IDA:AgBase.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IPI:AgBase.
DR GO; GO:0034605; P:cellular response to heat; IDA:AgBase.
DR GO; GO:0032355; P:response to estradiol; IDA:AgBase.
DR GO; GO:0032868; P:response to insulin; IDA:AgBase.
DR GO; GO:1903165; P:response to polycyclic arene; IDA:AgBase.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.20.50.20; -; 2.
DR Gene3D; 2.20.90.10; -; 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; IPR015258; Vitellinogen_b-sht_shell.
DR InterPro; IPR037088; Vitellinogen_b-sht_shell_sf.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF09172; DUF1943; 1.
DR Pfam; PF09175; DUF1944; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM01170; DUF1944; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 3.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1659
FT /note="Vitellogenin"
FT /id="PRO_0000041580"
FT CHAIN 16..1088
FT /note="Lipovitellin I"
FT /id="PRO_0000041581"
FT CHAIN 1089..1145
FT /note="Phosvitin"
FT /id="PRO_0000041582"
FT CHAIN 1146..1659
FT /note="Lipovitellin II"
FT /id="PRO_0000041583"
FT DOMAIN 24..662
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1389..1565
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1090..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1089
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1391..1528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1414..1564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT VARIANT 1130
FT /note="I -> T"
FT CONFLICT 894
FT /note="F -> L (in Ref. 4; AAB37720)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="Missing (in Ref. 4; AAB37720)"
FT /evidence="ECO:0000305"
FT CONFLICT 1158
FT /note="S -> P (in Ref. 4; AAB37720)"
FT /evidence="ECO:0000305"
FT CONFLICT 1208..1218
FT /note="TAYLNKATSRL -> LGRPKTTSDEP (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="M -> T (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1246
FT /note="T -> N (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1254
FT /note="E -> G (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1278..1281
FT /note="RLSW -> L (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1305
FT /note="Y -> H (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1322
FT /note="N -> S (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331..1335
FT /note="VATSE -> LPHLK (in Ref. 3; AAB02176)"
FT /evidence="ECO:0000305"
FT CONFLICT 1352
FT /note="L -> T (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1419
FT /note="A -> G (in Ref. 3; AAB02176)"
FT /evidence="ECO:0000305"
FT CONFLICT 1431..1443
FT /note="LLKKDHASEQNHI -> SAEEGSVHLTKTRS (in Ref. 2;
FT AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1457
FT /note="E -> Q (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1470
FT /note="I -> V (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1473..1474
FT /note="DN -> EQ (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1490..1491
FT /note="GK -> KGE (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1491
FT /note="K -> E (in Ref. 2; AAA81577 and 3; AAB02176)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504
FT /note="E -> K (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1509..1512
FT /note="KYSW -> SNSR (in Ref. 3; AAB02176)"
FT /evidence="ECO:0000305"
FT CONFLICT 1546
FT /note="L -> V (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1563..1565
FT /note="SCR -> RC (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1606
FT /note="L -> S (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
FT CONFLICT 1622
FT /note="V -> F (in Ref. 2; AAA81577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1659 AA; 183128 MW; 2ADF42980339B019 CRC64;
MRAVVLALTL ALVASQSVNF APDFAASKTY VYKYEALLLG GLPEEGLARA GVKVISKVLI
SAVAENTYLL KLVNPEIFEY SGVWPKDPFV PAAKLTSALA AQFSIPIKFE YAKGVVGKVL
APTAVSETVL NVHRGILNIL QLNIKKTQNV YELQEAGAQG VCKTHYVIRE DAKAERIHLT
KSKDLNNCQQ RIMKDFGLAY TEKCVECRQR GEALMGAATY NYLMKPADNG ALILEATVTE
LHQFTPFNEM SGAAQMEAKQ MLTFVEIKKD PIIVPDNNYV HRGSIRYEFA TEILQMPIQL
LKISNARAQA VKILNHLVTY NTAPVHEDAP LKFLQFIQLL RMASSETINA IWAEFKAKPA
YRHWILDAVP SIGSSVAVRF IKEKFLAGDI TIFEAAQALV AAVHMVAADL ETVKLVESLA
FNHKIQTHPV LRELTMLGYG TMVSKYCVEH PNCPAELVKP IHELAVQAVA NSKFEELSMV
LKALGNAGHP ASIKPITKLL PVFGTAAAAL PLRVQADAVL ALRNIAKREP RMVQEVAVQL
FMDKALHPEL RMLACIVLFE TKPPMGLVIT LASILKTEKN MQVASFTYSH MMSLTRSTAP
DFASVAAACN VAVKMLSNKF RRLSCHFSQA IHLDAYSNPL RIGAAASAFY INDAATLFPR
TVVAKARTYF AGAAADVLEV GVRTEGIQEA LLKLPPAPEN ADRITKMRRV IKALSDWRSL
ATSKPLASIY VKFFGQEIAF ANIDKSIIDQ ALQLANSPSA HALGRNALKA LLAGATFQYV
KPLLAAEVRR IFPTAVGLPM ELSYYTAAVA KAYVNVRATL TPALPETFHA AQLLKTNIEL
HAEVRPSIVM HTFAVMGVNT AFIQAAIMAR AKVRTIVPAK FAAQLDIANG NFKFEAFPVS
PPEHIAAAHI ETFAVARNVE DVPAERITPL IPAQGVARST QQSRDKLTSM IADSAASFAG
SLSRSSEILY SDLPSNFKPI IKAIVVHLEE TICVERLGVK ACFEFTSESA AFIRNTLFYN
MIGKHSVLIS VKPSASEPAI ERLEFEVQVG PKAAEKIIKV ITMNEEEEAP EGKTVLLKLK
KILLPDLKNG TRASSSSSSS SSSSSRSSSS RSRSRKSESS SSSSSSSSRI SKRDGPDQPY
NPNDRKFKKN HKDSQSTSNV ISRSKSSASS FHAIYKQDKF LGNKLAPMVI ILFRLVRADH
KIEGYQVTAY LNKATSRLQI IMAALDENDN WKLCADGVLL SKHKVTAKIA WGAECKDYNT
FITAETGLVG PSPAVRLRLS WDKLPKVPKA VWRYVRIVSE FIPGYIPYYL ADLVPMQKDK
NNEKQIQFTV VATSERTLDV ILKTPKMTLY KLGVNLPCSL PFESMTDLSP FDDNIVNKIH
YLFSEVNAVK CSMVRDTLTT FNNKKYKINM PLSCYQVLAQ DCTTELKFMV LLKKDHASEQ
NHINVKISDI DVDLYTEDHG VIVKVNEMEI SNDNLPYKDP SGSIKIDRKG KGVSLYAPSH
GLQEVYFDKY SWKIKVVDWM KGQTCGLCGK ADGENRQEYR TPSGRLTKSS VSFAHSWVLP
SDSCRDASEC LMKLESVKLE KQVIVDDRES KCYSVEPVLR CLPGCLPVRT TPITIGFHCL
PVDSNLNRSE GLSSIYEKSV DLMEKAEAHV ACRCSEQCM
