VIT1_FUNHE
ID VIT1_FUNHE Reviewed; 1704 AA.
AC Q90508;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Vitellogenin-1;
DE AltName: Full=Vitellogenin I;
DE Short=VTG I;
DE Contains:
DE RecName: Full=Lipovitellin-1;
DE Short=LV1;
DE Contains:
DE RecName: Full=Phosvitin;
DE Short=PV;
DE Contains:
DE RecName: Full=Lipovitellin-2;
DE Short=LV2;
DE Flags: Precursor;
GN Name=vtg1;
OS Fundulus heteroclitus (Killifish) (Mummichog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX NCBI_TaxID=8078;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1220-1225.
RC TISSUE=Liver;
RX PubMed=7563139; DOI=10.1007/bf00160323;
RA Lafleur G.J. Jr., Byrne B.M., Kanungo J., Nelson L.D., Greenberg R.M.,
RA Wallace R.A.;
RT "Fundulus heteroclitus vitellogenin: the deduced primary structure of a
RT piscine precursor to noncrystalline, liquid-phase yolk protein.";
RL J. Mol. Evol. 41:505-521(1995).
RN [2]
RP SEQUENCE REVISION TO 98-113.
RC TISSUE=Liver;
RA LaFleur G.J. Jr., Cerda J.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 285-303; 413-437; 964-1001; 1220-1230; 1254-1260 AND
RP 1439-1455.
RC TISSUE=Egg, and Oocyte;
RX PubMed=15930322; DOI=10.1095/biolreprod.105.041335;
RA LaFleur G.J. Jr., Raldua D., Fabra M., Carnevali O., Denslow N.,
RA Wallace R.A., Cerda J.;
RT "Derivation of major yolk proteins from parental vitellogenins and
RT alternative processing during oocyte maturation in Fundulus heteroclitus.";
RL Biol. Reprod. 73:815-824(2005).
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 composed of complex suite of small cleavage products.
CC -!- PTM: Phosvitin, an egg yolk storage protein, is one of the most highly
CC phosphorylated (10%) proteins in nature. {ECO:0000250}.
CC -!- PTM: The N-terminal of the blood vitellogenin is blocked.
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DR EMBL; U07055; AAA93123.2; -; mRNA.
DR PIR; T43141; T43141.
DR AlphaFoldDB; Q90508; -.
DR SMR; Q90508; -.
DR STRING; 8078.ENSFHEP00000029770; -.
DR PRIDE; Q90508; -.
DR Proteomes; UP000265000; Whole Genome Shotgun Assembly.
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; 2.20.50.20; -; 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..14
FT /evidence="ECO:0000255"
FT CHAIN 15..1704
FT /note="Vitellogenin-1"
FT /id="PRO_0000041564"
FT CHAIN 15..?
FT /note="Lipovitellin-1"
FT /id="PRO_0000041565"
FT CHAIN ?1081..?1258
FT /note="Phosvitin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041566"
FT CHAIN ?..1704
FT /note="Lipovitellin-2"
FT /id="PRO_0000041567"
FT DOMAIN 22..660
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1442..1617
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1078..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1054
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1444..1580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1467..1616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1704 AA; 187924 MW; ED49D83AD8D79393 CRC64;
MKAVVLALTL AFVAGQNFAP EFAAGKTYVY KYEALILGGL PEEGLARAGL KISTKLLLSA
ADQNTYMLKL VEPELSEYSG IWPKDPAVPA TKLTAALAPQ LAIPIKFEYT NGVVGKVFAP
EEVSTLVLNI YRGILNILQL NIKKTHKVYD LQEVGTQGVC KTLYSISEDA RIENILLTKT
RDLSNCQERL NKDIGLAYTE KCDKCQEETK NLRGTTTLSY VLKPVADAVM ILKAYVNELI
QFSPFSEANG AAQMRTKQSL EFLEIEKEPI PSVKAEYRHR GSLKYEFSDE LLQTPLQLIK
ISDAPAQVAE VLKHLATYNI EDVHENAPLK FLELVQLLRI ARYEDLEMYW NQYKKMSPHR
HWFLDTIPAT GTFAGLRFIK EKFMAEEITI AEAAQAFITA VHMVTADPEV IKLFESLVDS
DKVVENPLLR EVVFLGYGTM VNKYCNKTVD CPVELIKPIQ QRLSDAIAKN EEENIILYIK
VLGNAGHPSS FKSLTKIMPI HGTAAVSLPM TIHVEAIMAL RNIAKKESRM VQELALQLYM
DKALHPELRM LSCIVLFETS PSMGLVTTVA NSVKTEENLQ VASFTYSHMK SLSRSPATIH
PDVAAACSAA MKILGTKLDR LSLRYSKAVH VDLYNSSLAV GAAATAFYIN DAATFMPKSF
VAKTKGFIAG STAEVLEIGA NIEGLQELIL KNPALSESTD RITKMKRVIK ALSEWRSLPT
SKPLASVYVK FFGQEIGFAN IDKPMIDKAV KFGKELPIQE YGREALKALL LSGINFHYAK
PVLAAEMRRI LPTVAGIPME LSLYSAAVAA ASVEIKPNTS PRLSADFDVK TLLETDVELK
AEIRPMVAMD TYAVMGLNTD IFQAALVARA KLHSVVPAKI AARLNIKEGD FKLEALPVDV
PENITSMNVT TFAVARNIEE PLVERITPLL PTKVLVPIPI RRHTSKLDPT RNSMLDSSEL
LPMEEEDVEP IPEYKFRRFA KKYCAKHIGV GLKACFKFAS QNGASIQDIV LYKLAGSHNF
SFSVTPIEGE VVERLEMEVK VGAKAAEKLV KRINLSEDEE TEEGGPVLVK LNKILSSRRN
SSSSSSSSSS SSSESRSSRS SSSSSSSSRS SRKIDLAART NSSSSSSSRR SRSSSSSSSS
SSSSSSSSSS SSRRSSSSSS SSSSSSSRSS RRVNSTRSSS SSSRTSSASS LASFFSDSSS
SSSSSDRRSK EVMEKFQRLH KKMVASGSSA SSVEAIYKEK KYLGEEEAVV AVILRAVKAD
KRMVGYQLGF YLDKPNARVQ IIVANISSDS NWRICADAVV LSKHKVTTKI SWGEQCRKYS
TNVTGETGIV SSSPAARLRV SWERLPSTLK RYGKMVNKYV PVKILSDLIH TKRENSTRNI
SVIAVATSEK TIDIITKTPM SSVYNVTMHL PMCIPIDEIK GLSPFDEVID KIHFMVSKAA
AAECSFVEDT LYTFNNRSYK NKMPSSCYQV AAQDCTDELK FMVLLRKDSS EQHHINVKIS
EIDIDMFPKD DNVTVKVNEM EIPPPACLTA TQQLPLKIKT KRRGLAVYAP SHGLQEVYFD
RKTWRIKVAD WMKGKTCGLC GKADGEIRQE YHTPNGRVAK NSISFAHSWI LPAESCRDAS
ECRLKLESVQ LEKQLTIHGE DSTCFSVEPV PRCLPGCLPV KTTPVTVGFS CLASDPQTSV
YDRSVDLRQT TQAHLACSCN TKCS
