VIT2_FUNHE
ID VIT2_FUNHE Reviewed; 1687 AA.
AC Q98893;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Vitellogenin-2;
DE AltName: Full=Vitellogenin II;
DE Short=VTG II;
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;
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 16-35.
RC TISSUE=Liver;
RA Lafleur G.J. Jr., Byrne B.M., Haux C., Greenberg R.M., Wallace R.A.;
RT "Liver-derived cDNAs: vitellogenins and vitelline envelope protein
RT precursors (choriogenins).";
RL Int. Symp. Reprod. Physiol. Fish 5:336-338(1995).
CC -!- FUNCTION: Precursor of the 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 lipovitellins and phosvitin.
CC -!- INDUCTION: By steroids (estrogen). Expression of VTG II is lower than
CC that of VTG I.
CC -!- PTM: Phosvitin, an egg yolk storage protein, is one of the most highly
CC phosphorylated (10%) proteins in nature. {ECO:0000250}.
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DR EMBL; U70826; AAB17152.1; -; mRNA.
DR PIR; T43144; T43144.
DR AlphaFoldDB; Q98893; -.
DR SMR; Q98893; -.
DR STRING; 8078.ENSFHEP00000003399; -.
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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1687
FT /note="Vitellogenin-2"
FT /id="PRO_0000041568"
FT CHAIN 16..?
FT /note="Lipovitellin-1"
FT /id="PRO_0000041569"
FT CHAIN ?1083..?1230
FT /note="Phosvitin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041570"
FT CHAIN ?..1687
FT /note="Lipovitellin-2"
FT /id="PRO_0000041571"
FT DOMAIN 24..663
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1417..1593
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1081..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1004
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 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1419..1556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1442..1592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1687 AA; 186006 MW; 4965BB9DBFB4928F CRC64;
MRVLVLALTV ALVAGNQVSY APEFAPGKTY EYKYEGYILG GLPEEGLAKA GVKIQSKVLI
GAAGPDSYIL KLEDPVISGY SGIWPKEVFH PATKLTSALS AQLLTPVKFE YANGVIGKVF
APPGISTNVL NVFRGLLNMF QMNIKKTQNV YDLQETGVKG VCKTHYILHE DSKADRLHLT
KTTDLNHCTD SIHMDVGMAG YTEKCAECMA RGKTLSGAIS VNYIMKPSAS GTLILEATAT
ELLQYSPVNI VNGAVQMEAK QTVTFVDIRK TPLEPLKADY IPRGSLKYEL GTEFLQTPIQ
LLRITNVEAQ IVESLNNLVS LNMGHAHEDS PLKFIELIQL LRVAKYESIE ALWSQFKTKI
DHRHWLLSSI PAIGTHVALK FIKEKIVAGE VTAAEAAQAI MSSTHLVKAD LEAIKLQEGL
AVTPNIRENA GLRELVMLGF GIMVHKYCVE NPSCPSELVR PVHDIIAKAL EKRDNDELSL
ALKVLGNAGH PSSLKPIMKL LPGFGSSASE LELRVHIDAT LALRKIGKRE PKMIQDVALQ
LFMDRTLDPE LRMVAVVVLF DTKLPMGLIT TLAQSLLKEP NLQVLSFVYS YMKAFTKTTT
PDHSTVAAAC NVAIRILSPR FERLSYRYSR AFHYDHYHNP WMLGAAASAF YINDAATVLP
KNIMAKARVY LSGVSVDVLE FGARAEGVQE ALLKARDVPE SADRLTKMKQ ALKALTEWRA
NPSRQPLGSL YVKVLGQDVA FANIDKEMVE KIIEFATGPE IRTRGKKALD ALLSGYSMKY
SKPMSAIEVR HIFPTSLGLP MELSLYTAAV TAASVEVQAT ISPPLPEDFH PAHLLKSDIS
MKASVTPSVS LHTYGVMGVN SPFIQASVLS RAKDHAALPK KMEARLDIVK GYFSYQFLPV
EGVKTIASAR LETVAIARDV EGLAAAKVTP VVPYEPIVSK NATLNLSQMS YYLNDSISAS
SELLPFSLQR QTGKNKIPKP IVKKMCATTY TYGIEGCVDI WSRNATFLRN TPIYAIIGNH
SLLVNVTPAA GPSIERIEIE VQFGEQAAEK ILKEVYLNEE EEVLEDKNVL MKLKKILSPG
LKNSTKASSS SSGSSRSSRS RSSSSSSSSS SSSSSRSSSS SSRSSSSLRR NSKMLDLADP
LNITSKRSSS SSSSSSSSSS SSSSSSSSSK TKWQLHERNF TKDHIHQHSV SKERLNSKSS
ASSFESIYNK ITYLSNIVSP VVTVLVRAIR ADHKNQGYQI AVYYDKLTTR VQIIVANLTE
DDNWRICSDS MMLSHHKVMT RVTWGIGCKQ YNTTIVAETG RVEKEPAVRV KLAWARLPTY
IRDYARRVSR YISRVAEDNG VNRTKVASKP KEIKLTVAVA NETSLNVTLN TPKNTFFKLG
WVLPFYLPIN NTAAELQAFQ GRWMDQVTYM LTKSAAAECT VVEDTVVTFN NRKYKTETPH
SCHQVLAQDC TSEIKFIVLL KRDQTAERNE ISIKIENIDV DMYPKDNAVV VKVNGVEIPL
TNLPYQHPTG NIQIRQREEG ISLHAPSHGL QEVFLSLNKV QVKVVDWMRG QTCGLCGKAD
GEVRQEYSTP NERVSRNATS FAHSWVLPAK SCRDASECYM QLESVKLEKQ ISLEGEESKC
YSVEPVWRCL PGCAPVRTTS VTVGLPCVSL DSNLNRSDSL SSIYQKSVDV SETAESHLAC
RCTPQCA
