VIT1_CHICK
ID VIT1_CHICK Reviewed; 1912 AA.
AC P87498;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Vitellogenin-1;
DE AltName: Full=Minor vitellogenin;
DE AltName: Full=Vitellogenin I;
DE Contains:
DE RecName: Full=Lipovitellin-1;
DE AltName: Full=Lipovitellin I;
DE Short=LVI;
DE Contains:
DE RecName: Full=Phosvitin;
DE Short=PV;
DE Contains:
DE RecName: Full=Lipovitellin-2;
DE AltName: Full=Lipovitellin II;
DE Short=LVII;
DE Contains:
DE RecName: Full=YGP42 {ECO:0000303|PubMed:20509661};
DE AltName: Allergen=Gal d 6 {ECO:0000303|PubMed:20509661};
DE Flags: Precursor;
GN Name=VTG1; Synonyms=VTGI;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Mabuchi N., Yamamura J., Adachi T., Aoki N., Nakamura R., Matsuda T.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1628-1639, AND IDENTIFICATION OF YGP42.
RX PubMed=7599159; DOI=10.1016/0304-4165(95)00033-8;
RA Yamamura J., Adachi T., Aoki N., Nakajima H., Nakamura R., Matsuda T.;
RT "Precursor-product relationship between chicken vitellogenin and the yolk
RT proteins: the 40 kDa yolk plasma glycoprotein is derived from the C-
RT terminal cysteine-rich domain of vitellogenin II.";
RL Biochim. Biophys. Acta 1244:384-394(1995).
RN [3]
RP IGE-BINDING.
RX PubMed=20509661; DOI=10.1021/jf101403h;
RA Amo A., Rodriguez-Perez R., Blanco J., Villota J., Juste S., Moneo I.,
RA Caballero M.L.;
RT "Gal d 6 is the second allergen characterized from egg yolk.";
RL J. Agric. Food Chem. 58:7453-7457(2010).
RN [4]
RP ALLERGEN.
RX PubMed=26897338; DOI=10.1016/j.molimm.2016.02.005;
RA De Silva C., Dhanapala P., Doran T., Tang M.L.K., Suphioglu C.;
RT "Molecular and immunological analysis of hen's egg yolk allergens with a
RT focus on YGP42 (Gal d 6).";
RL Mol. Immunol. 71:152-160(2016).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during early development of oviparous organisms.
CC -!- FUNCTION: Phosvitin is believed to be of importance in sequestering
CC calcium, iron and other cations for the developing embryo.
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.
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 -!- PTM: Cathepsin D is responsible for intraoocytic processing of
CC vitellogenin.
CC -!- PTM: May contain intrachain disulfide bonds.
CC -!- ALLERGEN: [YGP42]: Causes an allergic reaction in human
CC (PubMed:26897338). Binds to IgE (PubMed:20509661, PubMed:26897338).
CC {ECO:0000269|PubMed:20509661, ECO:0000269|PubMed:26897338}.
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DR EMBL; D89547; BAA13973.1; -; mRNA.
DR PIR; T29088; T29088.
DR RefSeq; NP_001004408.1; NM_001004408.2.
DR AlphaFoldDB; P87498; -.
DR SMR; P87498; -.
DR STRING; 9031.ENSGALP00000032611; -.
DR Allergome; 8172; Gal d 6.
DR Allergome; 8173; Gal d 6.0101.
DR PaxDb; P87498; -.
DR GeneID; 424547; -.
DR KEGG; gga:424547; -.
DR CTD; 559475; -.
DR VEuPathDB; HostDB:geneid_424547; -.
DR eggNOG; KOG4338; Eukaryota.
DR InParanoid; P87498; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; P87498; -.
DR PRO; PR:P87498; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IBA:GO_Central.
DR GO; GO:0032355; P:response to estradiol; IBA:GO_Central.
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 Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Reference proteome; Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1912
FT /note="Vitellogenin-1"
FT /id="PRO_0000041552"
FT CHAIN 16..1139
FT /note="Lipovitellin-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041553"
FT CHAIN 1140..1391
FT /note="Phosvitin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041554"
FT CHAIN 1392..1627
FT /note="Lipovitellin-2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041555"
FT CHAIN 1628..1912
FT /note="YGP42"
FT /id="PRO_0000041556"
FT DOMAIN 24..663
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1640..1818
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 948..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1206
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 1662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1642..1781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1665..1817
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1912 AA; 210630 MW; 89BA6273D6492E51 CRC64;
MRGLISALVL TLVGSQHLNY QPDFGENKVY TYNYESILFS GIPEKGLART GIRIRSEVEI
SGIGPKLCLI RIHSIEAAEY NGIWPTSSFS RSLKLTQALT GQLSIPIKFE YSNGHVGNLM
APDSVSDDGL NIYRGILNIL ELSLKKMQHS YSIQEAGIGG ICNTTYAIQE NKKANLVDVT
KSKDLNSCEE KVQVVTGSAY TQPCQTCQQR NKNSRATATY NYKIKYTHNE AVITQAEVEE
VHQFTPFHEI TGGNAIVEAR QKLALIEVQK QVAEVPPKEF QKRGSLQYQF GSELLQLPVH
LFKIKDVERQ IEERLQDLVE TTYEQLPSDA PAKALKLMHL LRAANEENYE SVWKQFSSRP
AYRRYLLDLL PAAASHRSLR FLRHKMERQE LTNWEIAQTV LVALHSSSPT QEVMEEATLI
VKKHCPRSSS VLRKVCLLSY ASLCHKRCSS PYSCSECLQV FHVFAGEALG KSNIEEVLLA
LKALGNVGHP ASIKHIKKFL PGYAAGASEL PLKVHETAVM ALKSIGMRDP QMVQAITLEI
FLNHKIHPRI RMLAAVVLLE TKPGLPILMI LVDAVLKEPS MQVASFIYSH LRALGRSTAP
DLQMMASACR MAVRALSPKF DRSGYQFSKV FRFSMFKEFL MSGLAAKYFV LNNAGSLIPT
MAVSQLRTHF LGRVADPIEV GIAAEGLQEM FVRGYSPDKD WETNYDFREI LKKLSDWKAL
PRDKPFASGY LKMFGQELLF GRLDKDTLQN VLQVWYGPDE KIPSIRRLIS SLQTGIGRQW
TKALLLSEIR CIVPTCVGFP METSFYYSSV TKVAGNVQAQ ITPSPRSDFR LTELLNSNVR
LRSKMSLSMA KHMTFVIGIN TNMIQAGLEA HTKVNAHVPV NVVATIQMKE KSIKAEIPPC
KEETNLIIVS SKTFAVTRNI EDLAASKMTP VLLPEAVPDI MKMSFDSDSA SGETDNIRDR
QSVEDVSSGN SFSFGHPSSG KEPFIQSMCS NASTFGVQVC IEKKSVHAAF IRNVPLYNAI
GEHALRMSFK PVYSDVPIEK IQVTIQAGDQ APTKMVRLVT FEDPERQESS RKEVMKRVKK
ILDDTDNQAT RNSRSSSSSA SSISESSEST TSTPSSSDSD NRASQGDPQI NLKSRQSKAN
EKKFYPFGDS SSSGSSSSSS SSSSSSSDSS SSSRSSSSSD SSSSSSSSSS SSSSKSKSSS
RSSKSNRSSS SSNSKDSSSS SSKSNSKGSS SSSSKASGTR QKAKKQSKTT SFPHASAAEG
ERSVHEQKQE TQSSSSSSSR ASSNSRSTSS STSSSSESSG VSHRQWKQDR EAETKRVKSQ
FNSHSSYDIP NEWETYLPKV YRLRFRSAHT HWHSGHRTSS SSSSSSSESG SSHSNSSSSD
SSSRRSHMSD SSSSSSSHRH GEKAAHSSRR SPTSRAASAH HRPGSSLTRE RNFLGDVIPP
GITIVAQAVR SDNRNQGYQA TAYVRSDAAK VDVQLVVVQL AETNWKACAD AVILPLKAQA
RMRWGKECRD YRIAALATTG QMARKLAVQL KVQWGIIPSW IKKTSTALMR YVPGVALVLG
FSEAHQRNPS RELIVRAVAT SPRSIDTVIK VPGVTLYYQG LRVPFTLALG ASSSSYETRD
ITAWNFLPEI ASQIAQEDQS TCEVSKGDFK TFDRMSFTCS FNKSCNVVVA QDCTEHPKFI
ITTRKVDHQS LSREVHINTS SANITICPAA DSSLLVTCNK ESVLSDSGVS EYEKDNIKIY
KNGKTVIVEA PIHGLKNVNF DGEILKVTVA SWMRGKTCGV CGNNDREKHN ELLMPNHKLA
HSCSAFVHSW VLLEETCSGG CKLQRRYVKL NRNPTIDGEE STCYSVDPVL KCMKDCTPIE
KTSVKVGFHC FPKATAVSLL EWQRSSDKKS ASEDVVESVD ADIDCTCTGD CS
