VIT2_CHICK
ID VIT2_CHICK Reviewed; 1850 AA.
AC P02845; Q6LBT2; Q91026; Q91027;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Vitellogenin-2;
DE AltName: Full=Major vitellogenin;
DE AltName: Full=Vitellogenin II;
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=YGP40;
DE Flags: Precursor;
GN Name=VTG2; Synonyms=VTGII;
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 [GENOMIC DNA].
RX PubMed=3477646; DOI=10.1016/0022-2836(87)90688-7;
RA van Het Schip A.D., Samallo J., Broos J., Ophuis J., Mojet M., Gruber M.,
RA Ab G.;
RT "Nucleotide sequence of a chicken vitellogenin gene and derived amino acid
RT sequence of the encoded yolk precursor protein.";
RL J. Mol. Biol. 196:245-260(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3680202; DOI=10.1016/s0021-9258(18)47735-6;
RA Nardelli D., Het Schip F.D., Gerber-Huber S., Haefliger J.-A., Gruber M.,
RA Ab G., Wahli W.;
RT "Comparison of the organization and fine structure of a chicken and a
RT Xenopus laevis vitellogenin gene.";
RL J. Biol. Chem. 262:15377-15385(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RX PubMed=6199194; DOI=10.1002/j.1460-2075.1983.tb01734.x;
RA Walker P., Brown-Luedi M., Germond J.-E., Wahli W., Meijlink F.C.P.W.,
RA van Het Schip A.D., Roelink H., Gruber M., Geert A.B.;
RT "Sequence homologies within the 5' end region of the estrogen-controlled
RT vitellogenin gene in Xenopus and chicken.";
RL EMBO J. 2:2271-2279(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RX PubMed=6694908; DOI=10.1093/nar/12.2.1117;
RA Burch J.B.E.;
RT "Identification and sequence analysis of the 5' end of the major chicken
RT vitellogenin gene.";
RL Nucleic Acids Res. 12:1117-1135(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1092-1338.
RX PubMed=6091745; DOI=10.1021/bi00314a003;
RA Byrne B.M., van Het Schip A.D., van de Klundert J.A.M., Arnberg A.C.,
RA Gruber M., Ab G.;
RT "Amino acid sequence of phosvitin derived from the nucleotide sequence of
RT part of the chicken vitellogenin gene.";
RL Biochemistry 23:4275-4279(1984).
RN [6]
RP PROTEIN SEQUENCE OF 1112-1188.
RX PubMed=4065410; DOI=10.1016/0020-711x(85)90243-5;
RA Clark R.C.;
RT "The primary structure of avian phosvitins. Contributions through the Edman
RT degradation of methylmercaptovitins prepared from the constituent
RT phosphoproteins.";
RL Int. J. Biochem. 17:983-988(1985).
RN [7]
RP PROTEIN SEQUENCE OF 1567-1580, AND IDENTIFICATION OF CHAINS.
RC TISSUE=Liver;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1705-1757.
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=2494348; DOI=10.1007/bf02102475;
RA Philipsen J.N.J., De Vries J.E., Samallo J., Van Dijk C., Arnberg A.C.,
RA Ab G.;
RT "Characterization of a polymorphism in the 3' part of the chicken
RT vitellogenin gene.";
RL J. Mol. Evol. 28:185-190(1989).
CC -!- FUNCTION: Precursor of the major 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: After incorporation from serum via a specific
CC receptor, it is cleaved into four fragments, heavy and light chain
CC lipovitellins, phosphovitin and YGP40, and YGP40 is released into the
CC yolk plasma before or during compartmentation of lipovitellin-phosvitin
CC complex into the yolk granule.
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 -!- MISCELLANEOUS: Vitellogenin II is the most abundant of the three
CC vitellogenins (I, II, and III).
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DR EMBL; X00345; CAA25096.1; -; Genomic_DNA.
DR EMBL; M18060; AAA49139.1; -; Genomic_DNA.
DR EMBL; X00204; CAA25027.1; -; Genomic_DNA.
DR EMBL; X13607; CAA31942.1; -; Genomic_DNA.
DR EMBL; K02113; AAA98791.1; -; Genomic_DNA.
DR EMBL; X14729; CAA32851.1; -; Genomic_DNA.
DR PIR; I50441; VJCH2.
DR RefSeq; NP_001026447.1; NM_001031276.1.
DR AlphaFoldDB; P02845; -.
DR SMR; P02845; -.
DR STRING; 9031.ENSGALP00000002888; -.
DR PaxDb; P02845; -.
DR PRIDE; P02845; -.
DR GeneID; 424533; -.
DR KEGG; gga:424533; -.
DR CTD; 559931; -.
DR VEuPathDB; HostDB:geneid_424533; -.
DR eggNOG; KOG4338; Eukaryota.
DR InParanoid; P02845; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; P02845; -.
DR PRO; PR:P02845; -.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Reference proteome; Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1850
FT /note="Vitellogenin-2"
FT /id="PRO_0000041557"
FT CHAIN 16..1111
FT /note="Lipovitellin-1"
FT /id="PRO_0000041558"
FT CHAIN 1112..1328
FT /note="Phosvitin"
FT /id="PRO_0000041559"
FT CHAIN 1329..1566
FT /note="Lipovitellin-2"
FT /id="PRO_0000041560"
FT CHAIN 1567..1850
FT /note="YGP40"
FT /id="PRO_0000041561"
FT DOMAIN 24..662
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1579..1756
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 935..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1280
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 1417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 1581..1719
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1604..1755
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT VARIANT 1840
FT /note="T -> A"
FT CONFLICT 14
FT /note="G -> AHVVFLSLFVG (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="S -> SKT (in Ref. 2; AAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="R -> L (in Ref. 2; AAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="S -> A (in Ref. 2; AAA49139)"
FT /evidence="ECO:0000305"
FT CONFLICT 1436..1437
FT /note="HK -> PQ (in Ref. 2; AAA49139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1850 AA; 204808 MW; F3D546F6150A1DEA CRC64;
MRGIILALVL TLVGSQKFDI DPGFNSRRSY LYNYEGSMLN GLQDRSLGKA GVRLSSKLEI
SGLPENAYLL KVRSPQVEEY NGVWPRDPFT RSSKITQVIS SCFTRLFKFE YSSGRIGNIY
APEDCPDLCV NIVRGILNMF QMTIKKSQNV YELQEAGIGG ICHARYVIQE DRKNSRIYVT
RTVDLNNCQE KVQKSIGMAY IYPCPVDVMK ERLTKGTTAF SYKLKQSDSG TLITDVSSRQ
VYQISPFNEP TGVAVMEARQ QLTLVEVRSE RGSAPDVPMQ NYGSLRYRFP AVLPQMPLQL
IKTKNPEQRI VETLQHIVLN NQQDFHDDVS YRFLEVVQLC RIANADNLES IWRQVSDKPR
YRRWLLSAVS ASGTTETLKF LKNRIRNDDL NYIQTLLTVS LTLHLLQADE HTLPIAADLM
TSSRIQKNPV LQQVACLGYS SVVNRYCSQT SACPKEALQP IHDLADEAIS RGREDKMKLA
LKCIGNMGEP ASLKRILKFL PISSSSAADI PVHIQIDAIT ALKKIAWKDP KTVQGYLIQI
LADQSLPPEV RMMACAVIFE TRPALALITT IANVAMKESN MQVASFVYSH MKSLSKSRLP
FMYNISSACN IALKLLSPKL DSMSYRYSKV IRADTYFDNY RVGATGEIFV VNSPRTMFPS
AIISKLMANS AGSVADLVEV GIRVEGLADV IMKRNIPFAE YPTYKQIKEL GKALQGWKEL
PTETPLVSAY LKILGQEVAF ININKELLQQ VMKTVVEPAD RNAAIKRIAN QIRNSIAGQW
TQPVWMGELR YVVPSCLGLP LEYGSYTTAL ARAAVSVEGK MTPPLTGDFR LSQLLESTMQ
IRSDLKPSLY VHTVATMGVN TEYFQHAVEI QGEVQTRMPM KFDAKIDVKL KNLKIETNPC
REETEIVVGR HKAFAVSRNI GELGVEKRTS ILPEDAPLDV TEEPFQTSER ASREHFAMQG
PDSMPRKQSH SSREDLRRST GKRAHKRDIC LKMHHIGCQL CFSRRSRDAS FIQNTYLHKL
IGEHEAKIVL MPVHTDADID KIQLEIQAGS RAAARIITEV NPESEEEDES SPYEDIQAKL
KRILGIDSMF KVANKTRHPK NRPSKKGNTV LAEFGTEPDA KTSSSSSSAS STATSSSSSS
ASSPNRKKPM DEEENDQVKQ ARNKDASSSS RSSKSSNSSK RSSSKSSNSS KRSSSSSSSS
SSSSRSSSSS SSSSSNSKSS SSSSKSSSSS SRSRSSSKSS SSSSSSSSSS SSKSSSSRSS
SSSSKSSSHH SHSHHSGHLN GSSSSSSSSR SVSHHSHEHH SGHLEDDSSS SSSSSVLSKI
WGRHEIYQYR FRSAHRQEFP KRKLPGDRAT SRYSSTRSSH DTSRAASWPK FLGDIKTPVL
AAFLHGISNN KKTGGLQLVV YADTDSVRPR VQVFVTNLTD SSKWKLCADA SVRNAHKAVA
YVKWGWDCRD YKVSTELVTG RFAGHPAAQV KLEWPKVPSN VRSVVEWFYE FVPGAAFMLG
FSERMDKNPS RQARMVVALT SPRTCDVVVK LPDIILYQKA VRLPLSLPVG PRIPASELQP
PIWNVFAEAP SAVLENLKAR CSVSYNKIKT FNEVKFNYSM PANCYHILVQ DCSSELKFLV
MMKSAGEATN LKAINIKIGS HEIDMHPVNG QVKLLVDGAE SPTANISLIS AGASLWIHNE
NQGFALAAPG HGIDKLYFDG KTITIQVPLW MAGKTCGICG KYDAECEQEY RMPNGYLAKN
AVSFGHSWIL EEAPCRGACK LHRSFVKLEK TVQLAGVDSK CYSTEPVLRC AKGCSATKTT
PVTVGFHCLP ADSANSLTDK QMKYDQKSED MQDTVDAHTT CSCENEECST
