ID   VITA2_XENLA             Reviewed;        1807 AA.
AC   P18709; Q91895;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Vitellogenin-A2;
DE            Short=VTG A2;
DE   Contains:
DE     RecName: Full=Lipovitellin I;
DE   Contains:
DE     RecName: Full=Lipovitellin II;
DE   Contains:
DE     RecName: Full=Phosvitin;
DE   Flags: Precursor;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 16-28.
RX   PubMed=3601655; DOI=10.1093/nar/15.12.4737;
RA   Gerber-Huber S., Nardelli D., Haefliger J.-A., Cooper D.N., Givel F.,
RA   Germond J.-E., Engel J., Green N.M., Wahli W.;
RT   "Precursor-product relationship between vitellogenin and the yolk proteins
RT   as derived from the complete sequence of a Xenopus vitellogenin gene.";
RL   Nucleic Acids Res. 15:4737-4760(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-25.
RX   PubMed=8185593; DOI=10.1006/bbrc.1994.1607;
RA   Montorzi M., Falchuk K.H., Vallee B.L.;
RT   "Xenopus laevis vitellogenin is a zinc protein.";
RL   Biochem. Biophys. Res. Commun. 200:1407-1413(1994).
RN   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 1291-1302.
RX   PubMed=2352275; DOI=10.1016/s0022-2836(05)80203-7;
RA   Wallace R.A., Hoch K.L., Carnevali O.;
RT   "Placement of small lipovitellin subunits within the vitellogenin precursor
RT   in Xenopus laevis.";
RL   J. Mol. Biol. 213:407-409(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RX   PubMed=6504705; DOI=10.1093/nar/12.22.8611;
RA   Walker P., Germond J.-E., Brown-Luedi M., Givel F., Wahli W.;
RT   "Sequence homologies in the region preceding the transcription initiation
RT   site of the liver estrogen-responsive vitellogenin and apo-VLDLII genes.";
RL   Nucleic Acids Res. 12:8611-8626(1984).
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.
CC   -!- INDUCTION: By steroids (estrogen).
CC   -!- MISCELLANEOUS: The serine-rich portion of vitellogenin encodes
CC       phosvitin (or two phosvettes). It is assumed to be phosphorylated to a
CC       level of about 80%.
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DR   EMBL; Y00354; CAA68433.1; -; Genomic_DNA.
DR   EMBL; M18061; AAA49982.1; -; Genomic_DNA.
DR   EMBL; X00205; CAA25028.1; -; Genomic_DNA.
DR   PIR; S03124; S03124.
DR   RefSeq; NP_001152753.1; NM_001159281.1.
DR   AlphaFoldDB; P18709; -.
DR   SMR; P18709; -.
DR   BioGRID; 674349; 1.
DR   PRIDE; P18709; -.
DR   GeneID; 100037071; -.
DR   KEGG; xla:100037071; -.
DR   CTD; 100037071; -.
DR   Xenbase; XB-GENE-5791437; vtga2.L.
DR   OMA; FIMNSAN; -.
DR   OrthoDB; 36651at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 100037071; Expressed in liver and 8 other tissues.
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; -; 1.
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:0000269|PubMed:3601655,
FT                   ECO:0000269|PubMed:8185593"
FT   CHAIN           16..1807
FT                   /note="Vitellogenin-A2"
FT                   /id="PRO_0000041585"
FT   CHAIN           16..?
FT                   /note="Lipovitellin I"
FT                   /id="PRO_0000041586"
FT   CHAIN           ?..1290
FT                   /note="Phosvitin"
FT                   /id="PRO_0000041587"
FT   CHAIN           1291..?
FT                   /note="Lipovitellin II"
FT                   /id="PRO_0000041588"
FT   DOMAIN          24..664
FT                   /note="Vitellogenin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT   DOMAIN          1536..1714
FT                   /note="VWFD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   REGION          953..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1122..1162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1199..1233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1234..1248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1277..1306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        1094
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1538..1677
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1561..1713
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   VARIANT         662
FT                   /note="V -> I"
FT   VARIANT         958
FT                   /note="A -> T"
FT   VARIANT         1572
FT                   /note="E -> K"
FT   CONFLICT        72
FT                   /note="I -> V (in Ref. 5; CAA25028)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1807 AA;  201545 MW;  D109BBF568147742 CRC64;
     MKGIVLALLL ALAGSERTHI EPVFSESKIS VYNYEAVILN GFPESGLSRA GIKINCKVEI
     SAYAQRSYFL KIQSPEIKEY NGVWPKDPFT RSSKLTQALA EQLTKPARFE YSNGRVGDIF
     VADDVSDTVA NIYRGILNLL QVTIKKSQDV YDLQESSVGG ICHTRYVIQE DKRGDQIRII
     KSTDFNNCQD KVSKTIGLEL AEFCHSCKQL NRVIQGAATY TYKLKGRDQG TVIMEVTARQ
     VLQVTPFAER HGAATMESRQ VLAWVGSKSG QLTPPQIQLK NRGNLHYQFA SELHQMPIHL
     MKTKSPEAQA VEVLQHLVQD TQQHIREDAP AKFLQLVQLL RASNFENLQA LWKQFAQRTQ
     YRRCLLDALP MAGTVDCLKF IKQLIHNEEL TTQEAAVLIT FAMRSARPGQ RNFQISADLV
     QDSKVQKYST VHKAAILAYG TMVRRYCDQL SSCPEHALEP LHELAAEAAN KGHYEDIALA
     LKALGNAGQP ESIKRIQKFL PGFSSSADQL PVRIQTDAVM ALRNIAKEDP RKVQEILLQI
     FMDRDVRTEV RMMACLALFE TRPGLATVTA IANVAARESK TNLQLASFTF SQMKALSKSS
     VPHLEPLAAA CSVALKILNP SLDNLGYRYS KVMRVDTFKY NLMAGAAAKV FIMNSANTMF
     PVFILAKFRE YTSLVENDDI EIGIRGEGIE EFLRKQNIQF ANFPMRKKIS QIVKSLLGFK
     GLPSQVPLIS GYIKLFGQEI AFTELNKEVI QNTIQALNQP AERHTMIRNV LNKLLNGVVG
     QYARRWMTWE YRHIIPTTVG LPAELSLYQS AIVHAAVNSD VKVKPTPSGD FSAAQLLESQ
     IQLNGEVKPS VLVHTVATMG INSPLFQAGI EFHGKVHAHL PAKFTAFLDM KDRNFKIETP
     PFQQENHLVE IRAQTFAFTR NIADLDSARK TLVVPRNNEQ NILKKHFETT GRTSAEGASM
     MEDSSEMGPK KYSAEPGHHQ YAPNINSYDA CTKFSKAGVH LCIQCKTHNA ASRRNTIFYQ
     AVGEHDFKLT MKPAHTEGAI EKLQLEITAG PKAASKIMGL VEVEGTEGEP MDETAVTKRL
     KMILGIDESR KDTNETALYR SKQKKKNKIH NRRLDAEVVE ARKQQSSLSS SSSSSSSSSS
     SSSSSSSSSS SSSPSSSSSS SYSKRSKRRE HNPHHQRESS SSSSQEQNKK RNLQENRKHG
     QKGMSSSSSS SSSSSSSSSS SSSSSSSSSS SSEENRPHKN RQHDNKQAKM QSNQHQQKKN
     KFSESSSSSS SSSSSEMWNK KKHHRNFYDL NFRRTARTKG TEHRGSRLSS SSESSSSSSE
     SAYRHKAKFL GDKEPPVLVV TFKAVRNDNT KQGYQMVVYQ EYHSSKQQIQ AYVMDISKTR
     WAACFDAVVV NPHEAQASLK WGQNCQDYKI NMKAETGNFG NQPALRVTAN WPKIPSKWKS
     TGKVVGEYVP GAMYMMGFQG EYKRNSQRQV KLVFALSSPR TCDVVIRIPR LTVYYRALRL
     PVPIPVGHHA KENVLQTPTW NIFAEAPKLI MDSIQGECKV AQDQITTFNG VDLASALPEN
     CYNVLAQDCS PEMKFMVLMR NSKESPNHKD INVKLGEYDI DMYYSADAFK MKINNLEVSE
     EHLPYKSFNY PTVEIKKKGN GVSLSASEYG IDSLDYDGLT FKFRPTIWMK GKTCGICGHN
     DDESEKELQM PDGSVAKDQM RFIHSWILPA ESCSEGCNLK HTLVKLEKAI ATDGAKAKCY
     SVQPVLRCAK GCSPVKTVEV STGFHCLPSD VSLDLPEGQI RLEKSEDFSE KVEAHTACSC
     ETSPCAA