VIT2_CAEEL
ID VIT2_CAEEL Reviewed; 1613 AA.
AC P05690;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 5.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Vitellogenin-2;
DE Flags: Precursor;
GN Name=vit-2; ORFNames=C42D8.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1904098; DOI=10.1007/bf02101283;
RA Spieth J., Nettleton M., Zucker-Aprison E., Lea K., Blumenthal T.;
RT "Vitellogenin motifs conserved in nematodes and vertebrates.";
RL J. Mol. Evol. 32:429-438(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
RX PubMed=3841791; DOI=10.1128/mcb.5.10.2495-2501.1985;
RA Spieth J., Blumenthal T.;
RT "The Caenorhabditis elegans vitellogenin gene family includes a gene
RT encoding a distantly related protein.";
RL Mol. Cell. Biol. 5:2495-2501(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=4022780; DOI=10.1093/nar/13.14.5283;
RA Spieth J., Denison K., Kirtland S., Cane J., Blumenthal T.;
RT "The C. elegans vitellogenin genes: short sequence repeats in the promoter
RT regions and homology to the vertebrate genes.";
RL Nucleic Acids Res. 13:5283-5295(1985).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in Caenorhabditis only by 32 cells
CC building the intestine of adult hermaphroditic individuals; they are
CC cotranslationally secreted into the body cavity and subsequently taken
CC up by the gonad.
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DR EMBL; X56212; CAA39669.1; -; Genomic_DNA.
DR EMBL; FO080659; CCD65563.1; -; Genomic_DNA.
DR EMBL; M10105; AAA28162.1; -; Genomic_DNA.
DR EMBL; X02753; CAA26530.1; -; Genomic_DNA.
DR PIR; A43081; A43081.
DR PIR; F89528; F89528.
DR RefSeq; NP_508868.1; NM_076467.5.
DR AlphaFoldDB; P05690; -.
DR SMR; P05690; -.
DR BioGRID; 45716; 18.
DR DIP; DIP-27283N; -.
DR IntAct; P05690; 3.
DR STRING; 6239.C42D8.2a; -.
DR iPTMnet; P05690; -.
DR EPD; P05690; -.
DR PaxDb; P05690; -.
DR PeptideAtlas; P05690; -.
DR EnsemblMetazoa; C42D8.2.1; C42D8.2.1; WBGene00006926.
DR GeneID; 180781; -.
DR KEGG; cel:CELE_C42D8.2; -.
DR UCSC; C42D8.2a.1; c. elegans.
DR CTD; 180781; -.
DR WormBase; C42D8.2; CE06950; WBGene00006926; vit-2.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00530000064273; -.
DR HOGENOM; CLU_003821_0_0_1; -.
DR InParanoid; P05690; -.
DR OMA; EVENNMP; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; P05690; -.
DR SignaLink; P05690; -.
DR PRO; PR:P05690; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006926; Expressed in adult organism and 2 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031983; C:vesicle lumen; IDA:WormBase.
DR GO; GO:0042718; C:yolk granule; IDA:WormBase.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.20; -; 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; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF09172; DUF1943; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 2.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1613
FT /note="Vitellogenin-2"
FT /id="PRO_0000041533"
FT DOMAIN 24..687
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1308..1477
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1491..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT DISULFID 1310..1440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1332..1476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CONFLICT 656
FT /note="A -> V (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="L -> R (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="R -> C (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063..1068
FT /note="FNKMVK -> STRWST (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127
FT /note="L -> V (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1224
FT /note="Q -> H (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1302
FT /note="L -> F (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310
FT /note="C -> W (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1313..1314
FT /note="QK -> KR (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1426..1429
FT /note="QLPS -> KIPY (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1447..1451
FT /note="STNEF -> VHQRV (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1472
FT /note="K -> R (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1572
FT /note="L -> W (in Ref. 1; CAA39669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1613 AA; 187722 MW; CD89484814D516A8 CRC64;
MRSIIIASLV ALALASSPAF ERTFEPKTDY HYKFDGLVLS GLPSASSELS QSRISARARI
QAVDDRYIHL QLVNIRMAAS HLPESEQMPS LNSMEQRELS EEYKQMLELP LRAQLRNGLI
SELQFDKEDA EWSKNMKRAV VNMISFNPIA PRNEIEKIES SYDKEEQSEE NTSFFTNEKT
LEGDCQVAYT VIREQKKTII TKSINFDKCT ERSEIAYGLR YSSECPECEK DTELIRPQTV
YTYVLENEEL KESEVRSLYT VNVNGQEVMK TETRSKLVLE ENHSIKSHIK KVNGEKESII
YSSRWEQLVE DFFKNGDKAE FAPFEKFPLD KKMHLIKTIT EQIQEVENNM PETSHFLARL
VRIFRTTSTS QLKEIHETLY VKADKKIQSL MEHALAIAGT KNTIQHILVH MENEDILPLG
QILKTIQETP FPSQSIAEAL IKFAESRVAK NNLVVRQAAW LAAGSVVRGI VDYKNIRPLV
REDKRELKEK FLRVFMQQYK DAETTYEKIL ALKTIGNAGL DISVNQLNEI IVDKRQPLPV
RKEAIDALRL LKDTMPRKIQ KVLLPIYKNR QYEPEIRMLA LWRMMHTRPE ESLLVQVVSQ
MEKETNQQVA ALTHQMIRHF AMSTNPCYQR VAIVCSKVLS FTRYQPQEQM IASSYAQLPL
FLQNSFSGAQ FDFAAIFEKN SFLPKDLHAS LDAVFGGNWN KYFAQIGFSQ QHMDKYVQMA
LEKLESLEKE STTVVRGRRI QTGIKLLKEL AQKMNIRARP ATYTEKDAFA MVYLRYKDMD
YAFLPIDRQL VENLIEKFTS NGKVQFSEIR RLLNQELEFE THHAAYFYEA IRKFPTTLGL
PLTISGKIPT VISAEGQFSL ELEGTELRLT VEARPSVAAT HVYEMRMFTP LFEQGVKSVQ
SVRAYTPIKI QAVAGMKRNF EIVYKVVVPE NQKSIVSLTT RPVVFLRFPG FSKFEYIEAE
ERTVVVPQWQ QKTQEIEKVF NFLGLEVSTR GNILNQHTLE NWLLAEQDFE VSVENKNRPA
EFTARLTVGQ LEKTELSQIK YNKIFEKEFE LEQENTESRR EYFNKMVKNI QKEQGYKSVI
SLKLEAPRDY TMNTELTTVC DKQVRMCQWE VEIRRSPILE ETKEWTLRSQ LLVVRPEMPS
SLRQLRDQPH REVQLSLTST WGSQKKSEVT VNAQLQQSKE QKKYERNMDR QFNGMPEYEL
LIKAARLNQI NAVAEYKLTR ETEQVLARYF DLVKTYNYWT VSSRPENNEN DRVVVQLTVE
PMSRQYVNIT MQSPMERIEL KNVQVPRVYL PSIAQRSVKH QLTEASGSVC KVQKNQIRTF
DDVLYNTPLT TCYSLIAKDC SEEPTFAVLS KKTEKNSEEM IIKVIRGEQE IVAQLQNEEI
RVKVDGKKIQ SEDYSAYQIE RLGESAIVIE LPEGEVRFDG YTIKTQLPSY SRKNQLCGLC
GNNDDESTNE FYTSDNTETE DIEEFHRSYL LKNEECEAEE ERLSEKKNYR KYERDEEQSD
EYSSEETYDY EQENTKKSQK NQRSQKKSDL VEKTQIKEFS HRICFSVEPV AECRRGYEVE
QQQQRKIRFT CLQRHNRDAS RLLKESRQQP LQLDDYPVSF VESVKVPTAC VAY
