VIT3_CAEEL
ID VIT3_CAEEL Reviewed; 1603 AA.
AC Q9N4J2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Vitellogenin-3;
DE Flags: Precursor;
GN Name=vit-3; ORFNames=F59D8.1;
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 [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 [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1266, 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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1266, 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.
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DR EMBL; FO081486; CCD71957.1; -; Genomic_DNA.
DR RefSeq; NP_001294839.1; NM_001307910.1.
DR AlphaFoldDB; Q9N4J2; -.
DR SMR; Q9N4J2; -.
DR STRING; 6239.F59D8.1; -.
DR iPTMnet; Q9N4J2; -.
DR EPD; Q9N4J2; -.
DR PaxDb; Q9N4J2; -.
DR PeptideAtlas; Q9N4J2; -.
DR EnsemblMetazoa; F59D8.1.1; F59D8.1.1; WBGene00006927.
DR UCSC; F59D8.1; c. elegans.
DR WormBase; F59D8.1; CE20900; WBGene00006927; vit-3.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00530000064273; -.
DR HOGENOM; CLU_003821_0_0_1; -.
DR InParanoid; Q9N4J2; -.
DR OMA; AKECERE; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; Q9N4J2; -.
DR PRO; PR:Q9N4J2; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006927; Expressed in germ line (C elegans) and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
KW Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1603
FT /note="Vitellogenin-3"
FT /id="PRO_0000041534"
FT DOMAIN 24..685
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1306..1475
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CARBOHYD 1266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 1308..1438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1330..1474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1603 AA; 186530 MW; BCA0276E477D37DE CRC64;
MKSIIIASLV ALAIAASPAL DRTFSPKSEY VYKFDGLLLS GLPTTFSDAS QTLISCRTRL
QAVDDRYIHL QLIDIQYSAS HIPQSEQWPK IKSLEQRELS DELKELLELP FRAQIRNGLV
SEIQFSSEDA EWSKNAKRSI LNLFSLRKSA PVDEMSQDQK DMESDKDSLF FNVHEKTMEG
DCEVAYTIVQ EGEKTIYTKS VNFDKCITRP ETAYGLRFGS ECKECEKEGQ FVKPQTVYTY
TFKNEKLQES EVHSIYTLNV NGQEVVKSET RSKVTFVEES KINREIKKVS GPKEEIVYSM
ENEKLIEQFY QQGDQAEVNP FKAIEMEQKV EQLDEIFRQI QEHEQNTPET VHLIARAVRM
FRMCTIEELK KVHTTIYTKA EKKVQLVIET TLAVAGTKNT IQHLIHHFEK KSITPLRAAE
LLKSVQETLY PSEHIADLLI QLAQSPLSEK YEPLRQSAWL AAGSVVRGFA SKTQDLPLIR
PASRQTKEKY VRVFMQHFRN ADSTYEKVLA LKTLGNAGID LSVYELVQLI QDPRQPLSIR
TEAVDALRLL KDVMPRKIQK VLLPVYKNRQ NKPELRMAAL WRMMHTIPEE PVLAHIVSQM
ENESNQHVAA FTYNVLRQFS KSTNPCYQQL AVRCSKVLLF TRYQPQEQML STYSQLPLFN
SEWLSGVQFD FATIFEKNAF LPKEVQASFE TVFGGNWNKY FAQVGFSQQN FEQVILKTLE
KLSLYGKQSD ELRSRRVQSG IQMLQEIVKK MNIRPRVQQT DSQNAHAVFY LRYKEMDYIV
LPIDMETIDN VVEKYVRNGE FDIKSLLTFL TNDSKFELHR ALFFYEAERR IPTTIGMPLT
ISGKMPTILS INGKVSIELE KLGARLVLDI VPTVATTHVT EMRFWYPVIE QGVKSLQSAR
LHTPLRFEST VELKKNTLEI THKFVVPENK KTTVSVHTRP VAFIRVPKNQ DSEYVETEEK
TISHSQYQMS TEEIDRQYET FGLRINAQGN VLSQWTLPMV LMTEQDFEFT LENKNRPVEF
TARVTIGNLE KTDLSEIKFD KIFEKEFDLE NNESENRRQY FHKMIREIQS EQGFKNLITL
KLEAPQQMYW NTELRTVCDK WIRMCKVEMD ARRSPMEHEN KEWTLRTELL AARPQMPSSL
RQLREQPHRE VQLALNAKWG SSKKSEITFN AQLEQSTEQK KFLRNIEREY KGIPEYELLI
KAARLNQVNV VSEYKLTPES EYTFSRIFDL IKAYNFWTVS EKRVQNEDRR VVLQLSVEPL
SRQYMNMTIQ TPEQEVELKN VRIPRVVLPT IARRAMFQQT WEKTGATCKV GQSEVSTFDN
VIYRAPLTTC YSLVAKDCSE QPRFAVLAKK INKNSEELLV KVVRREEEIV VKKSDDKFLV
KVDEKKVNPT ELEQYNIEIL GDNLIVIRLP HGEVRFDGYT VKTNMPSVAS QNQLCGLCGN
NDGERDNEFM TADNYETEDV EEFHRSYLLK NEECEVENDR ISEKKNYRNK WNREEKKSDY
VSSSDYENNY DEKETENQLF KKTLIKEFSN RVCFSIEPVS ECRRGLESEK TSNEKIRFTC
MPRHSKNARR FLKEAREQTV ADLVDFPVSF VESVKIPTAC VAY
