VIT4_CAEEL
ID VIT4_CAEEL Reviewed; 1603 AA.
AC P18947; Q9BPP3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Vitellogenin-4;
DE Flags: Precursor;
GN Name=vit-4; ORFNames=F59D8.2;
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-282.
RA Blumenthal T., Spieth J., Zucker E.;
RL Submitted (NOV-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
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 [4]
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 [5]
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.
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; FO081486; CCD71958.1; -; Genomic_DNA.
DR EMBL; M11498; AAA28163.1; -; Genomic_DNA.
DR EMBL; X02754; CAA26531.1; -; Genomic_DNA.
DR PIR; A43084; A43084.
DR RefSeq; NP_508612.1; NM_076211.5.
DR AlphaFoldDB; P18947; -.
DR SMR; P18947; -.
DR BioGRID; 45584; 16.
DR STRING; 6239.F59D8.2; -.
DR iPTMnet; P18947; -.
DR EPD; P18947; -.
DR PaxDb; P18947; -.
DR PeptideAtlas; P18947; -.
DR PRIDE; P18947; -.
DR EnsemblMetazoa; F59D8.2.1; F59D8.2.1; WBGene00006928.
DR GeneID; 180646; -.
DR KEGG; cel:CELE_F59D8.2; -.
DR UCSC; F59D8.2; c. elegans.
DR CTD; 180646; -.
DR WormBase; F59D8.2; CE26817; WBGene00006928; vit-4.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00530000064273; -.
DR HOGENOM; CLU_003821_0_0_1; -.
DR InParanoid; P18947; -.
DR OMA; GHCHHRV; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; P18947; -.
DR PRO; PR:P18947; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006928; Expressed in adult organism and 1 other tissue.
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-4"
FT /id="PRO_0000041535"
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"
FT CONFLICT 169
FT /note="L -> V (in Ref. 2; AAA28163)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..187
FT /note="EVAYT -> RSRLH (in Ref. 2; AAA28163)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="T -> S (in Ref. 2; AAA28163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1603 AA; 186309 MW; E303170325BC99BB CRC64;
MKSIIIASLV ALAIAASPAL DRTFSPKSEY VYKFDGLLLS GLPTTFSDAS QTLISCRTRL
QAVDDRYIHL QLIDIQYSAS HIPQSEQWPK IESLEQRELS DELKELLELP FRAQIRNGLV
SEIQFSSEDA EWSKNAKRSI LNLFSLRKSA PVDEMSQDQK DMESDKDSLF FNVHEKTMEG
DCEVAYTIVQ EGGKTIYTKS VNFDKCITRP ETAYGLRFGS ECKECEKEGQ FVQPQTVYTY
TFKNEKLQES EVNSIYTLNV NGQEVVKSET RAKVTFVEES KINREIKKVS GPKEEIVYSM
ENEKLIEQFY KQGDKAEVNP FKAIEIEQKV EQLEEIFRQI 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 DSEYVEAEEK
TISHSQYQMS TEEIDRQYET FGLRINAQGN VLSQWTLPMV LMTEQDFEFT LENKNRPVEF
TARVTIGNLE KTDLSEIKFD KIFEKEFDLE NNESENRRQY FHKMIREIQS EQGFKNLITL
KLEAPQQMYW NTELRTVCDK WIRMCKVEMD ARRSPIEHEN KEWTLRTELL AARPQMPSSL
RQLREQPHRE VQLALNAKWG SSKKSEITFN AQLEQSTEQK KFLRNIEREY KGIPEYELLI
KAARLNQVNV VSEYKLTPES EYTFSRIFDL IKAYNFWTVS EKRVQNEDRR VVLQLSVEPL
SRQYMNMTIQ TPEQEVELKN VRIPRVVLPT IARRAMFQQT WEKTGATCKV DQSEVSTFDN
VIYRAPLTTC YSLVAKDCSE QPRFAVLAKK INKNSEELLV KVVRREEEIV VKKSDDKFLV
KVDGKKVNPT ELEQYNIEIL GDNLIVIRLP HGEVRFDGYT VKTNMPSVAS QNQLCGLCGN
NDGERDNEFM TADNYETEDV EEFHRSYLLK NEECEVEKDR ISEKKNYKNK WNREEKKSDY
ESSSDYESNY DEKETEKELV KKTLIKEFSN RVCFSIEPVS ECRRGLESEK TSNKKIRFTC
MPRHSKNARR FLKEAREQTV ADLVDFPVSF VESVKIPTAC VAY
