ID VIT5_CAEEL Reviewed; 1603 AA.
AC P06125;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Vitellogenin-5;
DE Flags: Precursor;
GN Name=vit-5; ORFNames=C04F6.1;
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 [GENOMIC DNA].
RX PubMed=3855245; DOI=10.1093/nar/13.19.7129;
RA Spieth J., Denison K., Zucker E., Blumenthal T.;
RT "The nucleotide sequence of a nematode vitellogenin gene.";
RL Nucleic Acids Res. 13:7129-7138(1985).
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 1-24.
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26671266; DOI=10.1080/15548627.2015.1127464;
RA Seah N.E., de Magalhaes Filho C.D., Petrashen A.P., Henderson H.R.,
RA Laguer J., Gonzalez J., Dillin A., Hansen M., Lapierre L.R.;
RT "Autophagy-mediated longevity is modulated by lipoprotein biogenesis.";
RL Autophagy 12:261-272(2016).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development (Probable). Together with other
CC vitellogenins, may play a role in modulating life-span, acting via
CC induction of autophagy and lysosomal lipolysis (PubMed:26671266).
CC {ECO:0000269|PubMed:26671266, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26671266}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestine of adult hermaphrodites.
CC {ECO:0000305|PubMed:26671266}.
CC -!- PTM: Vitellogenin 5 undergoes little if any processing before being
CC packaged into yolk platelets. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous RNAi-mediated knockdown of
CC vitellogenins vit-1, vit-2, vit-3, vit-4 and vit-5 increases life span,
CC causes accumulation of neutral lipid and an increase in lgg-1 foci in
CC the proximal intestine; however, does not affect fertility or
CC pharyngeal pumping rates (PubMed:26671266). Expression of transcription
CC factors pha-4 and daf-16 are increased (PubMed:26671266).
CC {ECO:0000269|PubMed:26671266}.
CC -!- CAUTION: High sequence similarity with other vitellogenin genes means
CC that assigning functions to individual proteins is difficult; authors
CC sometimes refer to VITs or vitellogenins.
CC {ECO:0000305|PubMed:26671266}.
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DR EMBL; X03044; CAA26849.1; -; Genomic_DNA.
DR EMBL; FO080344; CCD63027.1; -; Genomic_DNA.
DR EMBL; X02755; CAA26532.1; -; Genomic_DNA.
DR PIR; A03334; VJKW5.
DR PIR; F89497; F89497.
DR RefSeq; NP_508589.1; NM_076188.6.
DR AlphaFoldDB; P06125; -.
DR SMR; P06125; -.
DR BioGRID; 45570; 23.
DR DIP; DIP-25459N; -.
DR IntAct; P06125; 1.
DR STRING; 6239.C04F6.1.1; -.
DR iPTMnet; P06125; -.
DR EPD; P06125; -.
DR PaxDb; 6239-C04F6-1; -.
DR PeptideAtlas; P06125; -.
DR EnsemblMetazoa; C04F6.1.1; C04F6.1.1; WBGene00006929.
DR GeneID; 180630; -.
DR KEGG; cel:CELE_C04F6.1; -.
DR UCSC; C04F6.1.1; c. elegans.
DR AGR; WB:WBGene00006929; -.
DR WormBase; C04F6.1; CE03921; WBGene00006929; vit-5.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00530000064273; -.
DR HOGENOM; CLU_003821_0_0_1; -.
DR InParanoid; P06125; -.
DR OMA; DMRPANG; -.
DR OrthoDB; 3076121at2759; -.
DR PhylomeDB; P06125; -.
DR SignaLink; P06125; -.
DR PRO; PR:P06125; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006929; Expressed in adult organism and 1 other cell type or 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; 2.20.80.10; Lipovitellin-phosvitin complex, chain A, domain 4; 1.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 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 PANTHER; PTHR23345:SF8; VITELLOGENIN-3-RELATED; 1.
DR PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1.
DR Pfam; PF09172; Vit_open_b-sht; 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; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Reference proteome; Secreted; Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1603
FT /note="Vitellogenin-5"
FT /id="PRO_0000041536"
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 REGION 1492..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1308..1438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1330..1474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CONFLICT 45
FT /note="A -> R (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="L -> V (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..187
FT /note="EVAYT -> RSRLH (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..392
FT /note="TL -> SI (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="N -> H (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="F -> L (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 883..885
FT /note="RFW -> PLL (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1264..1269
FT /note="YMNMTI -> SHEHDH (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1281
FT /note="V -> A (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="D -> H (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1476..1478
FT /note="VEN -> FEF (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1517
FT /note="K -> E (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1565..1569
FT /note="SKNAR -> RQERS (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1573..1576
FT /note="KEAR -> QGSS (in Ref. 1; CAA26849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1603 AA; 186439 MW; 00904A8F18BFB1B9 CRC64;
MKSIIIASLV ALAIAASPAL DRTFSPKSEY VYKFDGLLLS GLPTASSDAS QTLISCRTRL
QAVDDRYIHL QLTDIQYSAS HIPQSEQWPK IESLEQRELS DEFKELLELP FRAQIRNGLI
SEIQFSSEDA EWSKNAKRSI LNLFSLRKSA PVDEMNQDQK DMESDKDSLF FNVHEKTMEG
DCEVAYTIVQ EGEKTIYTKS VNFDKCITRP ETAYGLRFGS ECKECEKEGQ FVKPQTVYTY
TFKNEKLQES EVHSVYTLNV NGQEVVKSET RAKVTFVEES KINREIKKVS GPKEEIVYSM
ENEKLIEQFY QQGDKAEVNP FKAIEMEQKV EQLQEIFRQI QEHEQNTPET VHLIARAVRM
FRMCTIEELK KVHTTIYTKA EKKVQLVIET TLAVAGTKNT IQHLIHHFEK KSITPLRAAE
LLKSVQETLY PSEHIADLLI QLAQSPLSEK YEPLRQSAWL AAGSVVRGFA SKTQDLPLIR
PASRQTKEKY VRVFMQHFRN ADSTYEKVLA LKTLGNAGID LSVYELVQII QDPRQPLSIR
TEAVDALRLL KDVMPRKIQK VLLPVYKNRQ NKPELRMAAL WRMMHTIPEE PVLAHIVSQM
ENESNQHVAA FTYNVLRQFY KSTNPCYQQL AVRCSKILLF TRYQPQEQML STYSQLPLFN
SEWLSGVQFD FATIFEKNAF LPKEVQASFE TVFGGNWNKY FAQVGFSQQN FEQVILKTLE
KLSLYGKQSD ELRSRRVQSG IQMLQEIVKK MNIRPRVQQT DSQNAHAVFY LRYKEMDYIV
LPIDMETIDT LVEKYVRNGE FDIKSLLTFL TNDSKFELHR ALFFYEAERR IPTTIGMPLT
ISGKMPTILS INGKVSIELE KLGARLVLDI VPTVATTHVT EMRFWYPVIE QGVKSLQSAR
LHTPLRFEST VELKKNTLEI THKFVVPENK KTTVSVHTRP VAFIRVPKNQ DSEYVEAEEK
TISHSQYQMS TEEIDRQYET FGLRINAQGN VLSQWTLPMV LMTEQDFEYT LENKNRPVEF
TARVTIGNLE KTDLSEIKFD KIFEKEFDLE NNESENRRQY FHKMIREIQS EQGFKNLITL
KLEAPQQMYW NTELRTVCDK WIRMCKVEMD ARRSPMEHEN KEWTLRTELL AARPQMPSSL
RQLREQPHRE VQLAFNAKWG SSKKSEITVN AQLEQSTEQK KFIRNIEREY KGIPEYELLI
KAARLNQVNV VSEYKLTPQS EYTFSRIFDL IKAYNFWTVS EKRVQNENRR VVLQLSVEPL
SRQYMNMTIQ TPEQEVELKN VRIPRVVLPT IARSAMFQQT WEKTGATCKV DQSEVSTFDN
VIYRAPLTTC YSLVAKDCSE QPRFAVLAKK INKNSEELLV KVVRREEEIV VKKSDDKFLV
KVDGKKVNPT ELEQYNIEIL GDNLIVIRLP QGEVRFDGYT VKTNMPSVAS QNQLCGLCGN
NDGERDNEFM TADNYETEDV EEFHRSYLLK NEECEVENDR ISEKKNYRNK WNREEKKSDY
ESSSDYESNY DEKETEKELV KKTLIKEFSN RVCFSIEPVS ECRRGLESEK TSNKKIRFTC
MPRHSKNARR FLKEAREQTV AELVDFPVSF VESVKIPTAC VAY
//
