VIT6_OSCTI
ID VIT6_OSCTI Reviewed; 1648 AA.
AC Q94637;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Vitellogenin-6;
DE Short=OTI-VIT-6;
DE Contains:
DE RecName: Full=VT3;
DE Contains:
DE RecName: Full=VT2;
DE Flags: Precursor;
GN Name=vit-6;
OS Oscheius tipulae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Rhabditinae;
OC Oscheius.
OX NCBI_TaxID=141969;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CEW1;
RX PubMed=8676742; DOI=10.1093/oxfordjournals.molbev.a025628;
RA Winter C.E., Penha C., Blumenthal T.;
RT "Comparison of a vitellogenin gene between two distantly related rhabditid
RT nematode species.";
RL Mol. Biol. Evol. 13:674-684(1996).
RN [2]
RP SEQUENCE REVISION TO 244 AND 320-357.
RA Winter C.E.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 16-18, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP PROTEOLYTIC PROCESSING, AND GLYCOSYLATION.
RX PubMed=23308227; DOI=10.1371/journal.pone.0053460;
RA Almenara D.P., de Moura J.P., Scarabotto C.P., Zingali R.B., Winter C.E.;
RT "The molecular and structural characterization of two vitellogenins from
RT the free-living nematode Oscheius tipulae.";
RL PLoS ONE 8:E53460-E53460(2013).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23308227}.
CC -!- DEVELOPMENTAL STAGE: VT2 is detected in mature oocytes and in embryos
CC with a small number of cells (at protein level).
CC {ECO:0000269|PubMed:23308227}.
CC -!- PTM: The precursor protein is probably further processed into vitellin
CC polypeptides VT2 and VT3. {ECO:0000269|PubMed:23308227}.
CC -!- PTM: Both VT2 and VT3 polypeptides seem to be N-glycosylated.
CC {ECO:0000269|PubMed:23308227}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U35449; AAB49749.2; -; Genomic_DNA.
DR AlphaFoldDB; Q94637; -.
DR SMR; Q94637; -.
DR PRIDE; Q94637; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.30.230.10; -; 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 Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Repeat; Secreted; Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:23308227"
FT CHAIN 16..1648
FT /note="Vitellogenin-6"
FT /id="PRO_0000041538"
FT CHAIN 16..740
FT /note="VT3"
FT /evidence="ECO:0000305"
FT /id="PRO_5001030786"
FT CHAIN 743..1648
FT /note="VT2"
FT /evidence="ECO:0000305"
FT /id="PRO_5001030787"
FT DOMAIN 26..691
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1346..1514
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1070..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 741..742
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..203
FT /evidence="ECO:0000250"
FT DISULFID 219..222
FT /evidence="ECO:0000250"
FT DISULFID 1348..1477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1370..1513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1648 AA; 191052 MW; 82F1ED71588F05A7 CRC64;
MRFAVLLALF GLALAARQSS VSEQYYRSGR EYRYQFNGHL SAGLPIPGEE NSATRIQSLI
RIQPENGDFM RLQMTKTRFA TSEEDRVLSF ENMNEVPVSE KVEKVLSLPI RFSYRHGMVG
EIEFSTEEQT WSSNIKKAVV NMLQVNLVKK GMSEKNEYET EHDNDFFLSN ERTLEGECEV
AYTKIEKSEK EQQWTKSINF EKCSLRPEIV YGRRYAEECN ECRERDEKFS STVFFYNITG
TPEEFLINSV ELQSKHMFAP VTEQKQLITA RITNRLELVY SGEQKEQIEA VRNSDKKENL
LYNPEHEIAE EKFAQTGDEK YLRRIPNYVD QGEIIRQQLN RLSKQTEQIE LESNHVHARL
VKSLRFATED NLSSIRSLVS QKSEVVQSLY WDALAIAGTK VTVSHLLEKI NNKEISPMKA
SQLMKILAEV RIPSEQIAQE LHRFCESDIV SRSAVLRQSC WLSYGSVLNG VCGQTKNVYG
SEITETRKQC TRQMKEKYIR ELIEKMNQAE SRYEKVLFVK AIANAGIDTS VVELEKIIRN
QEVEKTVRMQ AIDALRRLRL SMPKKIQNVL MPVYRNHKET PGIRISALHM IMQTQPTSGV
LDMIVRGLEK ERSQQVRVYT WSTLKTLSES ENPAEKEIRR RVSQSLASIP VEEQKYLESK
HKTFNWFNMQ SGATLNWATI FSNDSVLPKE ITASLETVFG GEWNKYLAQI GLYQNNLDSV
LSKLLQKVEE TGLEQLVVRG KRSSSFFRPA EMLRSLVESL RISHRQVPAM SPIAMIYLRY
KDQDYAFLPI DIDTLPEMIR RVARDGQLDL SEIEKVLTQA ARFTVAGSAF FHETVRKVPS
ALGMPQVMTS KMPTVAQMNG EVKFDLEPLN SDKFTGLRLR VKAEPHVAST HVCKLELFTP
IGGQGIKLLH GGRIQAPIDS EIEINWEKKL IVKATIKSPE QKRHIAHFMT RPVLFSREVT
MDKQMRQYPE PREKTIQLRE NRFPIHAFER QYFEQTGLKM TVSGHYRRPF TTAFTLGESI
MMSSSSLPRM LSLKEVVAYM SFSGFEETEM DEPRLLNRFY EKETELFETE KNVEYEQEDK
EPKSSQLQSQ IRKVKSEGKA YKHRVHMKIH TVGGPKTQEA ECEIRALCDE RVRFCRLNLD
ASRSPIQGES RQWQLKSSAE WLYPEVPSTM KKMLESRREW NAMWTGKWGS EKQNEVTIRV
QGEQSSEQKF WMKKAEREQS PLTSGGQASR AAQLNQYNIH ATYEVTPETE FWMENVYSMF
KTYYFFSAEV QPKQNKENRI QCQITLEPFT RQLFNVTVMS PKEKLVLELE NQQTPFRLPA
VNIGREFGRV QSVRHVVKAV ERQTRPECIV KSKEIQTFDE VFYRTPVMEC FSVLAKDCSE
NPDFAVLMRK VSKRGEEKMW KVISRENVIE LEKKSEEMSV RVNGKEISED KWEDFGISQR
GEEKFFIDAE KVTVEFDGFQ AKIQMSSLYK NKQCGLCGHY DGEKTNEFRR ADNEETDDIE
EFSRSYLSKD DECEVDEQEM TNKRNYKVLR EETSSSEEIS ESLIELYSEA FQSREAHHRL
GRREDRQVCF SQQAWNKCLK SKDNKTETKN VHFKCLTETT RSPRISSVFS QADISENLSD
VEGLPSLAEP SPHSRFLPCV IPSLSLSQ
