ID C3ZJ91_BRAFL Unreviewed; 1042 AA.
AC C3ZJ91;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Vitellogenin domain-containing protein {ECO:0000259|PROSITE:PS51211};
GN ORFNames=BRAFLDRAFT_119256 {ECO:0000313|EMBL:EEN47422.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN47422.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN47422.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN47422.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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DR EMBL; GG666631; EEN47422.1; -; Genomic_DNA.
DR RefSeq; XP_002591411.1; XM_002591365.1.
DR AlphaFoldDB; C3ZJ91; -.
DR STRING; 7739.C3ZJ91; -.
DR eggNOG; KOG4338; Eukaryota.
DR InParanoid; C3ZJ91; -.
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; 2.20.50.20; Lipovitellin. Chain A, domain 3; 1.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 1.
DR InterPro; IPR000225; Armadillo.
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; IPR015817; Vitellinogen_open_b-sht_sub1.
DR InterPro; IPR001747; Vitellogenin_N.
DR PANTHER; PTHR23345:SF15; VITELLOGENIN-1-RELATED; 1.
DR PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1.
DR Pfam; PF09172; Vit_open_b-sht; 1.
DR Pfam; PF01347; Vitellogenin_N; 2.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Storage protein {ECO:0000256|ARBA:ARBA00022761}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1042
FT /note="Vitellogenin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002934882"
FT DOMAIN 28..826
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT REPEAT 662..692
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 90..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 117997 MW; 183FCA1BC2EBFC1F CRC64;
MNKLLILLLG VCLTQATLRS EDLADKVFGQ GREYVYKYEG EVKSGIPQSS DRFSGMKIEC
EARLQFKTDT EVLMRLEKIR LKTLRGELES PEEKTLKKLM KKTSQETTFE KKHQDAFRQD
HFSSSPEEWE RSIKTSSSSS QERETPSFEK WEQQETIRKQ KEQRTSSEEA GRPSSAQSGS
SSQRSSQSAS REESEEVPEQ QLAELRRQLE KAVRVTYEQG QVVSIQADRG EPQWSVNIKR
GICNMLQITR NPKNSELLDK DGRAESNVAF EKAPERLFRI MEQGVNGLCE TQLFRIMEQG
VNGLCETQYD IRDSQTQPGA QLVTRTKNLQ NCRQKPKEWL ARITGGKAIK DPTEEHFQSH
AQTRMRVVTD RSPAGKFLIQ RAESRDQHVF VPYSQQGGEV ITFAKQILEL VEAKTTISGP
KIPEPSQAEN KGNLIFVFEP RRPEGGSSAE SREESRETEE KVKQLCEGIA RGLREAITEE
TPKKFLQLVR ELRKMSQAQL KQFCIEKIPK IKQSSRETSQ EKEEAEARKL IIDAVSMVGT
EEALKAVAEL LQEEKIAAGD AQSLIGGLSV SITTCTPSAT NIMLEIAKSK QAQQDKNLRK
VAWLAFGTMV HKLTQTHPQQ SPEIVQLKKE YANQLLHGVQ QDKAPEEQMM CIKAIGNAGL
EDSVDRLVQI INSKTTPTEI RLQAIYALRR IAKKLPHKTR NILFPVFKNP ENPVEERAAA
FVVMMDSEPQ TSFLELLAQS TQRETSNQVG RFVYTTLRSC AASRLTRDQR MRRTCEKALR
LCRPFNLGMQ YSETSEWQAM SEEMRVGASV KIQTIADKRS VLPRAATAKM NVQALGLSIN
FLEAGVRASG LQTMVDSLYR QYADNKSFMY HLKKKSQETS REYRDSASTE RQRTLRNIEV
EKIQSKLNIK TRVPEDPKGQ IYLKVGGNEL YYHQFRSALL EKFVSEDSLS IGDIEKQLQE
GVKTSWTKAS LLADITQRTP TSLGLPLKLD LKAVAVTRSD IGGKVTVAPR LFREDRPKEL
QAISDVNAEV TSTHSTAMRI TS
//
