ID A0A226DXB2_FOLCA Unreviewed; 2079 AA.
AC A0A226DXB2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Vitellogenin-2 {ECO:0000313|EMBL:OXA50115.1};
GN ORFNames=Fcan01_14814 {ECO:0000313|EMBL:OXA50115.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA50115.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA50115.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA50115.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA50115.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA50115.1}.
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DR EMBL; LNIX01000009; OXA50115.1; -; Genomic_DNA.
DR STRING; 158441.A0A226DXB2; -.
DR OMA; ISTAYQY; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
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:SF15; VITELLOGENIN-1-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 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..964
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 1716..1915
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT REGION 277..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1927..1980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2079 AA; 232846 MW; A819DE30064038F0 CRC64;
MEHCISLSVR LELAMKTLNC AFLHWTGVGG GGGIGRLLRW GPYKKTSTGV TIHSQFTKFP
VCEKFLQLFA NMRVAVGLLA LAVLAGFVST EYAWTPGTEY VYSVRGRMMT GVSVINNQHA
GFEIQYKLYV KLLSQGKLAI KPENVELVET EEELDPREGD IEKGKQIQLI AEMKKALESP
ILVTLKQGVP SSIQVEKDLP VALMNVKRAQ VSQVIVDTVG AKIVIEGNIH RRTNSVRQAD
KNDDSGFFFE TLEKTVHGEC ETYYTVSQTG PYQSVFQHEA QDQPAGQQSS ESSSASKERP
SLRRADYQKL SQKYNSASLE SSSEEQQREM PWPKAFNQFC REQDQIYEIY KVINFTACQN
KPVLAFFSPV ELLKCRPGDN SCGSIWNRAL VSRILACGSS RRDFNILQIN QEEQFNFGLQ
DEQRIVAVGV QNITIEKISH GSSVHYSLSQ PQTIDLTYEF SRKEQRQQIN GRTPQSWNLQ
SRTPHSTHGK QSSSSSSEEQ VRSSSNRYPR QASQEYSQGH QSYHGSQYNK LPFPTLKDAP
LRPLLISPLT IPQMQERAVE LVLESALDIH DESRSIAEHE TLSKLTVTAK VLRFLSQDEI
LNVYNNLTQK QSSSSDKQEE LQQKTRKNFI LDAMCQAGTN PAITAVMKLI KQQKVTGEKA
AQLISTFALY IRHPTPELLK EIFEFLKSSV VQQDQQMKTT TILAFSVLLN QACIKYNRYN
VALYGEFCQV KDTTEYVQHF EKKLNETLNQ SGNHWTHVYI TALGNIGHPR IVKVVQMILD
DSNDPIEKSK AIFALKNVVV SKEAEQTSSD DSIEVVDRVA KVVIDDEYVE KKVLPILVSV
AFDKSEHPMV RMAAIQMLIY SPQADVAIWQ QLAISTWSEI SQEVHSFVYS TIKNLAQLHT
ILRPAHLNMV RNANAVLSLT KDFDDGLLKS RNIFSSGYVG DLNSGYFQQL TYYGARDSII
PSSLYYRNYL QFGTGAFGTN PIEFSLQART VSQIAEVVAD QLDNSSSSEE SGEKNPVIQE
LKSLLGIEKR EMDETAHGSM FLNIRNEVQR IVEINVKDLQ KQWKSQAIYA LASLRRGVDI
NYQKVAQLVH HTMEMPTIFG VPLLYKQRLP VMLSVVGKTK LQGGSSDGQL QAQLEVVLAG
KLTQKVAVKV PFLGKKYESG YQRHIVVDAP FRATVRIASK KPITVAVTPT KDINGPAAGT
IELVTYHQRP YTAIITDELY PTVHHRGGQM NVINSEEKSP VYTNEETYGK QILGLAFRVK
EQSDYREEQE TLTGWGRFIR RFHSPSCFLN LGVYGPKTIK FAERQILLDV GESKTKTFVV
ALAAKRGSSS LDGSFHTDSS SSSSSSSSSS ESADNSDSSD STSSQSGDKQ SRLRFIRGSS
SSSSSSETNE SSDSNENSKE VYSKARVIAL AVFGKVRAIP PVEQTSSIVN NLDQQIESKI
QYLLQIAVRK NKILIQAASA DAANEVAKAL PTDSESLQVL RDALVKGPNA KEQQDGCMEL
YAKYTAPQHA NQQILTVLRK TLLEKDLKVQ VQGQYKFGET CKDSDLKYKI ELDGQLERNA
EQTKYAGKES DEAQACEEDE KKGFTVSDTC LVVANSQAAA LNKWRLTFKW NKDMPNELKN
VTEQVEDFIK YLYYPYVSHS YYPEPQETSP DRTIIAEFEH SPDTLFWNLV VRKPTSVLAF
NDVRSGPVVQ AVLPLTATQT LPQNLMDYFA GNDSQPTCQF EQRYLSTFDG VTARYKPEVA
KGCYHLLTAD CSGKHTMAVS AKNLGTQDIK LKVVLSGAKI TIGKQQSGQG IVRLIKATQT
RALTVLVNGQ EVQLPYTVRK ENQKQKSNDF VARIKDMSNG GVQIETEEQD IGFDGERIVI
YGSEVYRNVT CGMCGDFDGE KVADFRSPQD FPLSSATLLY ASYAYNSKSD SETCHVEPAV
RQLIKQEESI GQQGHSRSYL SRSARQGSVY GKKSNKNQAS SSSSSSESSE QYSKSSRGQQ
KKSPKSPKVH QQIRMLESKN KICFSEKKVE ACPYGYQPKG GKTISVQFSC YKKNSSVANE
IKQQLKSRFV DLSQSQYRSY AERQTLDVHE KPNQCVRSY
//
