ID Q19V51_DERVA Unreviewed; 1547 AA.
AC Q19V51;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Hemelipoglycoprotein {ECO:0000313|EMBL:ABD83654.1};
OS Dermacentor variabilis (American dog tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae; Dermacentor.
OX NCBI_TaxID=34621 {ECO:0000313|EMBL:ABD83654.1};
RN [1] {ECO:0000313|EMBL:ABD83654.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17368200; DOI=10.1016/j.ibmb.2007.01.004;
RA Thompson D.M., Khalil S.M., Jeffers L.A., Sonenshine D.E., Mitchell R.D.,
RA Osgood C.J., Michael Roe R.;
RT "Sequence and the developmental and tissue-specific regulation of the first
RT complete vitellogenin messenger RNA from ticks responsible for heme
RT sequestration.";
RL Insect Biochem. Mol. Biol. 37:363-374(2007).
RN [2] {ECO:0000313|EMBL:ABD83654.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18477238; DOI=10.1111/j.1365-2583.2008.00794.x;
RA Donohue K.V., Khalil S.M.S., Mitchell R.D., Sonenshine D.E., Roe R.M.;
RT "Molecular characterization of the major hemelipoglycoprotein in ixodid
RT ticks.";
RL Insect Mol. Biol. 17:197-208(2008).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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; DQ422963; ABD83654.1; -; mRNA.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.50.20; Lipovitellin. Chain A, domain 3; 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; IPR015817; Vitellinogen_open_b-sht_sub1.
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 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00557};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1547
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012113275"
FT DOMAIN 16..695
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 1362..1543
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DISULFID 201..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
SQ SEQUENCE 1547 AA; 177656 MW; 52A922FD51E68DC7 CRC64;
MRVLWLSLLV AAASGFEVGK EYVYKYKGTL HVANPEQPLQ ASGIAFRTKL IVQPKPDGTH
FKIVNFEADS FNSEQIDVAH HEFNYAANPN AAGDLEHPFA GKFDEGKLEE FSIGKNEQLW
VRNLKKGVLS LFQLDLVKGR HEHHDDKGYH VKEDGLHGPC DTLYIVHEEE HDYIEVTKVK
NLDKCDHEHY SFYGHQKEYQ CVKCEALATY PHTATSEVYY ELKGTAQHYV IGHAWGESAQ
LFKPHGEGKQ FHVLLNRTLD LEEEHDAATT DTTLVEAGEK EHSLAQEFPE THELENPEEL
KRPNRLVTHF GLLPNKENFV EGLKKLAHIE YGDEDIKEID NKESGSLLFL MLFHNFLTFS
YDDINDVYQN HVLTAPEDIK DSLRHVFLDL LAAAGLNPHV TYGLNLIKHN ELSVDDADRF
YNKLHLNLKE VSPALLREIA DSCKSDAVKS HREIWTSCKL AASAIAGGKG CKYAHDTHEE
DKGTCSPEIV SHFFNYSVTP KDVEHEPEYE STVFIRSAGN LGTHKALHYL ERFIYPKWHA
NEHKRMAALW ALKQAAKHHP ELARSIALPV FHNTSEPSEV RIAALLVVVV TNPDLYVLRH
IGLEVLSDPS DQVVAFVISA FRALANSKYP CHKEIAQHLR YVLPLWETNP RFRKPIDRAS
SHLLISSGYN PKYDYGGLTL VEMIKSHDSY LPRNLYIHMK DYVAGHSTDT VAFSFESWGL
DKVFNRLVGP QPGSTKNLWN FMGRRRFPRD ASAKERKEIE DALHIHDREY DPVYARMSLS
VFGKAVDSWD FDESILDAIK SKDAPEKTAE KLLGKALRKK TFYLSHDMTY LNPTELGVPV
FFDFKQAEFI YANREKIDVT HGDNAEIHLD VKRHYLYESR TQQMLGFAWT FSRSSLGSGY
DARTVISWPL DLKVTLAPLE GKLSLNRPLH LPWNAINHHF HPFTFNMPYD LTQDHANAIT
EITANQKPLY RQDELLEFDR RYFGDVFGVA MNVKGHLIKR GLHSGLDEFY HQMTLRERLY
YITINPHWHP RNVKLYFEPA GDAPTKEMDI DIAYKFLEPD DERHSHFKVH DQIGDDTEVP
STHVLNIDVN FKGDAKERKV ATEFRYSFNH DLFNHKLQFF YDRTPFRSND QEGTKICLEA
SAKFPKPDWS RVKNLATFYQ GKHIDANLDI HYGSSCEGQS SISIHGQYTH TDKDEEQLVN
AAAGKPITGN LRYNGLHRMA LQCNAGREHG IPFNYYCMKF LRHSSRLAKL TADVEWKNYK
PLLNKLLPLH TKYHALRPEH GGFFGIIRSH FTGENGKLHL VSQVPWWDLK DKPHTDIVIT
TEDGQHFKHW NVPTFSHMLE PRAFSSLGYS NIAEYAKQYR HRHCDLQKLS LRTFDGSLVQ
LPETDCYKVV TRDCSPNKRF LVMARSTNNP SLTKALKVFI HTTKLEILPV TEDSGLIVRV
DGNKVDVVPE RPYSHTDHDV ELFEVRTREK WFEVTSKSYG IYLTFNGNLL FIQTAPFYRG
KLCGLCGDYN LDRNHELSGP DGHLYNSTLE FAKSYVVPSP DCHPPTH
//
