ID A0A085NQ85_9BILA Unreviewed; 1748 AA.
AC A0A085NQ85;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=von Willebrand factor type D domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M514_05347 {ECO:0000313|EMBL:KFD71631.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD71631.1};
RN [1] {ECO:0000313|EMBL:KFD71631.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD71631.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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; KL367481; KFD71631.1; -; Genomic_DNA.
DR Proteomes; UP000030758; Unassembled WGS sequence.
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 Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00557};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Storage protein {ECO:0000256|ARBA:ARBA00022761}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1748
FT /note="von Willebrand factor type D domain protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001796125"
FT DOMAIN 42..767
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 1396..1579
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT REGION 533..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 256..259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
SQ SEQUENCE 1748 AA; 203516 MW; 64B963FC036EC832 CRC64;
MRLKVVVLTL LTVALYAAGR HQQRLKLLRD TVNYQNVRET YFRVNQKYKF KYDGQVKIGV
PDHSNQNSAS RFRADVTLVK RSDEHFIIRM NNIRVGKQLA NMEDQDEIAP LEQFEPAEIK
QSDLRTLELP VEFTYAEGQV QDLVFQQDDE EWSENLKRGV INLFQIKLQS TDRTSMEEEQ
AALNRIDTES KTDVGTAYRT REKTVEGECD TMYTVSAIDD NDSEQGSRML VTKAIDMDSC
RRRPEVWRNF QFISSCPRCQ RLPGSGERSI ESSTTIRYQI RGKRDKFLIE RAELCNDHVI
AQQNADESAV VVKIRATLKL VSSQESNEAS SEMSNFPATG QRVSDLVYST RDDEDFDRFY
AEGDQHYRDR LFSQWQQGQD KSAALAEMIM KMMRHMKDTA DEKANRYFYK AVQLMRHMSE
SEIRSTNEYY FGRQQSGPLT PEERERARNI MPNLLAQAGT LNSFRQLADK IENGEIDPLK
AAVVITTMMN APRVSKEIIT EMMRLEKSQT FQRNEQLKRA ILLTAGSMMR TMCAPQRQRS
QQRQQSQNRD DMRTDNTNEQ RCNSEIKQRF VRMIADRWAA NDRWEDKVLL IRTLGNAGLD
VSISELESII RNQDRRNSAA IRLEAILALR HIKDSLPQKT KNILLSAAAN RMESSAVRMA
AIQLLLQQNP DRMTIDQIGV IINHDPNRRV ASFAYRLIRR LADSDQPCYE ENKLKLQTVA
KSVRRRNLQL PHSDMIFESL YDREKKAGFD FFIMPMYDMD DMVPKFMRAG INMVERGERN
RNLLALEIGT SSLSNVISEL LPSIEQNRQG GNTEIKMKLR RMAEQTRRNR NRDSRQQQQT
RAWMSMKFRN QDIMLLTLNE NRLKQLMQEN RGMESLLLLI AKMATTRQGS ISIDEATLLR
ETIVKIPTAI GSQLSIRRKA PATFSAHGQA SIERNMPIEA NIKARISSTI SMVTDVRSTT
PISTNGIYLI KNIKATVPVD MTISIDHKQE DEQLKIQMRN PEAYKDLIKL ESRPVIYYKR
SQNPLAEGEE KTVVAERNVR MESFKRCIRG PLFGSEICVR GVITTPMCNH NKLLHYQAPW
FGPNKVVMSV NADGRNSKQA SDQQRLHNDN QPRRVTISAY VRRTTESEND DGINRQVGLS
IRSDSMQNKL EVEYEISSRS MIPTKIDAKW QRQGYGGQRQ EICINMKTQG QGNDQRSEQT
RRSRDININW GQQCNDENYI KTRVGSSHCQ LRQKKIETAS RRKVYRDQWR SDAMQDDDEE
RDQKQIGYSV SKEETAGYKI QIQHRNVPEW AADRAEELIR MITSTNYWSS EVENKRQRYD
AAERNRQTYE QPREGEVRIQ AIMRNEDKAD VKIQTPRKTI RLNNVYIPTL LRRETYRRSN
LMRFMNLYMG NKHTKGTCQI RQNSITTFDG ATYRIPFSDC YTILARDSEE DPKFAIMARR
SREQQDKKVR GRIPACSTIV KLMTSDHEIE LIPERQGGIE VKVDGQRWDD QQAKHHRAMR
IRQRENEVTV DLKRPNVDVH YDGNEITIRV SDKYHGRQTG MCGNLNADWS DEFPMSNQKN
RDDIWEMFNE MTIKTDSCQH PQRQDRDDSQ QFDSYDSDSD SDSDDNWEMA RQHRSDDDVS
YDDEEESSIF DSDREQQRRD QGRNQNYRSL AIDDVLTETA PIRRNKVIDS RGRKCISMRP
IERCPEHGYT ARGEREEKEV PYTCLKANDE LYHKIGQMQR QGMSMDLSNR ERSFTRKETV
PRKCIAIV
//
