MVP_LEIBR
ID MVP_LEIBR Reviewed; 833 AA.
AC A4H452;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Major vault protein;
GN ORFNames=LBRM_05_0060;
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660;
RN [1] {ECO:0000312|EMBL:CAM36840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000312|EMBL:CAM36840.1};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
CC -!- FUNCTION: Required for normal vault structure. Vaults are multi-subunit
CC structures that may act as scaffolds for proteins involved in signal
CC transduction. Vaults may also play a role in nucleo-cytoplasmic
CC transport (By similarity). {ECO:0000250|UniProtKB:Q14764}.
CC -!- SUBUNIT: The vault ribonucleoprotein particle is a huge (400 A x 670 A)
CC cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with
CC each half-vault comprising 39 identical major vault protein (MVP)
CC chains, PARP4 and one or more vault RNAs (vRNAs) (By similarity).
CC {ECO:0000250|UniProtKB:Q14764}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14764,
CC ECO:0000255|PROSITE-ProRule:PRU00571}. Nucleus
CC {ECO:0000250|UniProtKB:Q14764}.
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DR EMBL; FR798979; CAM36840.1; -; Genomic_DNA.
DR RefSeq; XP_001561821.1; XM_001561771.1.
DR AlphaFoldDB; A4H452; -.
DR SMR; A4H452; -.
DR STRING; 5660.A4H452; -.
DR PRIDE; A4H452; -.
DR GeneID; 5412774; -.
DR KEGG; lbz:LBRM_05_0060; -.
DR VEuPathDB; TriTrypDB:LbrM.05.0060; -.
DR VEuPathDB; TriTrypDB:LBRM2903_050005500; -.
DR InParanoid; A4H452; -.
DR OMA; VIRIKRY; -.
DR Proteomes; UP000007258; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR CDD; cd08825; MVP_shoulder; 1.
DR Gene3D; 2.30.30.550; -; 4.
DR Gene3D; 2.30.30.560; -; 2.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR039059; MVP.
DR InterPro; IPR041139; MVP_rep_dom.
DR InterPro; IPR043023; MVP_rep_sf.
DR InterPro; IPR021870; MVP_shoulder.
DR InterPro; IPR041134; Vault_2.
DR InterPro; IPR043179; Vault_2_sf.
DR InterPro; IPR040989; Vault_3.
DR InterPro; IPR041136; Vault_4.
DR InterPro; IPR002499; Vault_N.
DR PANTHER; PTHR14165; PTHR14165; 1.
DR Pfam; PF11978; MVP_shoulder; 1.
DR Pfam; PF01505; Vault; 4.
DR Pfam; PF17794; Vault_2; 1.
DR Pfam; PF17795; Vault_3; 1.
DR Pfam; PF17796; Vault_4; 1.
DR PROSITE; PS51224; MVP; 8.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein.
FT CHAIN 1..833
FT /note="Major vault protein"
FT /id="PRO_0000414608"
FT REPEAT 10..52
FT /note="MVP 1"
FT /evidence="ECO:0000255"
FT REPEAT 54..115
FT /note="MVP 2"
FT /evidence="ECO:0000255"
FT REPEAT 119..170
FT /note="MVP 3"
FT /evidence="ECO:0000255"
FT REPEAT 171..223
FT /note="MVP 4"
FT /evidence="ECO:0000255"
FT REPEAT 224..278
FT /note="MVP 5"
FT /evidence="ECO:0000255"
FT REPEAT 280..328
FT /note="MVP 6"
FT /evidence="ECO:0000255"
FT REPEAT 329..380
FT /note="MVP 7"
FT /evidence="ECO:0000255"
FT REPEAT 381..433
FT /note="MVP 8"
FT /evidence="ECO:0000255"
SQ SEQUENCE 833 AA; 93280 MW; E382F37DFF268891 CRC64;
MTDSVIRIKR YYYIHILDNN TNVTRTISGP VVYTRQEHET CLFDPRPCVS VPPRHYCVVK
NPCVRNEAGE VVLESSGQVK LRLGDAEIRF EGEPFPLYPG EELDSKEEQS VRKLQVIPPN
TGLHVRCVRD FKDAERLVVA GTEWMVAGPQ SYIPRVEVAV VEEVKATVIY PNTALLLQAN
VNFTDRRGVL RVAGEKWLVR TLGAYLPSVE ETVVSLIQGT MLSELKALRL SAVRSFTDVY
GKARRAGEQW QVTLKDAPVH IVDAYETKVA EVAAVSLNAK EYVIIHHPVD ATGHNRFGET
LVRRGECTFF LQPEETMPRG VEQVLVVGKE EALLLEAVCE YHDGGGKHQP GSRWMVRGPC
EYIPANEVKL LEHRRVMALD RNEGIYVMNT TTGEVRAVIG KPYMLDSNEV LWEKHLPLAI
EELLESPNGS IKTCERNAGF VSRREKYRIV RFNVQHNAAV QIYDYRTKKP RIVLGPSLVM
LAPHEEFTVL SLSGGTPKVP NSMQSLQLFL GPRFSSDTIV VETSDHARLR LRLSYNWYFD
IDRANPSQRT FSVPDFIGDC CKTIASRVRG AVAAEDFDSF HRNSAKIIRI AVFGVDEVGE
AKKNLRFNAN DFVVTNIDVQ SAEPTDEKTR DSLQKSVQLA IEITTKSQEA AARHGNELKN
QEAKGHLERQ KLIDKIEVEN ARTKWLELQA KSEAVQASGQ SIAEAKARAE ALLIEVQSEM
QQAEMRAKAY RISAEAELQK LQQRQALELE YTQRQNEIDV AKARAAAEAE AEKVRRMVDA
IGRDTLVAIA RAGPEAQVKL LGSLGLKGYL ITDGNSPVNL FDAAHGMIGE PKK