MVP_LEIIN
ID MVP_LEIIN Reviewed; 833 AA.
AC A4HSC9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Major vault protein;
GN ORFNames=LINJ_05_0060;
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671;
RN [1] {ECO:0000312|EMBL:CAM65315.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000312|EMBL:CAM65315.1};
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; FR796437; CAM65315.1; -; Genomic_DNA.
DR RefSeq; XP_001462970.1; XM_001462933.1.
DR AlphaFoldDB; A4HSC9; -.
DR SMR; A4HSC9; -.
DR STRING; 5671.XP_001462970.1; -.
DR PRIDE; A4HSC9; -.
DR GeneID; 5066571; -.
DR KEGG; lif:LINJ_05_0060; -.
DR VEuPathDB; TriTrypDB:LINF_050005500; -.
DR eggNOG; ENOG502QPP0; Eukaryota.
DR InParanoid; A4HSC9; -.
DR OMA; VIRIKRY; -.
DR Proteomes; UP000008153; 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; 7.
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_0000414609"
FT REPEAT 54..118
FT /note="MVP 1"
FT /evidence="ECO:0000255"
FT REPEAT 119..170
FT /note="MVP 2"
FT /evidence="ECO:0000255"
FT REPEAT 171..223
FT /note="MVP 3"
FT /evidence="ECO:0000255"
FT REPEAT 224..278
FT /note="MVP 4"
FT /evidence="ECO:0000255"
FT REPEAT 280..328
FT /note="MVP 5"
FT /evidence="ECO:0000255"
FT REPEAT 329..380
FT /note="MVP 6"
FT /evidence="ECO:0000255"
FT REPEAT 381..433
FT /note="MVP 7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 833 AA; 93170 MW; 82CEF46B990CDEB8 CRC64;
MTDSVIRIKR YHYIHILDNN TNVTRTISGP VVYTRKEHET CLFDPCPCVS VPPRHYCVVK
NPCVRGEAGE VVLESSGQVK LRLGDSEIRF EGEPFPLYPG EELDCRDGKG VQKLQLIPPN
TGLHVRCVRD FKDADRRVGA GTEWMVAGPQ TYIPRVEVVV VEEVKATVIY PNTALLVQAN
VNFTDRCGVP RVAGEKWLVR ALGAYLKSVE ETVLGLIQGT MLSDLKALRL SAVRSFTDVY
GKARRAGEQW QVTLKDAPVH IVDAYETKVA DVAAVSLSAK EYVIIHHPVD DTGHNRFGET
LVRRGECTFF LQPGETMPRG VEQVLVVGKE EALLLEAVCE YRDGGEKRQP GSRWMVHGPL
EYIPANEVKL LEHRRMMALD KNEGIYIMNT TTGEVRAVIG KPYMLDVNEV LWEKHLPLAV
EELLESPNGS IQTSERNPGF VSHREKYRIV RFNVQHNAAV QIYDYRKKQP RIVLGPNLVM
LAPHEEFTVL SLSGGTPKVP NSLQSLQLFL GPRFSSDTIV VETSDHARLR LRLSYNWYFD
IDRANPSRRT FSVPDFIGDC CKTIASRVRG AVAAEDFDSF HRNSAKIIRT AVFGVDEAGE
TKKNLRFTAN DFVVTNIDVQ SSEPTDEKTR DSLQKSVQLA IEITTKSQEA AARHGNELKD
QEAKGQLERQ KLLDKIEVEN ARTKWLELQA KSEAVQASGQ SVAEAKARAE ALFIEVRSEM
QQAEMRAKAY RISAEAELQK LQQRQALELE YTQRQNEIDV SKARAAAEAE AEKVKRMVDC
IGRDTLVAIA RAGPETQVKL LSSLGLKGYL ITDGNSPVNL FGTAQGMIGE PKK