MVP_STRPU
ID MVP_STRPU Reviewed; 857 AA.
AC Q5EAJ7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Major vault protein {ECO:0000312|EMBL:DAA05661.1};
DE Short=MVP {ECO:0000303|PubMed:15710043};
GN Name=MVP {ECO:0000312|EMBL:DAA05661.1};
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-533 AND 616-857.
RC TISSUE=Gastrula {ECO:0000269|PubMed:14656975}, and
RC Larva {ECO:0000269|PubMed:14656975};
RX PubMed=14656975; DOI=10.1101/gr.1674103;
RA Poustka A.J., Groth D., Hennig S., Thamm S., Cameron A., Beck A.,
RA Reinhardt R., Herwig R., Panopoulou G., Lehrach H.;
RT "Generation, annotation, evolutionary analysis, and database integration of
RT 20,000 unique sea urchin EST clusters.";
RL Genome Res. 13:2736-2746(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 499-769.
RC TISSUE=Embryo {ECO:0000269|PubMed:11493577};
RX PubMed=11493577; DOI=10.1242/dev.128.13.2615;
RA Zhu X., Mahairas G., Illies M., Cameron R.A., Davidson E.H.,
RA Ettensohn C.A.;
RT "A large-scale analysis of mRNAs expressed by primary mesenchyme cells of
RT the sea urchin embryo.";
RL Development 128:2615-2627(2001).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9331335; DOI=10.1006/dbio.1997.8676;
RA Hamill D.R., Suprenant K.A.;
RT "Characterization of the sea urchin major vault protein: a possible role
RT for vault ribonucleoprotein particles in nucleocytoplasmic transport.";
RL Dev. Biol. 190:117-128(1997).
RN [4] {ECO:0000305, ECO:0000312|EMBL:DAA05661.1}
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS), IDENTIFICATION,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15710043; DOI=10.1186/1471-213x-5-3;
RA Stewart P.L., Makabi M., Lang J., Dickey-Sims C., Robertson A.J.,
RA Coffman J.A., Suprenant K.A.;
RT "Sea urchin vault structure, composition, and differential localization
RT during development.";
RL BMC Dev. Biol. 5:3-3(2005).
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).
CC {ECO:0000250|UniProtKB:Q14764, ECO:0000269|PubMed:15710043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00571,
CC ECO:0000269|PubMed:15710043, ECO:0000269|PubMed:9331335}. Nucleus
CC {ECO:0000269|PubMed:15710043, ECO:0000269|PubMed:9331335}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos, tube feet and coelomocytes
CC (at protein level). Not expressed in sperm cells (at protein level).
CC {ECO:0000269|PubMed:9331335}.
CC -!- DEVELOPMENTAL STAGE: Highly and constitutively expressed throughout
CC development. However, the ratio of soluble to insoluble protein changes
CC during embryogenesis. Additionally, the distribution changes from a
CC largely cytoplasmic distribution in the cleavage stage embryo to a
CC predominantly nuclear and/or perinuclear location at blastula and
CC gastrula stages. {ECO:0000269|PubMed:15710043,
CC ECO:0000269|PubMed:9331335}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CD295616; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CD295832; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CD304000; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CD305511; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CD333690; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CD292179; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD292477; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD295616; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD295832; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD304000; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD305382; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD305511; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD305646; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD307400; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD310423; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD333690; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BG784394; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BG784484; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK005641; DAA05661.1; -; mRNA.
DR RefSeq; NP_001116989.1; NM_001123517.1.
DR AlphaFoldDB; Q5EAJ7; -.
DR SMR; Q5EAJ7; -.
DR STRING; 7668.SPU_000881-tr; -.
DR EnsemblMetazoa; NM_001123517; NP_001116989; GeneID_575735.
DR GeneID; 575735; -.
DR KEGG; spu:575735; -.
DR CTD; 9961; -.
DR eggNOG; ENOG502QPP0; Eukaryota.
DR HOGENOM; CLU_016171_0_0_1; -.
DR InParanoid; Q5EAJ7; -.
DR OMA; VIRIKRY; -.
DR OrthoDB; 256008at2759; -.
DR PhylomeDB; Q5EAJ7; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IPR000048; IQ_motif_EF-hand-BS.
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; 2.
DR Pfam; PF17795; Vault_3; 1.
DR Pfam; PF17796; Vault_4; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51224; MVP; 8.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; Ribonucleoprotein.
FT CHAIN 1..857
FT /note="Major vault protein"
FT /id="PRO_0000394756"
FT REPEAT 18..60
FT /note="MVP 1"
FT /evidence="ECO:0000255"
FT REPEAT 62..122
FT /note="MVP 2"
FT /evidence="ECO:0000255"
FT REPEAT 123..174
FT /note="MVP 3"
FT /evidence="ECO:0000255"
FT REPEAT 175..227
FT /note="MVP 4"
FT /evidence="ECO:0000255"
FT REPEAT 228..282
FT /note="MVP 5"
FT /evidence="ECO:0000255"
FT REPEAT 284..332
FT /note="MVP 6"
FT /evidence="ECO:0000255"
FT REPEAT 333..387
FT /note="MVP 7"
FT /evidence="ECO:0000255"
FT REPEAT 388..441
FT /note="MVP 8"
FT /evidence="ECO:0000255"
FT DOMAIN 665..694
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 434..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 51
FT /note="F -> S (in Ref. 1; CD333690)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="T -> P (in Ref. 1; CD333690)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="I -> T (in Ref. 1; CD305511)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..76
FT /note="NDT -> ERY (in Ref. 1; CD333690)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="E -> K (in Ref. 1; CD333690)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="N -> T (in Ref. 1; CD333690)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="D -> T (in Ref. 1; CD333690)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="D -> N (in Ref. 1; CD305646)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="Q -> H (in Ref. 1; CD295616)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="C -> R (in Ref. 1; CD295616)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="E -> K (in Ref. 1; CD305646)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="G -> E (in Ref. 1; CD305646)"
FT /evidence="ECO:0000305"
FT CONFLICT 475..476
FT /note="YK -> LQ (in Ref. 1; CD295616)"
FT /evidence="ECO:0000305"
FT CONFLICT 489..491
FT /note="VML -> CHA (in Ref. 1; CD295616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 857 AA; 95925 MW; AEACAE46FEC9DDFA CRC64;
MASKRGSNQD ESIFRIPPYY YIHVLDHNDN VTKVVVGPKT YIRQDHERVI FGPEKMITIP
PRHYCIIENP VVRNDTDQVV YDNLGQVKLF HADQEIRLAR EPFPLYPGEV LKQAVTALKV
VQANAALRLR AILDFEDGTQ KRVAGDEWLF EGPGTYIPRK EVVVDETIRA TIIRPNQAIK
LRARKETNDR EGTARVTGEE WQVKKVGAYL PGAYEEVVDT VNAYVLTEKN ALHLRATRTF
VDMKGKTRKN GEEWLINMAD TDAHIPDVYE EVVGVVDINT LTNRQYCVIV DPVGPDGKPQ
LGQKKLVKGE VSFFLQPGET LEQGIQSVFI LGEDEGLILR AQESFKDANA AGAVRQPGDR
WMIRGPCEYV PTVELEVVTR RKAIPLDENE GVYIRDTKTG KVRAVTGETY MLSQDEELWA
KELSPAVEEL LQSAKDPVAE RSDRRGDRAA PRAREKTRVI SFRVPHNAAV QIYDYKEKKA
RVVFGPELVM LGPDEQFTQL SLSGGKPKRP NVIKALCLLL GPDFCTDIIT IETADHARLQ
LQLSYNWHFD VPDKTDVAAS AKLFSVPDFI GDACKAIASR IRGAVAGVQF DDFHKNSAKI
IRASVFGFDE KNKVRERFLF PQNSLVITSI DIQSVEPVDQ RTRDALQKSV QLAIEITTNS
QEATARHEAE RLEQEARGRL ERQKIMDEAE AEKSRKELLE LQANSAAVES TGQAKAEAQS
RAEAARIEGE AAVDQARLKA EAAKIESESE LQRLTNAREA ETKYVREQNA LEVNKTKQMS
DIETERFRNM VQSIGADTIK AMAMAGPEMQ VKLLSSLGLK STLITDGSTP INLFNTAQGL
LGGFSAKRGI EHVEEED