PLVAP_MOUSE
ID PLVAP_MOUSE Reviewed; 438 AA.
AC Q91VC4; Q99JB1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Plasmalemma vesicle-associated protein;
DE AltName: Full=MECA-32 antigen;
DE AltName: Full=Plasmalemma vesicle protein 1;
DE Short=PV-1;
GN Name=Plvap; Synonyms=Pv1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Endothelial cell;
RX PubMed=7626790; DOI=10.1002/aja.1002020402;
RA Hallmann R., Mayer D.N., Berg E.L., Broermann R., Butcher E.C.;
RT "Novel mouse endothelial cell surface marker is suppressed during
RT differentiation of the blood brain barrier.";
RL Dev. Dyn. 202:325-332(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ, and C57BL/6J;
RX PubMed=11401446; DOI=10.1006/geno.2000.6489;
RA Stan R.-V., Arden K.C., Palade G.E.;
RT "cDNA and protein sequence, genomic organization, and analysis of cis
RT regulatory elements of mouse and human PLVAP genes.";
RL Genomics 72:304-313(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Endothelial cell;
RA Mesak F.M., Krueger B., Ge A.Z., Butcher E.C., Hallmann R.;
RT "Molecular cloning and expression of cDNA encoding endothelial cell marker
RT MECA32.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22782339; DOI=10.1007/s00418-012-0987-3;
RA Herrnberger L., Seitz R., Kuespert S., Boesl M.R., Fuchshofer R.,
RA Tamm E.R.;
RT "Lack of endothelial diaphragms in fenestrae and caveolae of mutant Plvap-
RT deficient mice.";
RL Histochem. Cell Biol. 138:709-724(2012).
CC -!- FUNCTION: Endothelial cell-specific membrane protein involved in the
CC formation of the diaphragms that bridge endothelial fenestrae. It is
CC also required for the formation of stomata of caveolae and
CC transendothelial channels. Functions in microvascular permeability,
CC endothelial fenestrae contributing to the passage of water and solutes
CC and regulating transcellular versus paracellular flow in different
CC organs. Plays a specific role in embryonic development.
CC {ECO:0000269|PubMed:22782339}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9WV78}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WV78};
CC Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9WV78}. Note=Membrane-associated protein of
CC caveolae. Found in fenestral and stomatal diaphragms in fenestrated
CC endothelia and transendothelial channels. Also colocalized with CAV1 in
CC perinuclear region. {ECO:0000250|UniProtKB:Q9WV78}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, kidney, spleen, heart, muscle,
CC eye, pancreas, thyroid, thymus, submaxillary gland, prostate,
CC epididymis, uterus and liver. {ECO:0000269|PubMed:11401446,
CC ECO:0000269|PubMed:7626790}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 7 dpc. Expressed in the
CC brain vasculature at 12 up to 16 dpc, whereupon it disappears.
CC {ECO:0000269|PubMed:11401446, ECO:0000269|PubMed:7626790}.
CC -!- DISRUPTION PHENOTYPE: Mutant animals result in lethality during
CC prenatal development. Examination of the homozygous deficient embryos
CC reveal subcutaneous edema, hemorrhages and defects in the vascular wall
CC of subcutaneous capillaries. Hearts of deficient embryos show
CC ventricular septal defects (VSDs) and thinner ventricular walls, as
CC well as blood abnormalities. Analyses on protein expression and
CC localization in endothelial cells of subcutaneous capillaries and
CC endocardium show that the protein and caveolae with stomatal diaphragm
CC were present in wild-type embryos, whereas the diaphragm is missing in
CC the caveolae of deficient embryos. Deficient mice are viable after
CC birth and survive up to 4 weeks on a mixed C57BL/6N/FVB-N background.
CC Embryos on the mixed background show edema in neck and back, but no
CC visible hemorrhages. Postnatal mutant mice display marked reduction in
CC body size and kinked tails compare with wild-type, but no VSDs are
CC observed in hearts. Detailed examination of the capillaries of kidneys
CC and pancreas reveal that the knockout mice does not form fenestrae with
CC diaphragm. {ECO:0000269|PubMed:22782339}.
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DR EMBL; AF369900; AAK54730.1; -; mRNA.
DR EMBL; AF348402; AAK20902.1; -; Genomic_DNA.
DR EMBL; AF348403; AAK20039.1; -; mRNA.
DR EMBL; BC013517; AAH13517.1; -; mRNA.
DR CCDS; CCDS22396.1; -.
DR RefSeq; NP_115774.2; NM_032398.2.
DR AlphaFoldDB; Q91VC4; -.
DR SMR; Q91VC4; -.
DR BioGRID; 220001; 3.
DR STRING; 10090.ENSMUSP00000035404; -.
DR GlyGen; Q91VC4; 4 sites.
DR iPTMnet; Q91VC4; -.
DR PhosphoSitePlus; Q91VC4; -.
DR jPOST; Q91VC4; -.
DR MaxQB; Q91VC4; -.
DR PaxDb; Q91VC4; -.
DR PRIDE; Q91VC4; -.
DR ProteomicsDB; 289940; -.
DR GeneID; 84094; -.
DR KEGG; mmu:84094; -.
DR CTD; 83483; -.
DR MGI; MGI:1890497; Plvap.
DR eggNOG; ENOG502S1PR; Eukaryota.
DR InParanoid; Q91VC4; -.
DR OrthoDB; 1080934at2759; -.
DR PhylomeDB; Q91VC4; -.
DR BioGRID-ORCS; 84094; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Plvap; mouse.
DR PRO; PR:Q91VC4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91VC4; protein.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0032502; P:developmental process; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:UniProtKB.
DR GO; GO:0043114; P:regulation of vascular permeability; IBA:GO_Central.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR InterPro; IPR009538; PV-1.
DR PANTHER; PTHR21687; PTHR21687; 1.
DR Pfam; PF06637; PV-1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Glycoprotein; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..438
FT /note="Plasmalemma vesicle-associated protein"
FT /id="PRO_0000058463"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 140..160
FT /evidence="ECO:0000255"
FT COILED 189..224
FT /evidence="ECO:0000255"
FT COILED 281..383
FT /evidence="ECO:0000255"
FT COMPBIAS 396..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 192
FT /note="T -> A (in Ref. 2; AAK20902/AAK20039)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..278
FT /note="TT -> PP (in Ref. 2; AAK20902/AAK20039)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="L -> M (in Ref. 2; AAK20902/AAK20039)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> V (in Ref. 2; AAK20902/AAK20039)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="A -> R (in Ref. 2; AAK20902/AAK20039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 49933 MW; 2566D9633F6C9809 CRC64;
MGLSMDRSPY ARTGDQQRGC WYYLRYFFLF VSLIQFLIIL GLVLFMIYGN VHATTESSLR
ATEIRADSLY SQVVGLSASQ ANLSKQLNIS LLVKETVMQQ LLTTRREMER INASFRQCQG
DLITYINYNR FIAAIILSEK QCQEQLKEVN KTCEALLFKL GEKVKTLEME VAKEKAVCSK
DKESLLAGKR QTEEQLEACG KARERQQQEQ QVTEENLRKV QSLCIPLDQE KFQADVLSAW
RDSLIYRTLE TLPYHYQLMP EYASLRRTCE SLPGIMTTKI EELARGLRAG IERVTRENAE
LRRQKLELER AAQAAQEARA RAGTEAQARE TQLRAECARQ TQLALEEKAA LRAQRDNLER
ELEARKRELE QLRTEVDVRI SALDTCVKAK SLPAVPPRVS GPPPNPPPID PASLEEFKKR
ILESQRLPVV NPAAQPSG
