PLVAP_RAT
ID PLVAP_RAT Reviewed; 438 AA.
AC Q9WV78;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Plasmalemma vesicle-associated protein;
DE AltName: Full=Plasmalemma vesicle protein 1;
DE Short=PV-1;
DE AltName: Full=gp68;
GN Name=Plvap; Synonyms=Pv1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-16; 232-241 AND 248-264,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Lung endothelial cell;
RX PubMed=10366592; DOI=10.1083/jcb.145.6.1189;
RA Stan R.-V., Ghitescu L., Jacobson B.S., Palade G.E.;
RT "Isolation, cloning, and localization of rat PV-1, a novel endothelial
RT caveolar protein.";
RL J. Cell Biol. 145:1189-1198(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Lung endothelial cell;
RX PubMed=10557298; DOI=10.1073/pnas.96.23.13203;
RA Stan R.-V., Kubitza M., Palade G.E.;
RT "PV-1 is a component of the fenestral and stomatal diaphragms in
RT fenestrated endothelia.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13203-13207(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=12475376; DOI=10.1677/joe.0.1750649;
RA Hnasko R., McFarland M., Ben-Jonathan N.;
RT "Distribution and characterization of plasmalemma vesicle protein-1 in rat
RT endocrine glands.";
RL J. Endocrinol. 175:649-661(2002).
RN [5]
RP SUBUNIT.
RX PubMed=14630628; DOI=10.1152/ajpheart.00909.2003;
RA Stan R.-V.;
RT "Multiple PV1 dimers reside in the same stomatal or fenestral diaphragm.";
RL Am. J. Physiol. 286:H1347-H1353(2004).
RN [6]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15640522; DOI=10.1152/ajplung.00236.2004;
RA Hnasko R., Ben-Jonathan N.;
RT "Developmental regulation of PV-1 in rat lung: association with the nuclear
RT envelope and limited colocalization with Cav-1.";
RL Am. J. Physiol. 288:L275-L284(2005).
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:0000250|UniProtKB:Q91VC4}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14630628}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10366592,
CC ECO:0000269|PubMed:10557298}; Single-pass type II membrane protein
CC {ECO:0000255}. Membrane, caveola {ECO:0000269|PubMed:10366592,
CC ECO:0000269|PubMed:10557298}; Single-pass type II membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:15640522}. Note=Membrane-associated protein of
CC caveolae (PubMed:10366592). Found in fenestral and stomatal diaphragms
CC in fenestrated endothelia and transendothelial channels
CC (PubMed:10557298). Also colocalized with CAV1 in perinuclear region
CC (PubMed:15640522). {ECO:0000269|PubMed:10366592,
CC ECO:0000269|PubMed:10557298, ECO:0000269|PubMed:15640522}.
CC -!- TISSUE SPECIFICITY: Expressed in lung (alveolar endothelial and
CC bronchial epithelial cells), kidney (endothelium of peritubular
CC capillaries), spleen, liver, adrenal (endothelial cells of the zona
CC reticularis of the cortex and chromaffin cells in the medulla),
CC pancreas (islets of Langerhans), testis (germ cells, interstitial cells
CC in neonatal testis and spermatids), ovary (stromal endothelial, thecal
CC layer of developing follicles, luteal cells within the corpus luteum),
CC intestine (endothelium of capillaries of the intestinal villi) and
CC pituitary (pituicyte cells in the neural lobe) (at protein level).
CC Expressed in lung, kidney, spleen, liver, adrenal, testis, heart,
CC muscle, pituitary, thyroid and ovary. {ECO:0000269|PubMed:10366592,
CC ECO:0000269|PubMed:10557298, ECO:0000269|PubMed:12475376,
CC ECO:0000269|PubMed:15640522}.
CC -!- DEVELOPMENTAL STAGE: Expressed in endothelial cells of the lung at 12
CC dpc. {ECO:0000269|PubMed:15640522}.
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DR EMBL; AF154831; AAD41524.1; -; mRNA.
DR EMBL; BC070900; AAH70900.1; -; mRNA.
DR RefSeq; NP_064471.1; NM_020086.1.
DR AlphaFoldDB; Q9WV78; -.
DR SMR; Q9WV78; -.
DR BioGRID; 248574; 1.
DR IntAct; Q9WV78; 1.
DR STRING; 10116.ENSRNOP00000023927; -.
DR GlyGen; Q9WV78; 4 sites.
DR iPTMnet; Q9WV78; -.
DR PhosphoSitePlus; Q9WV78; -.
DR PaxDb; Q9WV78; -.
DR PRIDE; Q9WV78; -.
DR Ensembl; ENSRNOT00000023926; ENSRNOP00000023927; ENSRNOG00000017676.
DR GeneID; 56765; -.
DR KEGG; rno:56765; -.
DR UCSC; RGD:619971; rat.
DR CTD; 83483; -.
DR RGD; 619971; Plvap.
DR eggNOG; ENOG502S1PR; Eukaryota.
DR GeneTree; ENSGT00390000006166; -.
DR HOGENOM; CLU_049986_0_0_1; -.
DR InParanoid; Q9WV78; -.
DR OMA; HLTCESQ; -.
DR OrthoDB; 1080934at2759; -.
DR PhylomeDB; Q9WV78; -.
DR TreeFam; TF337332; -.
DR PRO; PR:Q9WV78; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000017676; Expressed in lung and 17 other tissues.
DR ExpressionAtlas; Q9WV78; baseline and differential.
DR Genevisible; Q9WV78; RN.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:RGD.
DR GO; GO:0043114; P:regulation of vascular permeability; IBA:GO_Central.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
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; Direct protein sequencing;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..438
FT /note="Plasmalemma vesicle-associated protein"
FT /id="PRO_0000058464"
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 393..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..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"
SQ SEQUENCE 438 AA; 50033 MW; 99A016CDD12568C2 CRC64;
MGLSMDRSPY SRTGDRDRGC WYYLRYFFLF VSLIQFLIIL GLVLFMIYGN VHATTESSLR
ATEIRADNLY SQVVGLSAAQ ANLSKQLNIS TLVKDTVMQQ LLTTRREVER INASFRQCQG
DLITYINYNR FIAAIILSEK QCQEQLKEGN KTCEALLFKL GEKVKTLEME VVKEKAVCSK
DKDSLLAGKR QAEMQQEACG KAREQQKQDQ QVTEEQLRKV QSLCLPLDQE KFQADVLNVW
RDSLVYRSLD NIGYHYSLMP EFSSLRRTCE SLPGIMTTKV EELARGLRAG IERVTRENGE
LRRQKLELER AIQGEREART RAGTEAQARE TQLRTECARQ TQLALEEKAA LRTQRDDLER
QLEARKRELE QLRTEVDVRI SALDTCVKAK SLPAIQPRLP GPPPNPPPID PASLEEFKKR
ILESQRPPLV NPAVPPSG
