PRAP1_MOUSE
ID PRAP1_MOUSE Reviewed; 149 AA.
AC Q80XD8; Q60874;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Proline-rich acidic protein 1;
DE AltName: Full=Pregnancy-specific uterine protein;
DE AltName: Full=Uterine-specific proline-rich acidic protein;
DE Flags: Precursor;
GN Name=Prap1; Synonyms=Upa;
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], AND TISSUE SPECIFICITY.
RC STRAIN=CF-1; TISSUE=Uterus;
RX PubMed=9065197; DOI=10.1016/s0002-9378(97)70514-3;
RA Kasik J., Rice E.;
RT "A novel complementary deoxyribonucleic acid is abundantly and specifically
RT expressed in the uterus during pregnancy.";
RL Am. J. Obstet. Gynecol. 176:452-456(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Swiss albino;
RX PubMed=10899595; DOI=10.1016/s0167-4781(00)00135-4;
RA Zhang J., Rajkumar N., Hooi S.C.;
RT "Characterization and expression of the mouse pregnant specific uterus
RT protein and its rat homologue in the intestine and uterus.";
RL Biomed. Biochim. Acta 1492:526-530(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32629119; DOI=10.1016/j.jcmgh.2020.06.011;
RA Wolfarth A.A., Liu X., Darby T.M., Boyer D.J., Spizman J.B., Owens J.A.,
RA Chandrasekharan B., Naudin C.R., Hanley K.Z., Robinson B.S., Ortlund E.A.,
RA Jones R.M., Neish A.S.;
RT "Proline-Rich Acidic Protein 1 (PRAP1) Protects the Gastrointestinal
RT Epithelium From Irradiation-Induced Apoptosis.";
RL Cell. Mol. Gastroenterol. Hepatol. 10:713-727(2020).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP INTERACTION WITH MTTP, AND MUTAGENESIS OF GLU-85.
RX PubMed=33168624; DOI=10.1074/jbc.ra120.015002;
RA Peng H., Chiu T.Y., Liang Y.J., Lee C.J., Liu C.S., Suen C.S., Yen J.J.,
RA Chen H.T., Hwang M.J., Hussain M.M., Yang H.C., Yang-Yen H.F.;
RT "PRAP1 is a novel lipid-binding protein that promotes lipid absorption by
RT facilitating MTTP-mediated lipid transport.";
RL J. Biol. Chem. 296:100052-100052(2020).
CC -!- FUNCTION: Lipid-binding protein which promotes lipid absorption by
CC facilitating MTTP-mediated lipid transfer (mainly triglycerides and
CC phospholipids) and MTTP-mediated apoB lipoprotein assembly and
CC secretion (PubMed:33168624). Protects the gastrointestinal epithelium
CC from irradiation-induced apoptosis (PubMed:32629119). May play an
CC important role in maintaining normal growth homeostasis in epithelial
CC cells (By similarity). Involved in p53/TP53-dependent cell survival
CC after DNA damage (By similarity). {ECO:0000250|UniProtKB:Q96NZ9,
CC ECO:0000269|PubMed:32629119, ECO:0000269|PubMed:33168624}.
CC -!- SUBUNIT: Interacts with MTTP (PubMed:33168624). Interacts with MAD1L1
CC (By similarity). {ECO:0000250|UniProtKB:Q96NZ9,
CC ECO:0000269|PubMed:33168624}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33168624}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:33168624}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the intestinal
CC epithelial cells than in the liver (at protein level) (PubMed:33168624,
CC PubMed:32629119). Abundantly expressed in the uterus during late
CC pregnancy by uterus epithelial cells. After birth expression rapidly
CC decreases and is no longer found in the uterus by the third day. Also
CC highly expressed in the small intestine where it shows a proximal-
CC distal graded expression. {ECO:0000269|PubMed:10899595,
CC ECO:0000269|PubMed:32629119, ECO:0000269|PubMed:33168624,
CC ECO:0000269|PubMed:9065197}.
CC -!- DISRUPTION PHENOTYPE: Mice show an increase in the length of the small
CC intestine (PubMed:33168624). Gain significantly less body weight and
CC fat mass when on high-fat diets compared with littermate controls and
CC are prevented from hepatosteatosis (PubMed:33168624). Show increased
CC cytokine expression and altered gut microbiota, and are significantly
CC more susceptible to oxidative insult by ionizing radiation, showing
CC accelerated mortality and enterocyte apoptosis (PubMed:32629119).
CC {ECO:0000269|PubMed:32629119, ECO:0000269|PubMed:33168624}.
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DR EMBL; U28486; AAC24897.1; -; mRNA.
DR EMBL; BC051092; AAH51092.1; -; mRNA.
DR CCDS; CCDS21963.1; -.
DR RefSeq; NP_033501.2; NM_009475.2.
DR AlphaFoldDB; Q80XD8; -.
DR STRING; 10090.ENSMUSP00000026540; -.
DR PhosphoSitePlus; Q80XD8; -.
DR CPTAC; non-CPTAC-3610; -.
DR MaxQB; Q80XD8; -.
DR PaxDb; Q80XD8; -.
DR PeptideAtlas; Q80XD8; -.
DR PRIDE; Q80XD8; -.
DR ProteomicsDB; 289395; -.
DR DNASU; 22264; -.
DR Ensembl; ENSMUST00000026540; ENSMUSP00000026540; ENSMUSG00000025467.
DR GeneID; 22264; -.
DR KEGG; mmu:22264; -.
DR UCSC; uc009kgt.2; mouse.
DR CTD; 118471; -.
DR MGI; MGI:893573; Prap1.
DR VEuPathDB; HostDB:ENSMUSG00000025467; -.
DR eggNOG; ENOG502TDVH; Eukaryota.
DR GeneTree; ENSGT00390000012626; -.
DR HOGENOM; CLU_148119_0_0_1; -.
DR InParanoid; Q80XD8; -.
DR OMA; WVETEDI; -.
DR OrthoDB; 1574174at2759; -.
DR PhylomeDB; Q80XD8; -.
DR TreeFam; TF337049; -.
DR BioGRID-ORCS; 22264; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q80XD8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80XD8; protein.
DR Bgee; ENSMUSG00000025467; Expressed in duodenum and 66 other tissues.
DR Genevisible; Q80XD8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0017129; F:triglyceride binding; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071481; P:cellular response to X-ray; IMP:UniProtKB.
DR GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1904731; P:positive regulation of intestinal lipid absorption; IMP:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; IMP:UniProtKB.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; IMP:UniProtKB.
DR InterPro; IPR027922; PRAP.
DR PANTHER; PTHR37861; PTHR37861; 1.
DR Pfam; PF15314; PRAP; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..149
FT /note="Proline-rich acidic protein 1"
FT /id="PRO_0000299417"
FT REGION 51..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 85
FT /note="E->V: Impairs its ability to form a complex with
FT triglycerides and MTTP, as well as its ability to
FT facilitate MTTP-mediated lipid transfer and MTTP-mediated
FT apoB lipoprotein assembly and secretion."
FT /evidence="ECO:0000269|PubMed:33168624"
FT CONFLICT 21
FT /note="A -> R (in Ref. 1; AAC24897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 16798 MW; 38D4FD997E0C90C0 CRC64;
MKRFLLATCL VAALLWEAGA APAHQVPVKT KGKHVFPEQE TEKVWDTRAL EPLEKDNQLG
PLLPEPKQKP AAAEEKRPDA MTWVETEDIL SHLRSPLQGP ELDLDSIDHP MSDDVQDEEV
PQSRPILYRQ VLQGPEEDLD HLAHSMEDS
