PRAP1_RAT
ID PRAP1_RAT Reviewed; 152 AA.
AC Q9ES75;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Proline-rich acidic protein 1;
DE Flags: Precursor;
GN Name=Prap1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Intestine;
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).
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 (By similarity). Protects the gastrointestinal epithelium
CC from irradiation-induced apoptosis (By similarity). 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:Q80XD8,
CC ECO:0000250|UniProtKB:Q96NZ9}.
CC -!- SUBUNIT: Interacts with MTTP (By similarity). Interacts with MAD1L1 (By
CC similarity). {ECO:0000250|UniProtKB:Q80XD8,
CC ECO:0000250|UniProtKB:Q96NZ9}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q80XD8}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q80XD8}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the small intestine where it
CC shows a proximal-distal graded expression.
CC {ECO:0000269|PubMed:10899595}.
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DR EMBL; AF214733; AAG31029.1; -; mRNA.
DR RefSeq; NP_113857.1; NM_031669.1.
DR AlphaFoldDB; Q9ES75; -.
DR STRING; 10116.ENSRNOP00000024912; -.
DR PaxDb; Q9ES75; -.
DR Ensembl; ENSRNOT00000024912; ENSRNOP00000024912; ENSRNOG00000018446.
DR GeneID; 60574; -.
DR KEGG; rno:60574; -.
DR UCSC; RGD:61876; rat.
DR CTD; 118471; -.
DR RGD; 61876; Prap1.
DR eggNOG; ENOG502TDVH; Eukaryota.
DR GeneTree; ENSGT00390000012626; -.
DR HOGENOM; CLU_148119_0_0_1; -.
DR InParanoid; Q9ES75; -.
DR OMA; WVETEDI; -.
DR OrthoDB; 1574174at2759; -.
DR PhylomeDB; Q9ES75; -.
DR TreeFam; TF337049; -.
DR PRO; PR:Q9ES75; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018446; Expressed in duodenum and 14 other tissues.
DR Genevisible; Q9ES75; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0017129; F:triglyceride binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071481; P:cellular response to X-ray; ISS: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; ISS:UniProtKB.
DR GO; GO:1904731; P:positive regulation of intestinal lipid absorption; ISS:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; ISS:UniProtKB.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; ISS:UniProtKB.
DR InterPro; IPR027922; PRAP.
DR PANTHER; PTHR37861; PTHR37861; 1.
DR Pfam; PF15314; PRAP; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..152
FT /note="Proline-rich acidic protein 1"
FT /id="PRO_0000299418"
SQ SEQUENCE 152 AA; 17322 MW; ECA2F608E132B767 CRC64;
MKRFLLATCL VAVLLWEAGA IPAHQVPVKT KGKHVFPEQE TEKAWGTRAM EPLEKDDQLR
ALLPVPKQKL AATEEKHSDT MTWVETKDIL SRFRNPLQGP ELDLDSIYHP MSEDVQNEEV
PQSRPILYRQ VLHGPEEDLD HISHSLEDSG EP