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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
 
 
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