ID   ESIP1_RAT               Reviewed;         314 AA.
AC   Q5BK43;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Epithelial-stromal interaction protein 1;
GN   Name=Epsti1;
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 [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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).
CC   -!- FUNCTION: Plays a role in M1 macrophage polarization and is required
CC       for the proper regulation of gene expression during M1 versus M2
CC       macrophage differentiation (By similarity). Might play a role in
CC       RELA/p65 and STAT1 phosphorylation and nuclear localization upon
CC       activation of macrophages (By similarity).
CC       {ECO:0000250|UniProtKB:Q8VDI1}.
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DR   EMBL; BC091212; AAH91212.1; -; mRNA.
DR   RefSeq; NP_001037722.1; NM_001044257.1.
DR   AlphaFoldDB; Q5BK43; -.
DR   STRING; 10116.ENSRNOP00000012632; -.
DR   PaxDb; Q5BK43; -.
DR   Ensembl; ENSRNOT00000012632; ENSRNOP00000012632; ENSRNOG00000009471.
DR   GeneID; 498547; -.
DR   KEGG; rno:498547; -.
DR   UCSC; RGD:1563207; rat.
DR   CTD; 94240; -.
DR   RGD; 1563207; Epsti1.
DR   eggNOG; ENOG502RZCM; Eukaryota.
DR   GeneTree; ENSGT00390000013820; -.
DR   HOGENOM; CLU_058937_1_0_1; -.
DR   InParanoid; Q5BK43; -.
DR   OMA; SGGYWNM; -.
DR   OrthoDB; 1284389at2759; -.
DR   PhylomeDB; Q5BK43; -.
DR   TreeFam; TF335788; -.
DR   Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR   PRO; PR:Q5BK43; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000009471; Expressed in spleen and 19 other tissues.
DR   Genevisible; Q5BK43; RN.
DR   InterPro; IPR026185; EPSTI1.
DR   PANTHER; PTHR22529; PTHR22529; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Reference proteome.
FT   CHAIN           1..314
FT                   /note="Epithelial-stromal interaction protein 1"
FT                   /id="PRO_0000314036"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          71..180
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        57..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   314 AA;  35965 MW;  9064431734F8062F CRC64;
     MYPRSRVVGP GLGTSSSSRD HAGAGQHGEL DLQQNQRQNL EVAEPKGPKL ERQGHGDQRS
     TGTYTLIAPN ETRRQKIQRI AEQELADLER WKQQNKAKPV HLVPQRLGGS QSEAEVRQKQ
     QLQQMRSKYQ QKLKRDEAIR IRKDAEEAEL QRMKAIQREK SNKLEKKKQL QEDIRRATLR
     EHHQSKTAEL LSRLDTDRTN RSACNIAPPA AQSSRWKLPV LLRDPSRAGS QAHKDSPQKE
     DNQKLQKTRD GHQKNKLLET KGQHQEEERA QIHQAEHWRV NNAFLDRLQG KSQPGGVEQS
     GGCWNMNSTD GWGI