ID   NRBP_MACFA              Reviewed;         535 AA.
AC   Q4R8X0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Nuclear receptor-binding protein;
GN   Name=NRBP1; ORFNames=QtsA-11263;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1] {ECO:0000312|EMBL:BAE00451.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in subcellular trafficking between the
CC       endoplasmic reticulum and Golgi apparatus through interactions with the
CC       Rho-type GTPases. {ECO:0000250|UniProtKB:Q9UHY1}.
CC   -!- SUBUNIT: Homodimer. Binds to MLF1, recruiting a serine kinase which
CC       phosphorylates both itself and MLF1. Phosphorylated MLF1 binds to YWHAZ
CC       and is retained in the cytoplasm (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}.
CC       Endomembrane system {ECO:0000250}. Cell projection, lamellipodium
CC       {ECO:0000250}. Note=Colocalizes with activated RAC3 to endomembranes
CC       and at the cell periphery in lamellipodia. {ECO:0000250}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB168327; BAE00451.1; -; mRNA.
DR   EMBL; AB169835; BAE01916.1; -; mRNA.
DR   RefSeq; XP_005576331.1; XM_005576274.2.
DR   AlphaFoldDB; Q4R8X0; -.
DR   SMR; Q4R8X0; -.
DR   STRING; 9541.XP_005576330.1; -.
DR   Ensembl; ENSMFAT00000067571; ENSMFAP00000017031; ENSMFAG00000031403.
DR   GeneID; 101866221; -.
DR   KEGG; mcf:101866221; -.
DR   CTD; 29959; -.
DR   VEuPathDB; HostDB:ENSMFAG00000031403; -.
DR   eggNOG; KOG1266; Eukaryota.
DR   GeneTree; ENSGT00940000155605; -.
DR   Proteomes; UP000233100; Chromosome 13.
DR   Bgee; ENSMFAG00000031403; Expressed in skeletal muscle tissue and 13 other tissues.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell projection; Cytoplasm; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT   CHAIN           2..535
FT                   /note="Nuclear receptor-binding protein"
FT                   /id="PRO_0000086450"
FT   DOMAIN          68..327
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT   MOD_RES         431
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99J45"
FT   MOD_RES         433
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHY1"
SQ   SEQUENCE   535 AA;  59845 MW;  398078661547EDD0 CRC64;
     MSEGESQTVL SSGSDPKVES SSSAPGLTSV SPPVTSTTSA ASPEEEEESE DESEILEESP
     CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ FSERKNYKLQ EEKVRAVFDN
     LIQLEHLNIV KFHKYWADIK ENKARVIFIT EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW
     CTQILSALSY LHSCDPPIIH GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL
     HFFAPEYGEV TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDPLQ
     REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE NALEEITKNM
     DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG IYPLTAFGLP RPQQPQQEEV
     TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN IESVEEGVKH HLTLLLKLED KLNRHLSCDL
     MPNENIPELA AELVQLGFIS EADQSRLTSL LEETLNKFNF ARNSTLNSAA VTVSS