SARNP_RAT
ID SARNP_RAT Reviewed; 210 AA.
AC Q498U4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=SAP domain-containing ribonucleoprotein;
DE AltName: Full=Nuclear protein Hcc-1;
GN Name=Sarnp; Synonyms=Hcc1;
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).
RN [2]
RP PROTEIN SEQUENCE OF 93-102; 110-119; 127-149 AND 157-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
CC -!- FUNCTION: Binds both single-stranded and double-stranded DNA with
CC higher affinity for the single-stranded form. Specifically binds to
CC scaffold/matrix attachment region DNA. Also binds single-stranded RNA.
CC Enhances RNA unwinding activity of DDX39A. May participate in important
CC transcriptional or translational control of cell growth, metabolism and
CC carcinogenesis. Component of the TREX complex which is thought to
CC couple mRNA transcription, processing and nuclear export, and
CC specifically associates with spliced mRNA and not with unspliced pre-
CC mRNA. TREX is recruited to spliced mRNAs by a transcription-independent
CC mechanism, binds to mRNA upstream of the exon-junction complex (EJC)
CC and is recruited in a splicing- and cap-dependent manner to a region
CC near the 5' end of the mRNA where it functions in mRNA export to the
CC cytoplasm via the TAP/NFX1 pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DDX39A. Interacts with FUS. Component of the
CC transcription/export (TREX) complex at least composed of ALYREF/THOC4,
CC DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have
CC dynamic structure involving ATP-dependent remodeling; in the complex
CC interacts directly with DDX39B in a ATP-dependent manner which bridges
CC it to ALYREF/THOC4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}.
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DR EMBL; BC100070; AAI00071.1; -; mRNA.
DR RefSeq; NP_001028242.1; NM_001033070.1.
DR AlphaFoldDB; Q498U4; -.
DR SMR; Q498U4; -.
DR IntAct; Q498U4; 7.
DR STRING; 10116.ENSRNOP00000009155; -.
DR iPTMnet; Q498U4; -.
DR PhosphoSitePlus; Q498U4; -.
DR jPOST; Q498U4; -.
DR PaxDb; Q498U4; -.
DR PRIDE; Q498U4; -.
DR Ensembl; ENSRNOT00000009155; ENSRNOP00000009155; ENSRNOG00000030520.
DR GeneID; 362819; -.
DR KEGG; rno:362819; -.
DR UCSC; RGD:1305692; rat.
DR CTD; 84324; -.
DR RGD; 1305692; Sarnp.
DR eggNOG; KOG0720; Eukaryota.
DR eggNOG; KOG4259; Eukaryota.
DR GeneTree; ENSGT00390000002944; -.
DR HOGENOM; CLU_073926_1_0_1; -.
DR InParanoid; Q498U4; -.
DR OMA; ETPTKKH; -.
DR OrthoDB; 1120366at2759; -.
DR PhylomeDB; Q498U4; -.
DR TreeFam; TF319843; -.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q498U4; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000030520; Expressed in thymus and 20 other tissues.
DR Genevisible; Q498U4; RN.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000346; C:transcription export complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; DNA-binding; mRNA transport;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation; Translation regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..210
FT /note="SAP domain-containing ribonucleoprotein"
FT /id="PRO_0000083918"
FT DOMAIN 8..42
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 45..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1J3"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1J3"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1J3"
SQ SEQUENCE 210 AA; 23605 MW; 9FAE0C30E62C0751 CRC64;
MATETVELHK LKLAELKQEC LARGLETKGI KQDLINRLQA YLEEHAEEEA NEEDVLGDET
EEEEPKPIEL PVKEEEPPEK VVDMASEKKV VKITSGIPQT ERMQKRAERF NVPVSLESKK
AARAARFGIS SVPTKGLSSD TKPMVNLDKL KERAQRFGLN VSSISRKSED DEKLKKRKER
FGIVTSSAGT GTTEDTEAKK RKRAERFGIA
