ID   SARNP_PONAB             Reviewed;         210 AA.
AC   Q5R4V4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=SAP domain-containing ribonucleoprotein;
DE   AltName: Full=Nuclear protein Hcc-1;
GN   Name=SARNP; Synonyms=HCC1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}.
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DR   EMBL; CR861137; CAH93212.1; -; mRNA.
DR   RefSeq; NP_001126889.1; NM_001133417.1.
DR   AlphaFoldDB; Q5R4V4; -.
DR   SMR; Q5R4V4; -.
DR   STRING; 9601.ENSPPYP00000005276; -.
DR   Ensembl; ENSPPYT00000055094; ENSPPYP00000044519; ENSPPYG00000004630.
DR   GeneID; 100173904; -.
DR   KEGG; pon:100173904; -.
DR   CTD; 84324; -.
DR   eggNOG; KOG0720; Eukaryota.
DR   eggNOG; KOG4259; Eukaryota.
DR   GeneTree; ENSGT00940000155637; -.
DR   HOGENOM; CLU_073926_1_0_1; -.
DR   InParanoid; Q5R4V4; -.
DR   OMA; ETPTKKH; -.
DR   OrthoDB; 1120366at2759; -.
DR   TreeFam; TF319843; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
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: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   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; mRNA transport; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Transcription; Transcription regulation;
KW   Translation regulation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P82979"
FT   CHAIN           2..210
FT                   /note="SAP domain-containing ribonucleoprotein"
FT                   /id="PRO_0000083917"
FT   DOMAIN          8..42
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   REGION          45..86
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..86
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:0000250|UniProtKB:P82979"
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;  23671 MW;  96AFDD37EA328126 CRC64;
     MATETVELHK LKLAELKQEC LARGLETKGI KQDLIHRLQA YLEEHAEEEA NEEDVLGDET
     EEEETKPIEL PVKEEEPPEK TVDVAAEKKV VKITSEIPQT ERMQKRAERF NVPVSLESKK
     AARAARFGIS SVPTKGLSSD NKPMVNLDKL KERAQRFGLN VSSISRKSED DEKLKKRKER
     FGIVTSSAGT GTTEDTEAKK RKRAERFGIA