ID   SARNP_MOUSE             Reviewed;         210 AA.
AC   Q9D1J3; Q3UJZ4; Q9CU18;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=SAP domain-containing ribonucleoprotein;
DE   AltName: Full=Nuclear protein Hcc-1;
GN   Name=Sarnp; Synonyms=Hcc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-10 AND LYS-142, CLEAVAGE
RP   OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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; AK003453; BAB22799.1; -; mRNA.
DR   EMBL; AK018773; BAB31400.1; -; mRNA.
DR   EMBL; AK088266; BAC40246.1; -; mRNA.
DR   EMBL; AK146248; BAE27010.1; -; mRNA.
DR   EMBL; BC027510; AAH27510.1; -; mRNA.
DR   CCDS; CCDS36092.1; -.
DR   RefSeq; NP_079640.1; NM_025364.2.
DR   AlphaFoldDB; Q9D1J3; -.
DR   SMR; Q9D1J3; -.
DR   BioGRID; 211227; 27.
DR   STRING; 10090.ENSMUSP00000100863; -.
DR   GlyGen; Q9D1J3; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q9D1J3; -.
DR   PhosphoSitePlus; Q9D1J3; -.
DR   SwissPalm; Q9D1J3; -.
DR   EPD; Q9D1J3; -.
DR   jPOST; Q9D1J3; -.
DR   MaxQB; Q9D1J3; -.
DR   PaxDb; 10090-ENSMUSP00000100863; -.
DR   ProteomicsDB; 256596; -.
DR   Pumba; Q9D1J3; -.
DR   Antibodypedia; 15547; 235 antibodies from 31 providers.
DR   DNASU; 66118; -.
DR   Ensembl; ENSMUST00000105230.4; ENSMUSP00000100863.3; ENSMUSG00000078427.4.
DR   GeneID; 66118; -.
DR   KEGG; mmu:66118; -.
DR   UCSC; uc007hor.2; mouse.
DR   AGR; MGI:1913368; -.
DR   CTD; 84324; -.
DR   MGI; MGI:1913368; Sarnp.
DR   VEuPathDB; HostDB:ENSMUSG00000078427; -.
DR   eggNOG; KOG0720; Eukaryota.
DR   eggNOG; KOG4259; Eukaryota.
DR   GeneTree; ENSGT00390000002944; -.
DR   HOGENOM; CLU_073926_1_0_1; -.
DR   InParanoid; Q9D1J3; -.
DR   OMA; ETPTKKH; -.
DR   OrthoDB; 5403910at2759; -.
DR   PhylomeDB; Q9D1J3; -.
DR   TreeFam; TF319843; -.
DR   Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-MMU-72187; mRNA 3'-end processing.
DR   Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR   BioGRID-ORCS; 66118; 13 hits in 78 CRISPR screens.
DR   ChiTaRS; Sarnp; mouse.
DR   PRO; PR:Q9D1J3; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9D1J3; Protein.
DR   Bgee; ENSMUSG00000078427; Expressed in ventricular zone and 71 other cell types or tissues.
DR   ExpressionAtlas; Q9D1J3; baseline and differential.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000346; C:transcription export complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
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; SAP domain; 1.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   PANTHER; PTHR46551; SAP DOMAIN-CONTAINING RIBONUCLEOPROTEIN; 1.
DR   PANTHER; PTHR46551:SF1; SAP DOMAIN-CONTAINING RIBONUCLEOPROTEIN; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   Genevisible; Q9D1J3; MM.
PE   1: Evidence at protein 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:0007744|PubMed:23806337"
FT   CHAIN           2..210
FT                   /note="SAP domain-containing ribonucleoprotein"
FT                   /id="PRO_0000083919"
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          162..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:0007744|PubMed:23806337"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         142
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   210 AA;  23533 MW;  15705691F989E9AB CRC64;
     MAAETVELHK LKLAELKQEC LARGLETKGI KQDLINRLQA YLEDHAEEEA NEEDVLGDET
     EEEEPKPIEL PVKEEEPPEK AVDMASEKKV VKITSGIPQT ERMQKRAERF NVPVSLESKK
     AARAARFGIS SVPTKGLSSD TKPMVNLDKL KERAQRFGLN VSSISRKSED DEKLKKRKER
     FGIVTSSAGT GTTEDTEAKK RKRAERFGIA
//