FA50A_MOUSE
ID FA50A_MOUSE Reviewed; 339 AA.
AC Q9WV03; Q9D866;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein FAM50A;
DE AltName: Full=Protein XAP-5;
GN Name=Fam50a; Synonyms=D0HXS9928E, Xap5;
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 [MRNA].
RX PubMed=10534398; DOI=10.1006/geno.1999.5931;
RA Sedlack Z., Muenstermann E., Dhorne-Pollet S., Otto C., Bock D.,
RA Schuetz G., Poustka A.;
RT "Human and mouse XAP-5 and XAP-5-like (X5L) genes: identification of an
RT ancient functional retroposon differentially expressed in testis.";
RL Genomics 61:125-132(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: Probably involved in the regulation of pre-mRNA splicing.
CC {ECO:0000250|UniProtKB:Q14320}.
CC -!- SUBUNIT: Interacts with EFTUD2, a component of the spliceosome U5
CC complex. Interacts with DDX41, a component of the spliceosome C
CC complex. {ECO:0000250|UniProtKB:Q14320}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14320}.
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues.
CC -!- SIMILARITY: Belongs to the FAM50 family. {ECO:0000305}.
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; Y18505; CAB46282.1; -; mRNA.
DR EMBL; AK008402; BAB25651.1; -; mRNA.
DR CCDS; CCDS41021.1; -.
DR RefSeq; NP_613073.2; NM_138607.3.
DR AlphaFoldDB; Q9WV03; -.
DR STRING; 10090.ENSMUSP00000109797; -.
DR iPTMnet; Q9WV03; -.
DR PhosphoSitePlus; Q9WV03; -.
DR EPD; Q9WV03; -.
DR MaxQB; Q9WV03; -.
DR PaxDb; Q9WV03; -.
DR PeptideAtlas; Q9WV03; -.
DR PRIDE; Q9WV03; -.
DR ProteomicsDB; 271842; -.
DR Antibodypedia; 488; 198 antibodies from 29 providers.
DR DNASU; 108160; -.
DR Ensembl; ENSMUST00000114160; ENSMUSP00000109797; ENSMUSG00000001962.
DR GeneID; 108160; -.
DR KEGG; mmu:108160; -.
DR UCSC; uc009ton.2; mouse.
DR CTD; 9130; -.
DR MGI; MGI:1351626; Fam50a.
DR VEuPathDB; HostDB:ENSMUSG00000001962; -.
DR eggNOG; KOG2894; Eukaryota.
DR GeneTree; ENSGT00390000004735; -.
DR HOGENOM; CLU_037985_1_1_1; -.
DR InParanoid; Q9WV03; -.
DR OMA; DFIWVFL; -.
DR OrthoDB; 1061864at2759; -.
DR PhylomeDB; Q9WV03; -.
DR TreeFam; TF314738; -.
DR BioGRID-ORCS; 108160; 25 hits in 75 CRISPR screens.
DR PRO; PR:Q9WV03; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9WV03; protein.
DR Bgee; ENSMUSG00000001962; Expressed in saccule of membranous labyrinth and 262 other tissues.
DR ExpressionAtlas; Q9WV03; baseline and differential.
DR Genevisible; Q9WV03; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR007005; XAP5.
DR PANTHER; PTHR12722; PTHR12722; 1.
DR Pfam; PF04921; XAP5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14320"
FT CHAIN 2..339
FT /note="Protein FAM50A"
FT /id="PRO_0000068285"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..155
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..31
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:Q14320"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14320"
FT CONFLICT 46
FT /note="D -> Y (in Ref. 2; BAB25651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 40252 MW; B7E700854B06F771 CRC64;
MAQYKGAASE AGRAMHLMKK REKQREQMEQ MKQRIAEENI MKSNIDKKFS AHYDAVEAEL
KSSTVGLVTL NDMKAKQEAL VKEREKQLAK KEQSKELQLK LEKLREKERK KEAKRKISSL
SFTLEEEEEG VEEEEEMAMY EEELEREEIT TKKKKLGKNP DVDTSFLPDR DREEEENRLR
EELRQEWEAK QEKIKSEEIE ITFSYWDGSG HRRTVKMKKG NTMQQFLQKA LEILRKDFSE
LRSAGVEQLM YIKEDLIIPH HHSFYDFIVT KARGKSGPLF NFDVHDDVRL LSDATVEKDE
SHAGKVVLRS WYEKNKHIFP ASRWEPYDPE KKWDKYTIR
