RBM27_MOUSE
ID RBM27_MOUSE Reviewed; 1060 AA.
AC Q5SFM8; E9QM85; Q6ZPT9; Q7TQK8; Q8C2X5; Q8C9A5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RNA-binding protein 27;
DE AltName: Full=Peri-implantation stem cell protein 1;
DE AltName: Full=RNA-binding motif protein 27;
GN Name=Rbm27; Synonyms=Kiaa1311;
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] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=15741184; DOI=10.1093/nar/gki269;
RA Kavanagh S.J., Schulz T.C., Davey P., Claudianos C., Russell C.,
RA Rathjen P.D.;
RT "A family of RS domain proteins with novel subcellular localization and
RT trafficking.";
RL Nucleic Acids Res. 33:1309-1322(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-1060 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-849 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-1060 (ISOFORM 3).
RC TISSUE=Olfactory epithelium;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447 AND SER-928, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, 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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15741184}. Nucleus
CC speckle {ECO:0000269|PubMed:15741184}. Note=Incorporated into the
CC nuclear speckles and to speckles proximal to the nuclear periphery.
CC Also localizes to punctate structures in the cytoplasm termed
CC cytospeckles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SFM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SFM8-2; Sequence=VSP_022462;
CC Name=3;
CC IsoId=Q5SFM8-3; Sequence=VSP_022463;
CC -!- DOMAIN: The RRM domain mediates integration into cytospeckles.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54080.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC31304.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC39993.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY461716; AAS19274.1; -; mRNA.
DR EMBL; AC125110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129330; BAC98140.1; -; mRNA.
DR EMBL; AK042613; BAC31304.2; ALT_FRAME; mRNA.
DR EMBL; AK087759; BAC39993.1; ALT_INIT; mRNA.
DR EMBL; BC054080; AAH54080.1; ALT_FRAME; mRNA.
DR CCDS; CCDS50267.1; -. [Q5SFM8-2]
DR RefSeq; NP_766214.2; NM_172626.2. [Q5SFM8-2]
DR RefSeq; XP_006525926.1; XM_006525863.2. [Q5SFM8-1]
DR AlphaFoldDB; Q5SFM8; -.
DR SMR; Q5SFM8; -.
DR BioGRID; 230393; 1.
DR IntAct; Q5SFM8; 1.
DR MINT; Q5SFM8; -.
DR STRING; 10090.ENSMUSP00000089540; -.
DR iPTMnet; Q5SFM8; -.
DR PhosphoSitePlus; Q5SFM8; -.
DR EPD; Q5SFM8; -.
DR jPOST; Q5SFM8; -.
DR MaxQB; Q5SFM8; -.
DR PeptideAtlas; Q5SFM8; -.
DR PRIDE; Q5SFM8; -.
DR ProteomicsDB; 300262; -. [Q5SFM8-1]
DR ProteomicsDB; 300263; -. [Q5SFM8-2]
DR ProteomicsDB; 300264; -. [Q5SFM8-3]
DR Ensembl; ENSMUST00000046972; ENSMUSP00000041688; ENSMUSG00000024491. [Q5SFM8-3]
DR Ensembl; ENSMUST00000091920; ENSMUSP00000089540; ENSMUSG00000024491. [Q5SFM8-2]
DR Ensembl; ENSMUST00000236240; ENSMUSP00000158063; ENSMUSG00000024491. [Q5SFM8-1]
DR GeneID; 225432; -.
DR KEGG; mmu:225432; -.
DR UCSC; uc008etr.2; mouse. [Q5SFM8-2]
DR UCSC; uc008ets.1; mouse. [Q5SFM8-3]
DR UCSC; uc008ett.1; mouse. [Q5SFM8-1]
DR CTD; 54439; -.
DR MGI; MGI:2147194; Rbm27.
DR VEuPathDB; HostDB:ENSMUSG00000024491; -.
DR eggNOG; KOG2135; Eukaryota.
DR GeneTree; ENSGT00510000046929; -.
DR HOGENOM; CLU_006190_0_0_1; -.
DR InParanoid; Q5SFM8; -.
DR OMA; CPMEHGL; -.
DR OrthoDB; 741871at2759; -.
DR TreeFam; TF319253; -.
DR BioGRID-ORCS; 225432; 12 hits in 76 CRISPR screens.
DR ChiTaRS; Rbm27; mouse.
DR PRO; PR:Q5SFM8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q5SFM8; protein.
DR Bgee; ENSMUSG00000024491; Expressed in ear vesicle and 224 other tissues.
DR Genevisible; Q5SFM8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14398; PTHR14398; 1.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..1060
FT /note="RNA-binding protein 27"
FT /id="PRO_0000273045"
FT DOMAIN 600..674
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 273..301
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 80..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 810..887
FT /evidence="ECO:0000255"
FT COMPBIAS 88..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1052
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 455
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2N5"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2N5"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2N5"
FT VAR_SEQ 427..482
FT /note="RQPMYSREHGAAASERLQLGTPPPLLAARLVPPRNLMGSSIGYHTSVSSPTP
FT LVPD -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15741184"
FT /id="VSP_022462"
FT VAR_SEQ 632..730
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022463"
FT CONFLICT 214
FT /note="S -> P (in Ref. 1; AAS19274)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="V -> L (in Ref. 4; BAC31304)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="D -> Y (in Ref. 3; BAC98140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1060 AA; 118552 MW; F2B182125E8D1333 CRC64;
MLIEDVDALK SWLAKLLEPI CDADPSALAN YVVALVKKDK PEKELKAFCA DQLDVFLQKE
TSGFVDKLFE SLYTKNYLPP LEPVKPEPKP LVQEKEEIKE EVFQEPAEEE RDTRKKKYPS
PQKSRSESSE RRTREKKRED GKWRDYERYY ERNELYREKY DWRRGRSKSR SKSRGLSRSR
SRSRGRSKDR DPNRNVEHRE RSKFKSERND LESSYVPVSA PPPSSSEQYS SGAQSIPSTV
TVIAPAHHSE NTTESWSNYY NNHSSSNSFG RNPPPKRRCR DYDERGFCVL GDLCQFDHGN
DPLVVDEVAL PSMIPFPPPP PGLPPPPPPG MLMPPMPGPG PGPGPGPGPG PGPGPGPGHS
MRLPVPQGHG QPPPSVVLPI PRPPISQSSL INSRDQPGTS AVPNLAPVGA RLPPPLPQNL
LYTVSERQPM YSREHGAAAS ERLQLGTPPP LLAARLVPPR NLMGSSIGYH TSVSSPTPLV
PDTYEPDGYN PEAPSITSSG RSQYRQFFSR AQTQRPNLIG LTSGDMDANP RAANIVIQTE
PPVPVSVNSN VTRVVLEPES RKRAISGLEG PLTKKPWLGK QGNNNQSKPG FLRKNHYTNT
KLEVKKIPQE LNNITKLNEH FSKFGTIVNI QVAFKGDPEA ALIQYLTNEE ARKAISSTEA
VLNNRFIRVL WHRENNEQPA LQSSAQILLQ QQHTLSHLSQ QHHSLPQHLH PQQVMVTQSS
PSSVHGGIQK MMGKPQTSGA YVLNKVPVKH RLGHASTNQS DTSHLLNQTG GSSGEDCPVF
STPGHPKTIY SSSNLKAPSK LCSGSKSHDV QEVLKKKQEA MKLQQDMRKK KQEMLEKQIE
CQKMLISKLE KNKNMKPEER ANIMKTLKEL GEKISQLKDE LKTSSTVSTP SKVKTKTEAQ
KELLDTELDL HKRLSSGEDT TELRKKLSQL QVEAARLGIL PVGRGKTISS QGRGRGRGRG
RGRGSLNHMV VDHRPKALPG GGFIEEEKDE LLQHFSATNQ ASKFKDRRLQ ISWHKPKVPS
ISTETEEEEV KEEETETSDL FLHDDDDEDE DEYESRSWRR
