ID A0A2K5KV10_CERAT Unreviewed; 977 AA.
AC A0A2K5KV10;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=RNA binding motif protein 15 {ECO:0000313|Ensembl:ENSCATP00000004523.1};
GN Name=RBM15 {ECO:0000313|Ensembl:ENSCATP00000004523.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000004523.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000004523.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RRM Spen family.
CC {ECO:0000256|ARBA:ARBA00005387}.
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DR RefSeq; XP_011933721.1; XM_012078331.1.
DR AlphaFoldDB; A0A2K5KV10; -.
DR SMR; A0A2K5KV10; -.
DR STRING; 9531.ENSCATP00000004523; -.
DR Ensembl; ENSCATT00000017961.1; ENSCATP00000004523.1; ENSCATG00000015743.1.
DR GeneID; 105594365; -.
DR CTD; 64783; -.
DR GeneTree; ENSGT00940000158161; -.
DR OrthoDB; 2873387at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000015743; Expressed in bone marrow and 12 other cell types or tissues.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IEA:Ensembl.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; IEA:Ensembl.
DR GO; GO:0001510; P:RNA methylation; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR CDD; cd12553; RRM1_RBM15; 1.
DR CDD; cd12555; RRM2_RBM15; 1.
DR CDD; cd12557; RRM3_RBM15; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034470; RBM15_RRM1.
DR InterPro; IPR034472; RBM15_RRM2.
DR InterPro; IPR034473; RBM15_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR010912; SPOC_met.
DR PANTHER; PTHR23189; RNA RECOGNITION MOTIF-CONTAINING; 1.
DR PANTHER; PTHR23189:SF43; RNA-BINDING PROTEIN 15; 1.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF07744; SPOC; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR SUPFAM; SSF100939; SPOC domain-like; 1.
DR PROSITE; PS50102; RRM; 3.
DR PROSITE; PS50917; SPOC; 1.
PE 3: Inferred from homology;
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 170..252
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 374..451
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 455..529
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 777..956
FT /note="SPOC"
FT /evidence="ECO:0000259|PROSITE:PS50917"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 107151 MW; C27C6B4D274B818A CRC64;
MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VDQLRGDDLR GPATMKGKER SPVKAKRSRG
GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL DKSSSRGGSR EYDTGGGSSS
SRLHSYSSPS TKNSSGGGES RSSSRGGGGE SRSSGAASSA PGGGDGAEYK TLKISELGSQ
LSDEAVEDGL FHEFKRFGDV SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL
YDRPLKIEAV YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL
GYRDYRLQQL ALGRLPPPPP PPLPRELERE RDYPFYERVR PAYSLEPRVG AGAGAAPFRE
VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI TEVDIKRPSR GQTSTYGFLK
FENLDMSHRA KLAMSGKIII RNPIKIGYGK ATPTTRLWVG GLGPWVPLAA LAREFDRFGT
IRTIDYRKGD SWAYIQYESL DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP
LPLTHYELVT DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT
AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG RHLDRSPESD
RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS PIRDRRGSLE KSQGDKRDRK
NSASAERDRK HRTTAPTEGK SPLKKEDRSD GSAPSTSTAS CKLKSPSQKQ DGGTAPAAAA
SPKLCLAWQG MLLLKNSNFP SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP
KLDEVTRRIK VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA
AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM IIVRVFGFEI
GVRYENKKRE NMALTLL
//
