ID A0A2K6SYJ3_SAIBB Unreviewed; 984 AA.
AC A0A2K6SYJ3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=RNA binding motif protein 10 {ECO:0000313|Ensembl:ENSSBOP00000012435.1};
GN Name=RBM10 {ECO:0000313|Ensembl:ENSSBOP00000012435.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000012435.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000012435.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A2K6SYJ3; -.
DR STRING; 39432.ENSSBOP00000012435; -.
DR Ensembl; ENSSBOT00000029225.1; ENSSBOP00000012435.1; ENSSBOG00000022873.1.
DR GeneTree; ENSGT00940000160369; -.
DR OMA; RQHTDWS; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IEA:Ensembl.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1905288; P:vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR CDD; cd16167; OCRE_RBM10; 1.
DR CDD; cd12753; RRM1_RBM10; 1.
DR CDD; cd12754; RRM2_RBM10; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR035618; RBM10_OCRE.
DR InterPro; IPR034992; RBM10_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948; RNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR13948:SF4; RNA-BINDING PROTEIN 10; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 188..268
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 271..301
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 359..452
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 813..843
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 912..958
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 109327 MW; 33CDE6D28D867628 CRC64;
MSGSPPLTAR AEKVSVDAES LQEESPRLAD HGSSSGGGWE VKRSQRLRRG PSSPRRSYQD
MEYERRGGRG DRTGRYGATD RSQDDGENRS RDHDYRDMDY RSYPREYGSQ EGKHDYDDSS
EEQSAEDSYE ASPGSETQRR RRRRHRHSPT GPPGFPRDGD YRDQDYRTEQ GEEDEEEEDE
EEEEKASNIV MLRMLPQAAT EDDIRGQLQS HGVQAREVRL MRNKSSGQSR GFAFVEFSHL
QDATRWMEAN QHSLSILGQK VSMHYSDPKP KINEDWLCNK CGVQNFKRRE KCFKCGVPKS
EAEQKLPLGT RLDQQTLPLG GRELSQGLLP LPQPYQAQGV LASQSLSQGS EPSSENANDT
IILRNLNPHS TMDSILGALA PYAVLSSSNV RVIKDKQTQL NRGFAFIQLS TIVVRAAQLG
AGQSLPPLLP QEALHPPLTI DGKTINVEFA KGSKRDMASN EGSRISAASV ASTAIAAAQW
AISQASQGGE GAWATSEEPP VDYSYYQQDE GYGNSQGTES SLYAHGYLKG TKGPGITGTK
GDPTGAGPEA SLEPGADSLS LQAFSRAQPG AAPGIYQQSA EASSSQGTAA NSQSYTIMSP
AVLKSELQSP THPSSALPPA TSPTAQESYS QYPVPDVSTY QYDETSGYYY DPQTGLYYDP
NSQYYYNAQS QQYLYWDGER RTYVPALEQS ADGHKETGAP SKEGKEKKEK HKTKTAQQIA
KDMERWARSL NKQKENFKNS FQPISSLRDD ERRESATADA GYAILEKKVC WSHPPALCGV
PEFLSYSGES DSEEEQERGG PEREEKLTDW QKLACLLCRR QFPSKEALIR HQQLSGLHKQ
NLEIHRRAHL SENELEALEK NDMEQMKYRD RAAERREKYG IPEPPEPKRR KYGGISTASV
DFEQPTRDGL GSDNIGSRML QAMGWKEGSG LGRKKQGIVT PIEAQTRVRG SGLGARGSSY
GVTSTESYKE TLHKTMVTRF NEAQ
//
