RBMS1_RAT
ID RBMS1_RAT Reviewed; 403 AA.
AC Q5PQP1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RNA-binding motif, single-stranded-interacting protein 1;
GN Name=Rbms1 {ECO:0000312|EMBL:AAH87094.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH87094.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000312|EMBL:AAH87094.1};
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).
CC -!- FUNCTION: Single-stranded DNA binding protein that interacts with the
CC region upstream of the MYC gene. Binds specifically to the DNA sequence
CC motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P29558}.
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DR EMBL; BC087094; AAH87094.1; -; mRNA.
DR RefSeq; NP_001012184.1; NM_001012184.1.
DR AlphaFoldDB; Q5PQP1; -.
DR SMR; Q5PQP1; -.
DR STRING; 10116.ENSRNOP00000011682; -.
DR jPOST; Q5PQP1; -.
DR PaxDb; Q5PQP1; -.
DR PRIDE; Q5PQP1; -.
DR GeneID; 362138; -.
DR KEGG; rno:362138; -.
DR UCSC; RGD:1307777; rat.
DR CTD; 5937; -.
DR RGD; 1307777; Rbms1.
DR VEuPathDB; HostDB:ENSRNOG00000008482; -.
DR eggNOG; KOG4733; Eukaryota.
DR InParanoid; Q5PQP1; -.
DR OrthoDB; 810893at2759; -.
DR PRO; PR:Q5PQP1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000008482; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; Q5PQP1; baseline and differential.
DR Genevisible; Q5PQP1; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd12470; RRM1_MSSP1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR034404; MSSP1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW DNA replication; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..403
FT /note="RNA-binding motif, single-stranded-interacting
FT protein 1"
FT /id="PRO_0000293625"
FT DOMAIN 62..135
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 141..226
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 30..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29558"
SQ SEQUENCE 403 AA; 44068 MW; 4DAE522D5B53545A CRC64;
MGKVWKQQMY PQYATYYYPQ YLQAKQSLVP AHPMAPPSPS TTSSNNNSSS SSNSGWDQLS
KTNLYIRGLP PNTTDQDLVK LCQPYGKIVS TKAILDKATN KCKGYGFVDF DSPAAAQKAV
SALKASGVQA QMAKQQEQDP TNLYISNLPL SMDEQELENM LKPFGQVIST RVLRDSSGTS
RGVGFARMES TEKCEAVIGH FNGKFIKTPP GVSAPTEPLL CKFADGGQKK RQNPNKYIPN
GRPWPREGEA GMTLTYDPTT AALHNGFYPS PYSIATNRMI TQTSLTPYIA SPVSAYQVQS
PSWMQPQPYI LQHPGAVLTP SMEHTMSLQP ASMISPLAQQ MSHLSLGSTG TYMPATSAMQ
GAYLPQYTHM QTATVPVEEA SGQQQVTVET SNDHSPYTFP PNK