UNC50_RAT
ID UNC50_RAT Reviewed; 259 AA.
AC O55227;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein unc-50 homolog;
DE AltName: Full=Uncoordinated-like protein;
GN Name=Unc50; Synonyms=Uncl;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND RNA-BINDING.
RX PubMed=10980252; DOI=10.1016/s0006-8993(00)02692-5;
RA Fitzgerald J., Kennedy D., Viseshakul N., Cohen B.N., Mattick J.,
RA Bateman J.F., Forsayeth J.R.;
RT "UNCL, the mammalian homologue of UNC-50, is an inner nuclear membrane RNA-
RT binding protein.";
RL Brain Res. 877:110-123(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu L.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=17004066; DOI=10.1007/s00441-006-0304-3;
RA Kim H.-J., Choi Y.S., Jeong M.-J., Kim B.-O., Lim S.-H., Kim D.K.,
RA Kim C.K., Park J.-C.;
RT "Expression of UNCL during development of periodontal tissue and response
RT of periodontal ligament fibroblasts to mechanical stress in vivo and in
RT vitro.";
RL Cell Tissue Res. 327:25-31(2007).
CC -!- FUNCTION: Involved in the cell surface expression of neuronal nicotinic
CC receptors (PubMed:10980252). Binds RNA (PubMed:10980252).
CC {ECO:0000269|PubMed:10980252}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:10980252}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10980252}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney and testis, and at lower
CC levels in heart. {ECO:0000269|PubMed:10980252}.
CC -!- DEVELOPMENTAL STAGE: Not present in the maxillary first molar tooth
CC before E18. Present at high levels in ameloblasts and adjacent cells at
CC P7. At P14, present in differentiating pre-cementoblasts and pre-
CC osteoblasts along the developing root surface and alveolar bone. At
CC P28, present in cementoblastic cells in the periodontal ligament and
CC osteoblastic cells on the alveolar bone surface (at protein level).
CC {ECO:0000269|PubMed:17004066}.
CC -!- INDUCTION: By mechanical tensile force in periodontal ligament
CC fibroblasts. {ECO:0000269|PubMed:17004066}.
CC -!- SIMILARITY: Belongs to the unc-50 family. {ECO:0000305}.
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DR EMBL; U96638; AAB93932.1; -; mRNA.
DR EMBL; AY017209; AAK08985.1; -; mRNA.
DR EMBL; BC061976; AAH61976.1; -; mRNA.
DR RefSeq; NP_620274.1; NM_138919.2.
DR RefSeq; XP_006244798.1; XM_006244736.3.
DR RefSeq; XP_006244799.1; XM_006244737.3.
DR AlphaFoldDB; O55227; -.
DR STRING; 10116.ENSRNOP00000024582; -.
DR PaxDb; O55227; -.
DR Ensembl; ENSRNOT00000024582; ENSRNOP00000024582; ENSRNOG00000018128.
DR GeneID; 192356; -.
DR KEGG; rno:192356; -.
DR UCSC; RGD:621749; rat.
DR CTD; 25972; -.
DR RGD; 621749; Unc50.
DR eggNOG; KOG3012; Eukaryota.
DR GeneTree; ENSGT00390000018553; -.
DR HOGENOM; CLU_066239_0_0_1; -.
DR InParanoid; O55227; -.
DR OMA; ISTLMWV; -.
DR OrthoDB; 1351297at2759; -.
DR PhylomeDB; O55227; -.
DR TreeFam; TF105624; -.
DR PRO; PR:O55227; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018128; Expressed in stomach and 20 other tissues.
DR Genevisible; O55227; RN.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
DR InterPro; IPR007881; UNC-50.
DR PANTHER; PTHR12841; PTHR12841; 1.
DR Pfam; PF05216; UNC-50; 1.
PE 1: Evidence at protein level;
KW Acetylation; Golgi apparatus; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="Protein unc-50 homolog"
FT /id="PRO_0000308963"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..115
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..187
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..259
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q53HI1"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HI1"
SQ SEQUENCE 259 AA; 30436 MW; AD0D4799544D0D87 CRC64;
MLPSTSLNSS MYGNGALNSR DAARHTAGAK RYKYLRRLFR FRQMDFEFAA WQMLYLFTSP
QRVYRNFHYR KQTKDQWARD DPAFLVLLSI WLCVSTIGFG FVLDMGFFET IKLLLWVVFI
DCVGVGLLIS TLMWFISNKY LVKRQSRDYD VEWGYAFDVH LNAFYPLLVI LHFIQLFFIN
HVILTDTFIG YLVGNTLWLI AVGYYIYVTF LGYSALPFLK NTVVLLYPFA PLIVLYGLSL
ALGWNFTHTL CSFYKYRVK
