ID   RITA1_AILME             Reviewed;         269 AA.
AC   D2HS03;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=RBPJ-interacting and tubulin-associated protein 1;
DE   AltName: Full=RBPJ-interacting and tubulin-associated protein;
GN   Name=RITA1; Synonyms=RITA; ORFNames=PANDA_014816;
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
CC   -!- FUNCTION: Tubulin-binding protein that acts as a negative regulator of
CC       Notch signaling pathway. Shuttles between the cytoplasm and the nucleus
CC       and mediates the nuclear export of RBPJ/RBPSUH, thereby preventing the
CC       interaction between RBPJ/RBPSUH and NICD product of Notch proteins
CC       (Notch intracellular domain), leading to down-regulate Notch-mediated
CC       transcription. May play a role in neurogenesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RBPJ/RBPSUH. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250}. Note=Shuttles rapidly between the cytoplasm and the
CC       nucleus. The function of centrosome localization is still unclear (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RITA family. {ECO:0000305}.
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DR   EMBL; GL193258; EFB19061.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2HS03; -.
DR   STRING; 9646.ENSAMEP00000009219; -.
DR   eggNOG; ENOG502S61Y; Eukaryota.
DR   HOGENOM; CLU_062251_0_0_1; -.
DR   InParanoid; D2HS03; -.
DR   OMA; EGPWMAK; -.
DR   OrthoDB; 1387213at2759; -.
DR   TreeFam; TF337291; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR   GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0051168; P:nuclear export; ISS:UniProtKB.
DR   InterPro; IPR031418; RITA1.
DR   PANTHER; PTHR34917; PTHR34917; 1.
DR   Pfam; PF17066; RITA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; Neurogenesis; Notch signaling pathway; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..269
FT                   /note="RBPJ-interacting and tubulin-associated protein 1"
FT                   /id="PRO_0000404584"
FT   REGION          37..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..156
FT                   /note="Interaction with RBPJ/RBPSUH"
FT                   /evidence="ECO:0000250"
FT   REGION          141..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..269
FT                   /note="Interaction with tubulin"
FT                   /evidence="ECO:0000250"
FT   MOTIF           5..17
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           92..108
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        63..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  28911 MW;  83D2573DA7651B59 CRC64;
     MKTPVELAVS GIQTLPLQHR CRGSHRVKAR ASYVDESLFG SPAGTRPTPP DFDPPWVEKA
     NRTSGVGTGT SRASGANGSC ETTSSSGSTP TLTPRKKNKY RLISHTPSYC DESLFGSRPE
     GTNWEGPWMA KGDAAKLHSL FWTPPATPRG SHSPRPRETP LRAIHPAGPS KTEPKVAADS
     QKLSTDGLDS PHPLRRERSH SLTHLNVPRT GRPPTSGPHT NGPRDPRPSP SGVTLQSPLV
     TPRARSVRIS VPATPQRGGA TQKPKPPWK