RSH3A_MOUSE
ID RSH3A_MOUSE Reviewed; 516 AA.
AC Q3UFY4; Q9D8J2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Radial spoke head protein 3 homolog A;
DE AltName: Full=A-kinase anchor protein RSPH3A;
DE AltName: Full=Radial spoke head-like protein 2A;
GN Name=Rsph3a; Synonyms=Rshl2, Rshl2a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Functions as a protein kinase A-anchoring protein that
CC scaffolds the cAMP-dependent protein kinase holoenzyme. May serve as a
CC point of convergence for MAPK and PKA signaling in cilia (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with phosphorylated MAPK1. Interacts with MEK1.
CC Interacts with PKA regulatory subunits PRKAR1A and PRKAR1B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:P12759}.
CC -!- SIMILARITY: Belongs to the flagellar radial spoke RSP3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25385.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK007979; BAB25385.1; ALT_FRAME; mRNA.
DR EMBL; AK148230; BAE28425.1; -; mRNA.
DR CCDS; CCDS49943.1; -.
DR RefSeq; NP_080065.4; NM_025789.5.
DR AlphaFoldDB; Q3UFY4; -.
DR SMR; Q3UFY4; -.
DR BioGRID; 211749; 1.
DR STRING; 10090.ENSMUSP00000095034; -.
DR iPTMnet; Q3UFY4; -.
DR PhosphoSitePlus; Q3UFY4; -.
DR MaxQB; Q3UFY4; -.
DR PaxDb; Q3UFY4; -.
DR PRIDE; Q3UFY4; -.
DR ProteomicsDB; 257044; -.
DR DNASU; 66832; -.
DR Ensembl; ENSMUST00000097423; ENSMUSP00000095034; ENSMUSG00000073471.
DR GeneID; 66832; -.
DR KEGG; mmu:66832; -.
DR UCSC; uc008ait.2; mouse.
DR CTD; 66832; -.
DR MGI; MGI:1914082; Rsph3a.
DR VEuPathDB; HostDB:ENSMUSG00000073471; -.
DR eggNOG; ENOG502QQSZ; Eukaryota.
DR GeneTree; ENSGT00390000004172; -.
DR HOGENOM; CLU_036980_4_1_1; -.
DR InParanoid; Q3UFY4; -.
DR OMA; WHYVHLS; -.
DR OrthoDB; 955313at2759; -.
DR PhylomeDB; Q3UFY4; -.
DR TreeFam; TF324184; -.
DR BioGRID-ORCS; 66832; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Rsph3a; mouse.
DR PRO; PR:Q3UFY4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3UFY4; protein.
DR Bgee; ENSMUSG00000073471; Expressed in testis and 70 other tissues.
DR ExpressionAtlas; Q3UFY4; baseline and differential.
DR Genevisible; Q3UFY4; MM.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR InterPro; IPR009290; Radial_spoke_3.
DR PANTHER; PTHR21648; PTHR21648; 1.
DR Pfam; PF06098; Radial_spoke_3; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..516
FT /note="Radial spoke head protein 3 homolog A"
FT /id="PRO_0000313742"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..369
FT /evidence="ECO:0000255"
FT COMPBIAS 214..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250"
FT CONFLICT 297
FT /note="E -> G (in Ref. 1; BAB25385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 58786 MW; 50B579E28D5C0FD2 CRC64;
MAATNIWAAL PAKKRPLHQR ARRPAGGRGR EPEVPFTTDP SGNPAGRNCL EFLPPGGTSG
CSATDGGATV PLALRPFLRE RRPLGSQHPC PWHYLQVSDY DDSLAPTCFR AHLHRRGSSS
TLNQASAMTD PNPRTAEASG LYTYSSRPRA VACQRRRHRD SILQPVEEPM SYGNIMYDRR
VIRGNTYALP TGQVPGQPDP LELQRQQQAR RRALARKRAQ EQLKPRTPEP VEGRKHVDIQ
TELYLEEIAD RIVEVDMECQ TDAFLDRPPT PLFIPAKTGK DVATQILGGE LFDFDLEVKP
MLEVLVGKTI EQSLLEVMEE EELANLRARQ YAYEEIRNVE LAEVQRLEEQ ERRHREEKER
RKKQQWEIVH KRNETLQKIS ALIFARQYLA NLLPSVFDKL RNSGFFYDPI ERDIEVGFLP
WLMNEVEKSM EHSMVGRTVL DMLIRDVVER RINDYEHKEA MPPGQKTNVI NGPNTVTDPS
VTTLHTQKPV LDRVSSQPAP SQERKPVEEG GHLMAE
