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AK17B_MOUSE
ID   AK17B_MOUSE             Reviewed;         959 AA.
AC   A2A3V1; B0QZD2; Q0P534; Q8BR01; Q8C6P6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=A-kinase anchor protein 17B;
DE            Short=AKAP-17B;
DE   AltName: Full=Protein Talia;
DE   AltName: Full=Protein kinase A-anchoring protein 17B;
DE            Short=PRKA17B;
DE   AltName: Full=Splicing factor, arginine/serine-rich 17B;
GN   Name=Akap17b; Synonyms=Sfrs17b;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-304.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Oviduct;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-959.
RC   TISSUE=Brain;
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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17302988; DOI=10.1186/1471-213x-7-8;
RA   Frankenberg S., Smith L., Greenfield A., Zernicka-Goetz M.;
RT   "Novel gene expression patterns along the proximo-distal axis of the mouse
RT   embryo before gastrulation.";
RL   BMC Dev. Biol. 7:8-8(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671 AND SER-678, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Splice factor regulating alternative splice site selection
CC       for certain mRNA precursors. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Component of the spliceosome (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:17302988}.
CC   -!- DEVELOPMENTAL STAGE: Uniformally expressed in the extraembryonic
CC       ectoderm at 5.5 dpc. Restricted to the distal part of the
CC       extraembryonic ectoderm at 6.5 dpc-7.5 dpc.
CC       {ECO:0000269|PubMed:17302988}.
CC   -!- MISCELLANEOUS: 'Talia' means 'waistline' in Polish.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35651.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAQ12496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL450397; CAM13291.2; -; Genomic_DNA.
DR   EMBL; AL450397; CAQ12496.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK046007; BAC32570.2; -; mRNA.
DR   EMBL; AK054091; BAC35651.1; ALT_FRAME; mRNA.
DR   EMBL; BC120735; AAI20736.1; -; mRNA.
DR   EMBL; BC131917; AAI31918.1; -; mRNA.
DR   CCDS; CCDS40924.1; -.
DR   RefSeq; NP_001075425.1; NM_001081956.1.
DR   RefSeq; XP_006541446.1; XM_006541383.3.
DR   RefSeq; XP_006541447.1; XM_006541384.3.
DR   RefSeq; XP_017174021.1; XM_017318532.1.
DR   AlphaFoldDB; A2A3V1; -.
DR   STRING; 10090.ENSMUSP00000052042; -.
DR   iPTMnet; A2A3V1; -.
DR   PhosphoSitePlus; A2A3V1; -.
DR   EPD; A2A3V1; -.
DR   PaxDb; A2A3V1; -.
DR   PeptideAtlas; A2A3V1; -.
DR   PRIDE; A2A3V1; -.
DR   ProteomicsDB; 282058; -.
DR   Ensembl; ENSMUST00000051906; ENSMUSP00000052042; ENSMUSG00000059708.
DR   GeneID; 338351; -.
DR   KEGG; mmu:338351; -.
DR   UCSC; uc009sxp.1; mouse.
DR   CTD; 338351; -.
DR   MGI; MGI:2443758; Akap17b.
DR   VEuPathDB; HostDB:ENSMUSG00000059708; -.
DR   eggNOG; KOG2891; Eukaryota.
DR   GeneTree; ENSGT00440000039314; -.
DR   HOGENOM; CLU_356770_0_0_1; -.
DR   InParanoid; A2A3V1; -.
DR   OMA; HLPNQEE; -.
DR   OrthoDB; 635256at2759; -.
DR   TreeFam; TF320443; -.
DR   BioGRID-ORCS; 338351; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Akap17b; mouse.
DR   PRO; PR:A2A3V1; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; A2A3V1; protein.
DR   Bgee; ENSMUSG00000059708; Expressed in animal zygote and 244 other tissues.
DR   ExpressionAtlas; A2A3V1; baseline and differential.
DR   Genevisible; A2A3V1; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0051018; F:protein kinase A binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Spliceosome.
FT   CHAIN           1..959
FT                   /note="A-kinase anchor protein 17B"
FT                   /id="PRO_0000343419"
FT   DOMAIN          145..253
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          284..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          261..334
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        284..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..331
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        126
FT                   /note="E -> K (in Ref. 2; BAC35651)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   959 AA;  111066 MW;  B8663A72ECD8F434 CRC64;
     MTVTVVYDNS EATELCAAQH LYLKPIAKLM INVLLPECIE PVRPFSNWEV LDQLKSLICP
     DQFTTVRLSK STKDFIRFEG EAETRSLVQI LKAKLHGKII KLNGLKTDLK VVATDAQGEW
     EHFPKEKEAS VIEGAEEQDH DKGPDSIYFE GLPCKWFAPK GSSGEKPCEE ILRVVFESFG
     KIKNVDIPML DPYREVMTGG SFGGLNFGLQ TFEAFIQYQE STDFIKAMES LRGMKLMLKG
     DDGKALACNI KVMFDTTKHF SEGAIQRRNQ ERLKLQELEE ERKKEKKREE EVAERKRKDE
     VRKAQEKRKK ARDRRRALKE RDRHRQRKEK VKTKPEARQE LDSSGEWEER KYLLARRRVE
     ALRLLRVLLK KIAVWMRKEK NLKPCQTHIS LLLNCLGSTQ CNPQEVGVMK SEAHHTPGTA
     LKSPEEEELN TRHLLDWEEM PSYQASTLDL SQKAEKRCYQ ASKSDNKQKQ KGKKKTKAQL
     QKSSHTPGVK QMRHSARKEE TGKVLSDGCD YSLVSDQNSL QSTMIADQSL AKEDHASSNE
     SHSSRQAVIN RGRKQKIYET DEFIDYLLNY YQTPEYARFC LEASHLTSTC QWQRDVYAKG
     DGFQIYLRKQ GYHSNSLSEE ESLQGIEQDE EQDWPQVYIK DPESKSQKTG KINYAKEFTK
     KLKNHCKDIA SETDEHLSPT DGESYPVEKI HSHGVKDSQH IRKSPVSSSL RSVDVGLPLA
     DFLEEISSDS ECFSETLSMN QEEEERSMAV YNSSPEKRPL GTDKISTCKQ KTKSSQQTLC
     SEWKHDNEGK YSKHRVRAPG KRSKSELRYS WLEEEGDSIR VDKNISKTRG KLAPKHMLDE
     GQYHESSSSD ELESTTRKKR RLTSGMFDQN VKYRPLHMPS MPPKRARAFY LGYFSRKRQT
     PWKSEYNQDV RRFKRYENSE DYTLDSDNYY VSHDDNQEHI EYGSYLGDSY SSSLYFKMF
 
 
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