SPKAP_MOUSE
ID SPKAP_MOUSE Reviewed; 1687 AA.
AC Q6NSW3; Q6PAM6; Q6PAP7; Q80TA7; Q80XT3; Q8BYQ9; Q8BZL6; Q8C1G7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=A-kinase anchor protein SPHKAP;
DE AltName: Full=SPHK1-interactor and AKAP domain-containing protein;
GN Name=Sphkap; Synonyms=Kiaa1678;
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] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-868 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 899-1687 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Hypothalamus, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-1687 (ISOFORM 1).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010; SER-1070; SER-1092;
RP SER-1105; SER-1106; SER-1109; SER-1244 AND SER-1273, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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: Anchoring protein that binds preferentially to the type I
CC regulatory subunit of c-AMP-dependent protein kinase (PKA type I) and
CC targets it to distinct subcellular compartments. May act as a
CC converging factor linking cAMP and sphingosine signaling pathways.
CC Plays a regulatory role in the modulation of SPHK1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via the PKA-RII subunit binding domain) with the RI
CC subunit of PKA. Interacts with SPHK1; the interaction greatly reduces
CC SPHK1 activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalizes with
CC SPHK1 in the cytoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6NSW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NSW3-2; Sequence=VSP_031714;
CC Name=3;
CC IsoId=Q6NSW3-3; Sequence=VSP_031713;
CC Name=4;
CC IsoId=Q6NSW3-4; Sequence=VSP_031713, VSP_031715, VSP_031716;
CC -!- DOMAIN: RII-binding site, predicted to form an amphipathic helix, could
CC participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AKAP110 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25605.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK034183; BAC28620.1; -; mRNA.
DR EMBL; AK038638; BAC30075.1; -; mRNA.
DR EMBL; AK019735; BAC25605.1; ALT_FRAME; mRNA.
DR EMBL; BC042654; AAH42654.1; -; mRNA.
DR EMBL; BC060165; AAH60165.1; -; mRNA.
DR EMBL; BC060217; AAH60217.1; -; mRNA.
DR EMBL; BC069832; AAH69832.1; -; mRNA.
DR EMBL; AK122538; BAC65820.1; -; mRNA.
DR CCDS; CCDS48298.1; -. [Q6NSW3-2]
DR AlphaFoldDB; Q6NSW3; -.
DR SMR; Q6NSW3; -.
DR BioGRID; 218811; 6.
DR IntAct; Q6NSW3; 2.
DR STRING; 10090.ENSMUSP00000124872; -.
DR iPTMnet; Q6NSW3; -.
DR PhosphoSitePlus; Q6NSW3; -.
DR SwissPalm; Q6NSW3; -.
DR MaxQB; Q6NSW3; -.
DR PaxDb; Q6NSW3; -.
DR PeptideAtlas; Q6NSW3; -.
DR PRIDE; Q6NSW3; -.
DR ProteomicsDB; 257321; -. [Q6NSW3-1]
DR ProteomicsDB; 257322; -. [Q6NSW3-2]
DR ProteomicsDB; 257323; -. [Q6NSW3-3]
DR ProteomicsDB; 257324; -. [Q6NSW3-4]
DR ABCD; Q6NSW3; 3 sequenced antibodies.
DR UCSC; uc007bsp.2; mouse. [Q6NSW3-1]
DR UCSC; uc007bsr.2; mouse. [Q6NSW3-4]
DR MGI; MGI:1924879; Sphkap.
DR eggNOG; ENOG502QQ6Q; Eukaryota.
DR InParanoid; Q6NSW3; -.
DR OrthoDB; 330236at2759; -.
DR PhylomeDB; Q6NSW3; -.
DR BioGRID-ORCS; 77629; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Sphkap; mouse.
DR PRO; PR:Q6NSW3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6NSW3; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0051018; F:protein kinase A binding; IPI:MGI.
DR InterPro; IPR018292; AKAP_110_C.
DR InterPro; IPR008382; SPHK1-interactor_AKAP_110.
DR PANTHER; PTHR10226; PTHR10226; 1.
DR Pfam; PF05716; AKAP_110; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1687
FT /note="A-kinase anchor protein SPHKAP"
FT /id="PRO_0000320667"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..931
FT /note="PKA-RII subunit binding domain"
FT /evidence="ECO:0000250"
FT REGION 964..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..10
FT /note="MDVNSRLSVQ -> MSTPGFLCKAMWVVEPNSATCLSAALPVKRHCQES
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031713"
FT VAR_SEQ 1533..1561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031714"
FT VAR_SEQ 1561
FT /note="N -> K (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031715"
FT VAR_SEQ 1562..1687
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031716"
FT CONFLICT 22
FT /note="P -> S (in Ref. 1; BAC28620/BAC30075)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="N -> S (in Ref. 1; BAC28620)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="P -> L (in Ref. 1; BAC28620/BAC30075)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="K -> R (in Ref. 2; AAH69832)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="D -> G (in Ref. 1; BAC28620)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="A -> G (in Ref. 1; BAC28620)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="R -> Q (in Ref. 1; BAC28620)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="V -> A (in Ref. 2; AAH69832)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="P -> L (in Ref. 2; AAH69832)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="G -> A (in Ref. 1; BAC25605)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="S -> F (in Ref. 2; AAH69832)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="S -> C (in Ref. 1; BAC30075)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="D -> G (in Ref. 2; AAH69832)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212
FT /note="S -> C (in Ref. 1; BAC30075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1687 AA; 185095 MW; DB2E129AB9036F6E CRC64;
MDVNSRLSVQ SNVESPLMHE GPEPQQITSS AAGNLAGSIT ACKKVLRSNS LLESTDYWLQ
NQRTPCQIGF VEDESENCAS VCFVNLDVNK DACITENLQQ KLVNVSPDLP NLISSMNVQQ
PKENEIVLLS GLASGNPQAD FDVSQCPWLP DICLVQCARG NRPNSTNCII FEINKFLIGL
EVVQERQLHL ETNVLKLEDD TNCSLSSIEE DFLTASEHLE EEIEVDDCRS GLENTNVSAN
VLESKKPKET TQEGWDYHKE KLHCALGEKH IRKHRTPSTK TEGSKENTEE NTSLKSLNRL
VRPSHLKSEV AGNKQLATNY SYPENIKGEL ETSQMLFIPR DAYLSMVKKD VLSPCSVLSE
QGGSHRDHDV TPNPLPPVQN GEASTGEYAT NLAESVMQDA FIRLSQSQPT LPQESAVSFS
MRSALLPSGC CTKDMVVPRS WNELPKIVIV QSPDGSDTVP EPNVSSWPDM EFVETSGIFS
ADSSSRPTQS ALEVALACAA TVIGTISSPQ ATERFAMEQE SLVSTYAQRG TGVQQTQVPQ
AFMAPSTTEY SFPSALCGMT QVASAVAVCG LCEKEEATCP VAPTDLLPTS GASEEISSIG
SLVMERSTEL GKEAIAEALL REATLILARP DAYSSLGELL ESVNQRIIET TSKTQTLCTE
SVQRNELAHT LSNVILKHSV DELHQKTTMA HPTDERHPCG TLDTLMESVN QLLHNVICFT
FKKMNHIVTL SEHPSFDQAA GQAWVKAFAC PSSQPLSNAH GTGLVIRNLV EDASPKSNKG
GARPELVNNP RLQSEFSCSH RMFDSTAKSF PKEIYLKGIM GEDTRNPHHT LNYDSNERRA
STDLGKLTTA SEGCSGFQET EDSIVPNTQE KYICATPLNN EAQVNLSLLG DDLSVPAQST
LEAKQSEVYG ITDFAEELAE TVVSMATEIA AICLDNSNGK QPWFCAWKRG NEFLTAPNGS
CRSLKRKKEN SSAGSTVRKH KPPRLSEIKR KADEHPELKE KLMNRVMDES MNLEDIPDSV
STFANEVAAK IMNLTEFSMV DGVWQGQSCS RTRLLGGDRW NRLKASSCES IPEEDSEARV
FVNSLGLMST LSQPVSRASS VSKQSSCESI TDEFSRFMVK QMENEGRGFE LLLDYYAGKN
ASSIMSSAMQ QACQKNDHLN VRPSCPSKQS STESITEEFY RYMLRDIAKE SKDGASSRRS
SHDWTTGLLS PSTRSPLCYR QSSMPDSRSP CSRLTVNAPV KANSLDGFAQ NCPQDSVNVQ
PVSRASSSGL CKSDSCLYRR SGTDQITNML IHETWASSIE ALMRKNKIIA DDSEAANASP
GPVSSGSPLQ VEKNANRLAT SKGHRGPTLL VQESVDYQRK DAVTEGNHSP VSSPGKTAPV
KKPSDFDPRR ETSACHNAAG LNSPRRSLCS RDVPLIQIET DQKEECIGEP GPFLSQSGSL
EETEGHQPEE TIPDVARNED TAPSTCQSSR DSLETSGEVE VEVLKEDIPR DESRNPPSSS
EESTGSWSQL ANEEDIPDDT SSFLQLSERS MSNGNSSGTS SLGIMDLDIY QESIPSSPMI
NELVEEKEIL KEQSESIKEH ASGLPGRAAS PQRSLLVINF DLEPECPDAE LRATLQWIAA
SELGIPTIYF KKSQESRIEK FLDVVKLVQQ KSWKVGDIFH AVVQYCKLHA EQKERTPSLF
DWLLELG
