ID   SPKAP_DANRE             Reviewed;        1596 AA.
AC   Q1LV19;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=A-kinase anchor protein SPHKAP;
DE   AltName: Full=SPHK1-interactor and AKAP domain-containing protein;
GN   Name=sphkap; ORFNames=si:dkey-223n17.6, si:dkey-99o15.1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Anchoring protein that mediates the subcellular
CC       compartmentation of cAMP-dependent protein kinase (PKA type II).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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}.
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DR   EMBL; BX908751; CAK05475.1; -; Genomic_DNA.
DR   EMBL; BX649602; CAK05475.1; JOINED; Genomic_DNA.
DR   EMBL; BX649602; CAM56518.1; -; Genomic_DNA.
DR   EMBL; BX908751; CAM56518.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001076514.1; NM_001083045.1.
DR   AlphaFoldDB; Q1LV19; -.
DR   STRING; 7955.ENSDARP00000040668; -.
DR   PaxDb; Q1LV19; -.
DR   PRIDE; Q1LV19; -.
DR   Ensembl; ENSDART00000040669; ENSDARP00000040668; ENSDARG00000017429.
DR   GeneID; 100034387; -.
DR   KEGG; dre:100034387; -.
DR   CTD; 80309; -.
DR   ZFIN; ZDB-GENE-050419-32; sphkap.
DR   eggNOG; ENOG502QQ6Q; Eukaryota.
DR   GeneTree; ENSGT00940000153313; -.
DR   HOGENOM; CLU_243215_0_0_1; -.
DR   InParanoid; Q1LV19; -.
DR   OMA; NKESAGH; -.
DR   OrthoDB; 33853at2759; -.
DR   PhylomeDB; Q1LV19; -.
DR   TreeFam; TF105426; -.
DR   PRO; PR:Q1LV19; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000017429; Expressed in brain and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051018; F:protein kinase A binding; IBA:GO_Central.
DR   InterPro; IPR008382; SPHK1-interactor_AKAP_110.
DR   PANTHER; PTHR10226; PTHR10226; 3.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..1596
FT                   /note="A-kinase anchor protein SPHKAP"
FT                   /id="PRO_0000320669"
FT   REGION          214..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..846
FT                   /note="PKA-RII subunit binding domain"
FT                   /evidence="ECO:0000250"
FT   REGION          958..1022
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1328..1443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..479
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1022
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1329..1358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1359..1382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1596 AA;  174563 MW;  00B047ADBB280725 CRC64;
     MPLLFFALAG CDGSPLCGGL SQRNQFVRLA CSVTNFQSSA MFEGSESANT QEVKSESTLG
     SSLSACKKVL CSNSVLDSSE YWLKNDKTLC RIGFLEDQHD SGCPTICFVN LDRHTSDWHD
     DNYIKKLASV CPELPRLIES LGVRQPKENE ILLLSSLEPP DSCQHDPSHP QSPRTADVCL
     VHCSCGRRPT QTSSIIFEIN KFLIGLQSGQ ERQKHGRLAG QRAAEDDTNR SVSSIEEDFL
     TASEQLGEDS EEDPFRNDPE NSLMPESVKV LRAAHAQKRS EIEREDSEDS ETLCTSSNSQ
     KLSRTYSAPA RGRPTTPKQV KESAGHYATN LAESVLQDAF IRLSQDEPSF VAEAAVSVSS
     DISHSTEAPQ RARACSFELP KIVIVQSPDN SEEVTEWPEV QSHATSEHDS GNKAKAKHGT
     HPPHNSPVGH PAKPLEIALA CAASVIGTIT TPQVTEQLTL ESGEEYECED EEEESETDQG
     EYSFSSAVCG MSQVAGAVAA VDLADDSGDN EDLADMYSAS MGLLSVAQAS TAIPLHCSIA
     EGTSVEAFRA NVAEVLLREA SAVFTHRQSY SSVANFLETT HNKIVDGITN PRRPYQEQQD
     VDNFTQEISD SIFQYALEKA EKRKELEGPG KDAPNIEGFL SDCVNNLLFD VLCVTSRKIS
     DISNCNMESC DGQEGSVGYR AYEADSKAGR EALSQLQHLI EPSQAYNHGE RRSSVEKLSA
     LIGKREREQK HIQEERENEA RLKEPYRLAL NRVTATMVKE QSDLQGQLGR SDKNADSALP
     SAESSPLHMQ RGRAGGESET RQQSLSSSSG ALVALKMDSG ESKTPVTCFA EDLATTVVSM
     ATELAAICLE NSSGKQPWFC ALNGGSEGPE GLLLPCRTAA ALRRKETQNG TSVTKKHRPP
     RLSEIKRKTE EQPELMERLV NRVVDETVNL DEPTTTDPFA LFASEVTARI MNCPELSVVD
     TSKSGQSSRS RLQCERWSSR GKASSYESIP EEDADPSGTS NTLGPGNRLG HNLSRGSSIS
     KQSSCESITD EFSRFMVNQM ETEGRGFDLL LDYYAGKNAS SILAAAVQQA ASKKNGHLNV
     RTSSCLSKQS STESITEEFY RFMLKDMDKE NKDYSMTKTK EWSNSLLPPS PRTPFCIRQS
     SVPDRRSSDS RLTVNSPIKA NSFDGFAQNV HGDSLNIYPT NSVSSSGLCK SDSCLYKRGQ
     TDQITDMLIH ETWSSSIESL MRKNKIIAEP SEDSLELDSA DSQPHVQQFA NRLAADIVES
     GKSQLGGQQD VTAAACQPHI PVGERRHGFK HSRCNNSGNR PGVEHQENSC SSYSSSCVRQ
     AWRGQREVPL IHIEPDQREE ASEEKGGVET HHREASHQTQ QQSGKGSETA TKSSSDSDRV
     SSVATVPPAG VEVERRSLSA SSEESGSGSW AQIATEDDPQ EETTSSFIQL SEGNGNSSTS
     SLGLADLEGF PDFSISSNLI SEERERKTSH CQDQADVTLV VLSEVTSGLS TAGSSCQREL
     LVLNCDLEPD CVDGELRAAL QWISASELGV PALYFRKTHQ HNLTKLHRVL QLAGQKAWRV
     GDLFSAVAQF CQLHQDLELK GRPLPSLFDW ILKTKR