SPKAP_RAT
ID SPKAP_RAT Reviewed; 1683 AA.
AC P0C6C0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=A-kinase anchor protein SPHKAP;
DE AltName: Full=SPHK1-interactor and AKAP domain-containing protein;
DE AltName: Full=Sphingosine kinase type 1-interacting protein;
GN Name=Sphkap; Synonyms=Skip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND POSSIBLE
RP FUNCTION.
RX PubMed=16739995; DOI=10.1021/pr0600529;
RA Scholten A., Poh M.K., van Veen T.A.B., van Breukelen B., Vos M.A.,
RA Heck A.J.R.;
RT "Analysis of the cGMP/cAMP interactome using a chemical proteomics approach
RT in mammalian heart tissue validates sphingosine kinase type 1-interacting
RT protein as a genuine and highly abundant AKAP.";
RL J. Proteome Res. 5:1435-1447(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Abundant in heart ventricle (at protein level).
CC {ECO:0000269|PubMed:16739995}.
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; AABR03068405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03070740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03072061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03069799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03068568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C6C0; -.
DR SMR; P0C6C0; -.
DR IntAct; P0C6C0; 1.
DR STRING; 10116.ENSRNOP00000022281; -.
DR iPTMnet; P0C6C0; -.
DR PhosphoSitePlus; P0C6C0; -.
DR PaxDb; P0C6C0; -.
DR PRIDE; P0C6C0; -.
DR UCSC; RGD:1311951; rat.
DR RGD; 1311951; Sphkap.
DR eggNOG; ENOG502QQ6Q; Eukaryota.
DR InParanoid; P0C6C0; -.
DR PhylomeDB; P0C6C0; -.
DR PRO; PR:P0C6C0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0051018; F:protein kinase A binding; ISO:RGD.
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 Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1683
FT /note="A-kinase anchor protein SPHKAP"
FT /id="PRO_0000320668"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..927
FT /note="PKA-RII subunit binding domain"
FT /evidence="ECO:0000250"
FT REGION 960..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1006
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
FT MOD_RES 1101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
FT MOD_RES 1102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
FT MOD_RES 1240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
FT MOD_RES 1269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NSW3"
SQ SEQUENCE 1683 AA; 184451 MW; 7C7AD04ED4D5D04D CRC64;
MDVNSRLSVQ SNVESPLMPE DSEPQQITSS AAGSLAGSIT ACKKVLRSNS LLESTDYWLQ
NQRTPCQIGF VEDESENCAS VCFVNLDVNK DGCSTENLQQ KLVNVSPDLP KLINSMNVQK
PKENEIVLLS GLASGNRQAD FDVSQCPWLP DICLVQCARG NRPNSTNCII FEINKFLIGL
EVVQERQLHL ETSVLKLEDD TNCSLSSIEE DFLTASEHLE EEIEVEDCKS GLETINVSAN
VLESKRPKEA TQEGWDYHKE ILHCALGEKH IRKHRMPSMK TERSKENTAE NTALQSLNPS
ARPSRLKSEV AGSKQPATNY SYPENIRGEI ETSQMLFIPR DAYLSMVSSC GVLTEQGSNH
RDHDATPNSL PPVQNGEATA GEYATNLAES VMQDAFIRLS QSQPTLPQES AVSFSVGSAL
LPSGCCTKDM VVPRSWNELP KIVIVQSPEG SDTAPEPSVS SWPDLEVSVE TPGIFSEESS
SRPTQSALEV ALACAATVIG TTSSPQATER FTMEQESLVS TYTQRGNGIQ QTPVPRVFMG
PSTTEYSFPS ALCGMTQVAS AVAVCGLGER EEVTYSVAPS DLLPTPGASE ERSSIGSLVT
EESTELGKEA IAEALLREAT LVLARPNAYS SVGELLESVN RRIIETTSKT QMLCTENVRR
NELAHTLSNV ILKHSIDELH QKNIMAHPTE ERHPGGTLNT LMESVNQLLH NVMCFTFRKM
NHIVTLGEHP SFDKAAGHAW VKASACSSSH PSSNAHGTGL VIRDLVEDAS PKPDKGGARP
ELVNNPRLQS EFSCSHRMLD STARTFPKEM YPKGIVGEDT RNPLHTLSYD SSEQRTSTDI
GKLTTVGEVR STFQESEDSI VPKAQEKHTC ATTLNNEAQI NLSLLGDDLV VPDQSTLEAK
QSEVYGITNF AEELAETVVS MATEIAAICL DNSHGKQPWF CAWKRGNEFL MTPNASCRSL
KRKKENSGTG STVRKHKPPR LSEIKRKADE HPELKEKLMN RVMDESMNLE DIPDSVSTFA
NEVAAKIMNL TEFSTVDGVW QTQSCSRNRL LGGDRWNRLK ASSCESIPEE DSEARVFVNS
LGLMSTLSQP VSRASSVSKQ SSCESITDEF SRFMVKQMEN EGRGFELLLD YYAGKNASSI
LNSAIQQACQ KNDHLNVRPS CPSKQSSTES ITEEFYKYML RDIAKENKDG ALSRRSSHDW
STGLLSPSAR SPLCYRQSSM PDSRSPCSRL TVNAPIKANS LDGFAQNCPQ DSINVQPVSR
ASSSGLCKSD SCLYRRSGTD QITNMLIHET WASSIEALMR KNKIIADDGE AANASPGPVS
GGSPSQVEKC ANRLVTGTGH KGPALLVQES VDYQRKDAVT EGNCSPVSSP SKMAPVKKPS
GFDPTRETSA CHNAVALKSP RRSLCSREVP LIQIETDQKE ECVGESETLL PQSGSLEEAE
GPQPEETIPD VARSEDTALS ACQSSQDSLE TREELEVDVL KEDITLDESR NPPSSSEEST
GSWSQLANEE DNPDDTSSFL QLSERSMSNG NTSGTSSLGI MDLDIYQESI PSSPMINELV
EEKEILKEQS ESVKERASGL PGRAASPQRS LLVINFDLEP ECPDAELRAT LQWIAASELG
IPTIYFKKSQ ESRIEKFLDV VKLVHQKSWK VGDIFHAVVQ YCKMHAEQKE GTPSLFDWLL
ELG
