GKAP1_MOUSE
ID GKAP1_MOUSE Reviewed; 366 AA.
AC Q9JMB0; Q9CUD8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=G kinase-anchoring protein 1;
DE AltName: Full=cGMP-dependent protein kinase-anchoring protein of 42 kDa;
GN Name=Gkap1; Synonyms=Gkap42;
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 [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH PRKG1,
RP PHOSPHORYLATION AT SER-106, AND MUTAGENESIS OF SER-86; SER-106 AND THR-178.
RX PubMed=10671526; DOI=10.1074/jbc.275.7.4897;
RA Yuasa K., Omori K., Yanaka N.;
RT "Binding and phosphorylation of a novel male germ cell-specific cGMP-
RT dependent protein kinase-anchoring protein by cGMP-dependent protein kinase
RT Ialpha.";
RL J. Biol. Chem. 275:4897-4905(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 25-366.
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=15028281; DOI=10.1016/j.ygeno.2003.10.002;
RA Smolenski A., Schultess J., Danielewski O., Garcia Arguinzonis M.I.,
RA Thalheimer P., Kneitz S., Walter U., Lohmann S.M.;
RT "Quantitative analysis of the cardiac fibroblast transcriptome-implications
RT for NO/cGMP signaling.";
RL Genomics 83:577-587(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
RN [6]
RP FUNCTION, INTERACTION WITH IRS1, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25586176; DOI=10.1074/jbc.m114.624759;
RA Ando Y., Shinozawa Y., Iijima Y., Yu B.C., Sone M., Ooi Y., Watanaka Y.,
RA Chida K., Hakuno F., Takahashi S.;
RT "Tumor necrosis factor (TNF)-alpha-induced repression of GKAP42 protein
RT levels through cGMP-dependent kinase (cGK)-Ialpha causes insulin resistance
RT in 3T3-L1 adipocytes.";
RL J. Biol. Chem. 290:5881-5892(2015).
CC -!- FUNCTION: Regulates insulin-dependent IRS1 tyrosine phosphorylation in
CC adipocytes by modulating the availability of IRS1 to IR tyrosine
CC kinase. Its association with IRS1 is required for insulin-induced
CC translocation of SLC2A4 to the cell membrane. Involved in TNF-induced
CC impairment of insulin-dependent IRS1 tyrosine phosphorylation.
CC {ECO:0000269|PubMed:25586176}.
CC -!- SUBUNIT: Interacts with PRKG1 (PubMed:10671526). Interacts with IRS1
CC (PubMed:25586176). {ECO:0000269|PubMed:10671526,
CC ECO:0000269|PubMed:25586176}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10671526}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed in the
CC adipose tissue (at protein level) (PubMed:25586176). In the testis it
CC is restricted to spermatocytes and early round spermatids. Also
CC expressed in cardiac fibroblasts. {ECO:0000269|PubMed:15028281,
CC ECO:0000269|PubMed:25586176}.
CC -!- INDUCTION: Down-regulated by TNF in adipocytes (at protein level).
CC {ECO:0000269|PubMed:25586176}.
CC -!- SIMILARITY: Belongs to the GKAP1 family. {ECO:0000305}.
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DR EMBL; AB033130; BAA92254.1; -; mRNA.
DR EMBL; BC052347; AAH52347.1; -; mRNA.
DR EMBL; AK016588; BAB30326.1; -; mRNA.
DR CCDS; CCDS36684.1; -.
DR RefSeq; NP_062806.1; NM_019832.4.
DR RefSeq; XP_006517364.1; XM_006517301.3.
DR RefSeq; XP_011242844.1; XM_011244542.2.
DR RefSeq; XP_011242845.1; XM_011244543.2.
DR AlphaFoldDB; Q9JMB0; -.
DR SMR; Q9JMB0; -.
DR BioGRID; 207872; 3.
DR MINT; Q9JMB0; -.
DR STRING; 10090.ENSMUSP00000089169; -.
DR iPTMnet; Q9JMB0; -.
DR PhosphoSitePlus; Q9JMB0; -.
DR EPD; Q9JMB0; -.
DR MaxQB; Q9JMB0; -.
DR PaxDb; Q9JMB0; -.
DR PeptideAtlas; Q9JMB0; -.
DR PRIDE; Q9JMB0; -.
DR ProteomicsDB; 268826; -.
DR Antibodypedia; 27552; 171 antibodies from 23 providers.
DR DNASU; 56278; -.
DR Ensembl; ENSMUST00000091579; ENSMUSP00000089169; ENSMUSG00000021552.
DR GeneID; 56278; -.
DR KEGG; mmu:56278; -.
DR UCSC; uc007qtn.1; mouse.
DR CTD; 80318; -.
DR MGI; MGI:1891694; Gkap1.
DR VEuPathDB; HostDB:ENSMUSG00000021552; -.
DR eggNOG; ENOG502QUT6; Eukaryota.
DR GeneTree; ENSGT00390000008742; -.
DR HOGENOM; CLU_065161_1_0_1; -.
DR InParanoid; Q9JMB0; -.
DR OMA; RKNHQGR; -.
DR OrthoDB; 1595194at2759; -.
DR PhylomeDB; Q9JMB0; -.
DR TreeFam; TF328459; -.
DR BioGRID-ORCS; 56278; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Gkap1; mouse.
DR PRO; PR:Q9JMB0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JMB0; protein.
DR Bgee; ENSMUSG00000021552; Expressed in spermatid and 63 other tissues.
DR ExpressionAtlas; Q9JMB0; baseline and differential.
DR Genevisible; Q9JMB0; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; TAS:MGI.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR InterPro; IPR026109; GKAP1.
DR PANTHER; PTHR14899; PTHR14899; 1.
DR PRINTS; PR02083; GKINASEAP1.
PE 1: Evidence at protein level;
KW Coiled coil; Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..366
FT /note="G kinase-anchoring protein 1"
FT /id="PRO_0000315655"
FT REGION 1..95
FT /note="Interaction with IRS1"
FT /evidence="ECO:0000269|PubMed:25586176"
FT REGION 20..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..77
FT /evidence="ECO:0000255"
FT COILED 128..160
FT /evidence="ECO:0000255"
FT COILED 250..299
FT /evidence="ECO:0000255"
FT COILED 326..353
FT /evidence="ECO:0000255"
FT COMPBIAS 81..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000305|PubMed:10671526"
FT MUTAGEN 86
FT /note="S->A: Does not affect phosphorylation by PKG."
FT /evidence="ECO:0000269|PubMed:10671526"
FT MUTAGEN 106
FT /note="S->A: Affects phosphorylation by PKG."
FT /evidence="ECO:0000269|PubMed:10671526"
FT MUTAGEN 178
FT /note="T->A: Does not affect phosphorylation by PKG."
FT /evidence="ECO:0000269|PubMed:10671526"
FT CONFLICT 26
FT /note="G -> V (in Ref. 3; BAB30326)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="K -> I (in Ref. 3; BAB30326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 41763 MW; 9F8BCF183CEE37B8 CRC64;
MASAVLSSVL TTASRFALLQ VDSGSGSDSE PGKGKGRSNG KSQTLGNKAT SNEKKREKRR
KKKEQQQSEA NELRNLAFKK IPQKSSHSIC NVQHELSSPN PAQKESREEN WQEWRQKDEQ
LTSEMFEADL EKALLLSKLE YEEHKQDYEN AETASTQTKG INKKDKRKNH QGKDKPVTVS
LKDFQCEDHI SKKAEESNSA QTLSHDGGFF NRLEDDVHKI LIREKRREQL TEHNGTDNSP
APEHNQEVGL KDGRIERLKL ELERKDAEIQ KLKAVITQWE AKYKEVKARN GQLLKMLQEG
EMKDKAEILL QVDESQSIKN ELTVQVSSLH AALEQERSKV KVLQAELAKY QGGRKGKRNF
EPDHCR
