ID AKAP3_MOUSE Reviewed; 864 AA. AC O88987; Q497M9; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 2. DT 02-OCT-2024, entry version 150. DE RecName: Full=A-kinase anchor protein 3 {ECO:0000305}; DE Short=AKAP-3 {ECO:0000305}; DE AltName: Full=A-kinase anchor protein 110 kDa {ECO:0000303|PubMed:10319321}; DE Short=AKAP 110 {ECO:0000303|PubMed:10319321}; DE AltName: Full=Protein kinase A-anchoring protein 3; DE Short=PRKA3; GN Name=Akap3 {ECO:0000303|PubMed:31969357, ECO:0000312|MGI:MGI:1341149}; GN Synonyms=Akap110 {ECO:0000303|PubMed:10319321}; 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]. RC TISSUE=Testis; RX PubMed=10319321; DOI=10.1210/mend.13.5.0278; RA Vijayaraghavan S., Liberty G.A., Mohan J., Winfrey V.P., Olson G.E., RA Carr D.W.; RT "Isolation and molecular characterization of AKAP110, a novel, sperm- RT specific protein kinase A-anchoring protein."; RL Mol. Endocrinol. 13:705-717(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] RP SUBCELLULAR LOCATION. RX PubMed=11278869; DOI=10.1074/jbc.m011252200; RA Carr D.W., Fujita A., Stentz C.L., Liberty G.A., Olson G.E., Narumiya S.; RT "Identification of sperm-specific proteins that interact with A-kinase RT anchoring proteins in a manner similar to the type II regulatory subunit of RT PKA."; RL J. Biol. Chem. 276:17332-17338(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=31969357; DOI=10.1242/dev.181057; RA Xu K., Yang L., Zhang L., Qi H.; RT "Lack of AKAP3 disrupts integrity of the subcellular structure and proteome RT of mouse sperm and causes male sterility."; RL Development 147:0-0(2020). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=37709195; DOI=10.1016/j.jgg.2023.09.002; RA Wang Y., Huang X., Sun G., Chen J., Wu B., Luo J., Tang S., Dai P., RA Zhang F., Li J., Wang L.; RT "Coiled-coil domain-containing 38 is required for acrosome biogenesis and RT fibrous sheath assembly in mice."; RL J. Genet. Genomics 0:0-0(2023). RN [8] RP PHOSPHORYLATION AT SER-12. RX PubMed=37146716; DOI=10.1016/j.mcpro.2023.100564; RA Yu W., Li Y., Chen H., Cui Y., Situ C., Yao L., Zhang X., Lu S., Liu L., RA Li L., Ren J., Guo Y., Huo Z., Chen Y., Li H., Jiang T., Gu Y., Wang C., RA Zhu T., Li Y., Hu Z., Guo X.; RT "STK33 phosphorylates fibrous sheath protein AKAP3/4 to regulate sperm RT flagella assembly in spermiogenesis."; RL Mol. Cell. Proteomics 22:100564-100564(2023). CC -!- FUNCTION: Structural component of sperm fibrous sheath CC (PubMed:31969357). Required for the formation of the subcellular CC structure of the sperm flagellum, sperm motility and male fertility CC (PubMed:31969357). {ECO:0000269|PubMed:31969357}. CC -!- SUBUNIT: Interacts with ROPN1 and ROPN1L. Interacts with QRICH2. CC {ECO:0000250|UniProtKB:O75969}. CC -!- INTERACTION: CC O88987; Q99MP8: Brap; NbExp=3; IntAct=EBI-9033539, EBI-10818333; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome CC {ECO:0000269|PubMed:11278869}. Cell projection, cilium, flagellum CC {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:31969357, CC ECO:0000269|PubMed:37709195}. Note=Dorsal margin of the acrosomal CC segment (PubMed:11278869). Ribs of the fibrous sheath in the principal CC piece of the sperm tail (PubMed:11278869, PubMed:31969357, CC PubMed:37709195). {ECO:0000269|PubMed:11278869, CC ECO:0000269|PubMed:31969357, ECO:0000269|PubMed:37709195}. 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|UniProtKB:O75969}. CC -!- PTM: Phosphorylated by STK33 during sperm flagella assembly CC (PubMed:37146716). Phosphorylated on tyrosine (By similarity). CC {ECO:0000250|UniProtKB:O75969, ECO:0000269|PubMed:37146716}. CC -!- DISRUPTION PHENOTYPE: Male mice are sterile due to sperm morphology CC abnormalities (PubMed:31969357). The absence of Akap3 affects the CC integrity of sperm structure, causing mislocalizations of sperm CC proteins (PubMed:31969357). {ECO:0000269|PubMed:31969357}. CC -!- SIMILARITY: Belongs to the AKAP110 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF093406; AAC63369.1; -; mRNA. DR EMBL; CH466523; EDK99845.1; -; Genomic_DNA. DR EMBL; BC100458; AAI00459.1; -; mRNA. DR CCDS; CCDS20558.1; -. DR RefSeq; NP_033780.2; NM_009650.2. DR AlphaFoldDB; O88987; -. DR SMR; O88987; -. DR BioGRID; 198050; 1. DR IntAct; O88987; 2. DR STRING; 10090.ENSMUSP00000093091; -. DR iPTMnet; O88987; -. DR PhosphoSitePlus; O88987; -. DR SwissPalm; O88987; -. DR PaxDb; 10090-ENSMUSP00000093091; -. DR PeptideAtlas; O88987; -. DR ProteomicsDB; 296150; -. DR Antibodypedia; 22296; 205 antibodies from 33 providers. DR DNASU; 11642; -. DR Ensembl; ENSMUST00000095440.9; ENSMUSP00000093091.6; ENSMUSG00000030344.12. DR Ensembl; ENSMUST00000202574.2; ENSMUSP00000144405.2; ENSMUSG00000030344.12. DR Ensembl; ENSMUST00000202878.4; ENSMUSP00000143794.2; ENSMUSG00000030344.12. DR GeneID; 11642; -. DR KEGG; mmu:11642; -. DR UCSC; uc009dvf.2; mouse. DR AGR; MGI:1341149; -. DR CTD; 10566; -. DR MGI; MGI:1341149; Akap3. DR VEuPathDB; HostDB:ENSMUSG00000030344; -. DR eggNOG; ENOG502SM7F; Eukaryota. DR GeneTree; ENSGT00940000153313; -. DR HOGENOM; CLU_017072_0_0_1; -. DR InParanoid; O88987; -. DR OMA; MADKVDW; -. DR OrthoDB; 4627091at2759; -. DR PhylomeDB; O88987; -. DR TreeFam; TF105403; -. DR BioGRID-ORCS; 11642; 0 hits in 77 CRISPR screens. DR ChiTaRS; Akap3; mouse. DR PRO; PR:O88987; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; O88987; protein. DR Bgee; ENSMUSG00000030344; Expressed in seminiferous tubule of testis and 13 other cell types or tissues. DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IDA:MGI. DR GO; GO:0035686; C:sperm fibrous sheath; IDA:UniProtKB. DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl. DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB. DR GO; GO:0051018; F:protein kinase A binding; IMP:MGI. DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI. DR GO; GO:0007178; P:cell surface receptor protein serine/threonine kinase signaling pathway; IPI:MGI. DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB. DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR InterPro; IPR020799; AKAP_110. DR InterPro; IPR018292; AKAP_110_C. DR InterPro; IPR008382; SPHK1-interactor_AKAP_110. DR PANTHER; PTHR10226; A KINASE ANCHOR PROTEIN; 1. DR PANTHER; PTHR10226:SF9; A-KINASE ANCHOR PROTEIN 3; 1. DR Pfam; PF05716; AKAP_110; 1. DR SMART; SM00807; AKAP_110; 1. PE 1: Evidence at protein level; KW Cell projection; Cilium; Cytoplasmic vesicle; Flagellum; Phosphoprotein; KW Reference proteome. FT CHAIN 1..864 FT /note="A-kinase anchor protein 3" FT /id="PRO_0000064527" FT REGION 125..138 FT /note="PKA-RII subunit binding domain" FT /evidence="ECO:0000250|UniProtKB:O75969" FT REGION 190..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 251..281 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 619..638 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 190..218 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 219..235 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 620..637 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 12 FT /note="Phosphoserine; by STK33" FT /evidence="ECO:0000269|PubMed:37146716" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75969" FT MOD_RES 405 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75969" FT MOD_RES 406 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O75969" FT CONFLICT 215 FT /note="T -> M (in Ref. 1; AAC63369)" FT /evidence="ECO:0000305" SQ SEQUENCE 864 AA; 95556 MW; 3E24E63327BC4E78 CRC64; MADRVDWLQS QSGVCKVGVY SPGDNQHQDW KMDTSTDPVR VLSWLRKDLE KSTAGFQDSR FKPGESSFVE EVAYPVDQRK GFCVDYYNTT NKGSPGRLHF EMSHKENPSQ GLISHVGNGG SIDEVSFYAN RLTNLVIAMA RKEINEKIHG AENKCVHQSL YMGDEPTPHK SLSTVASELV NETVTACSKN ISSDKAPGSG DRASGSSQAP GLRYTSTLKI KESTKEGKCP DDKPGTKKSF FYKEVFESRN AGDAKEGGRS LPGDQKLFRT SPDNRPDDFS NSISQGIMTY ANSVVSDMMV SIMKTLKIQV KDTTIATILL KKVLMKHAKE VVSDLIDSFM KNLHGVTGSL MTDTDFVSAV KRSFFSHGSQ KATDIMDAML GKLYNVMFAK KFPENIRRAR DKSESYSLIS TKSRAGDPKL SNLNFAMKSE SKLKENLFST CKLEKEKTCA ETLGEHIIKE GLHMWHKSQQ KSPGLERAAK LGNAPQEVSF ECPDPCEANP PHQPQPPENF ANFMCDSDSW AKDLIVSALL LIQYHLAQGG KMDAQSFLEA AASTNFPTNK PPPPSPVVQD ECKLKSPPHK ICDQEQTEKK DLMSVIFNFI RNLLSETIFK SSRNCESNVH EQNTQEEEIH PCERPKTPCE RPITPPAPKF CEDEEATGGA LSGLTKMVAN QLDNCMNGQM VEHLMDSVMK LCLIIAKSCD SPLSELGEEK CGDASRPNSA FPDNLYECLP VKGTGTAEAL LQNAYLTIHN ELRGLSGQPP EGCEIPKVIV SNHNLADTVQ NKQLQAVLQW VAASELNVPI LYFAGDDEGI QEKLLQLSAT AVEKGRSVGE VLQSVLRYEK ERQLDEAVGN VTRLQLLDWL MANL //