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 13-SEP-2023, entry version 145. DE RecName: Full=A-kinase anchor protein 3; DE Short=AKAP-3; DE AltName: Full=A-kinase anchor protein 110 kDa; DE Short=AKAP 110; DE AltName: Full=Protein kinase A-anchoring protein 3; DE Short=PRKA3; GN Name=Akap3; Synonyms=Akap110; 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). CC -!- FUNCTION: May function as a regulator of both motility- and head- CC associated functions such as capacitation and the acrosome reaction. CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with ROPN1 and ROPN1L. Interacts with QRICH2 (By CC similarity). {ECO:0000250, 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}. Note=Ribs of the fibrous sheath in the CC principal piece of the sperm tail. Dorsal margin of the acrosomal CC segment. 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. CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000250}. 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 MaxQB; O88987; -. DR PaxDb; O88987; -. DR PeptideAtlas; O88987; -. DR ProteomicsDB; 296150; -. DR Antibodypedia; 22296; 204 antibodies from 33 providers. DR DNASU; 11642; -. DR Ensembl; ENSMUST00000095440; ENSMUSP00000093091; ENSMUSG00000030344. DR Ensembl; ENSMUST00000202574; ENSMUSP00000144405; ENSMUSG00000030344. DR Ensembl; ENSMUST00000202878; ENSMUSP00000143794; ENSMUSG00000030344. 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 12 other tissues. DR Genevisible; O88987; MM. 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:MGI. DR GO; GO:0097225; C:sperm midpiece; ISO:MGI. DR GO; GO:0097228; C:sperm principal piece; IDA:MGI. DR GO; GO:0051018; F:protein kinase A binding; IMP:MGI. DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IPI:MGI. DR InterPro; IPR020799; AKAP_110. DR InterPro; IPR018292; AKAP_110_C. DR InterPro; IPR018459; RII-bd_1. 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 Pfam; PF10522; RII_binding_1; 1. DR SMART; SM00807; AKAP_110; 1. PE 1: Evidence at protein level; KW Cytoplasmic vesicle; Phosphoprotein; 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 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 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 //