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 07-JUN-2017, entry version 114. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT project: 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., RA 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 RT subunit of 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 RT 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 CC reaction. {ECO:0000250}. CC -!- SUBUNIT: Interacts with ROPN1 AND ROPN1L. {ECO:0000250}. CC -!- INTERACTION: CC Q99MP8:Brap; NbExp=3; IntAct=EBI-9033539, EBI-10818333; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, CC acrosome {ECO:0000269|PubMed:11278869}. Note=Ribs of the fibrous CC sheath in the principal piece of the sperm tail. Dorsal margin of CC the acrosomal segment. CC -!- DOMAIN: RII-binding site, predicted to form an amphipathic helix, CC could participate in protein-protein interactions with a CC complementary 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 UniGene; Mm.87748; -. DR ProteinModelPortal; O88987; -. DR SMR; O88987; -. DR BioGrid; 198050; 1. DR IntAct; O88987; 2. DR STRING; 10090.ENSMUSP00000093091; -. DR PhosphoSitePlus; O88987; -. DR MaxQB; O88987; -. DR PaxDb; O88987; -. DR PeptideAtlas; O88987; -. DR PRIDE; O88987; -. 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 CTD; 10566; -. DR MGI; MGI:1341149; Akap3. DR eggNOG; ENOG410IEV9; Eukaryota. DR eggNOG; ENOG411183Z; LUCA. DR GeneTree; ENSGT00420000029845; -. DR HOGENOM; HOG000220883; -. DR HOVERGEN; HBG050478; -. DR InParanoid; O88987; -. DR KO; K16520; -. DR OMA; AMARKEI; -. DR OrthoDB; EOG091G0209; -. DR TreeFam; TF105403; -. DR PRO; PR:O88987; -. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; ENSMUSG00000030344; -. DR CleanEx; MM_AKAP3; -. DR Genevisible; O88987; MM. DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI. DR GO; GO:0031514; C:motile cilium; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0035686; C:sperm fibrous sheath; IDA: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:0008104; P:protein localization; IMP:MGI. DR GO; GO:0010738; P:regulation of protein kinase A signaling; IBA:GO_Central. 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_binding_1. DR InterPro; IPR008382; SPHK1-interactor_AKAP_110. DR PANTHER; PTHR10226; PTHR10226; 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 Complete proteome; Cytoplasmic vesicle; Phosphoprotein; KW Reference proteome. FT CHAIN 1 864 A-kinase anchor protein 3. FT /FTId=PRO_0000064527. FT REGION 125 138 PKA-RII subunit binding domain. FT MOD_RES 206 206 Phosphoserine. FT {ECO:0000250|UniProtKB:O75969}. FT MOD_RES 405 405 Phosphoserine. FT {ECO:0000250|UniProtKB:O75969}. FT MOD_RES 406 406 Phosphotyrosine. FT {ECO:0000250|UniProtKB:O75969}. FT CONFLICT 215 215 T -> M (in Ref. 1; AAC63369). FT {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 //