AKAP3_MOUSE
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 03-AUG-2022, entry version 139.
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}.
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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 MaxQB; O88987; -.
DR PaxDb; O88987; -.
DR PeptideAtlas; O88987; -.
DR PRIDE; O88987; -.
DR ProteomicsDB; 296150; -.
DR Antibodypedia; 22296; 188 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 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; ENFICDS; -.
DR OrthoDB; 221175at2759; -.
DR PhylomeDB; O88987; -.
DR TreeFam; TF105403; -.
DR BioGRID-ORCS; 11642; 0 hits in 72 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; 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 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
