AKAP3_BOVIN
ID AKAP3_BOVIN Reviewed; 858 AA.
AC O77797; A6QQY3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 25-MAY-2022, entry version 109.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-858.
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).
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 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250}. Note=Ribs of the fibrous sheath in the principal piece
CC of the sperm tail. Dorsal margin of the acrosomal segment (By
CC similarity). {ECO:0000250}.
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; BC150040; AAI50041.1; -; mRNA.
DR EMBL; AF093407; AAC63370.1; -; mRNA.
DR RefSeq; NP_001094509.1; NM_001101039.2.
DR AlphaFoldDB; O77797; -.
DR IntAct; O77797; 5.
DR MINT; O77797; -.
DR STRING; 9913.ENSBTAP00000001353; -.
DR PaxDb; O77797; -.
DR PRIDE; O77797; -.
DR GeneID; 281610; -.
DR KEGG; bta:281610; -.
DR CTD; 10566; -.
DR eggNOG; ENOG502SM7F; Eukaryota.
DR InParanoid; O77797; -.
DR OrthoDB; 221175at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Phosphoprotein; Reference proteome.
FT CHAIN 1..858
FT /note="A-kinase anchor protein 3"
FT /id="PRO_0000064525"
FT REGION 131..144
FT /note="PKA-RII subunit binding domain"
FT REGION 191..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75969"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75969"
FT MOD_RES 411
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75969"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75969"
FT CONFLICT 247
FT /note="F -> L (in Ref. 2; AAC63370)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="L -> F (in Ref. 2; AAC63370)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="L -> F (in Ref. 2; AAC63370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 94672 MW; CE6ABBEA1B203C90 CRC64;
MSDRVDWLQS QNGVCKVDVY SPGDSQPQDW KMSDESLSIF KEASHDPIRV LSWLRRDLEK
STAGFQDIRF KPGESSLGRE MVSSGDPRKG FCVDYYNTTS RGSPGRLHFE MSHRENPHQG
PTCNGSSVDE VSFYANRLTN LVIAMARKEI NEKIDGSENR CVHQSVYMGD EPPPNKSLSK
VASELVNETV TACSKNTPSD KAPGSGDRAS GTLQSPPNLK YKSTLKIKES NKGGRGPDDR
PSSKKSFFYK EVFESRNAGD AKEGGRTLPA ERKMFRGYER PDDFTASISQ GIMTYANSVV
SDMMVSIMKT LKIQVKDTTI ATIVLKKVLI KHAKEVVSDL IDSFMKNLHN VTGTLMTDTD
FVSAVKRSFF SHGSQKATDI MDAMLGKLYS VIFAKKPPET VRKTKDKSES YSLVSMKGMG
DPKHRNVNFA SMKSEGKVRE RVCTPTPKPE KSCVETLGEH IIKEGLTLWH NSQQKEGISA
CLQGSPFVTP KRQYKPVPDF PLGFPFDPCN FSLPMQCPEK PENFMCDSDS WAKDLLVSAL
LLIQYHLAQG GNMDAQSFLE AAGTSNLYPT KSPAVSHESS LRSPQVGADP EEVEKKDLMS
VFFNLIRNLL SETIFKSDHS CDPKATKEDN SPQCERPVTP SPAKLNECDE TGGAFAGLTK
MVANKLDGHM NGQMVDHLMD SVMKLCLIIA KSCDSPLAEL GDDKSGDASR PTSAFPESLY
ECLSTKGTGT AETLLQNAYQ AIHNELRSLS AQPPEGCTAP KVIVSNHNLT DTVQNKQLQA
VLQWVAASEL NVPILYFAGD DEGIQEKLLQ LSAAAVEKGR SVGEVLQSVL RYEKERQLDE
AVGNVTRLQL LDWLMVNL
