AKAP4_MOUSE
ID AKAP4_MOUSE Reviewed; 849 AA.
AC Q60662; B1AXM7; Q60630; Q8R2G7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=A-kinase anchor protein 4;
DE Short=AKAP-4;
DE AltName: Full=A-kinase anchor protein 82 kDa;
DE Short=AKAP 82;
DE Short=mAKAP82;
DE AltName: Full=FSC1;
DE AltName: Full=Major sperm fibrous sheath protein;
DE AltName: Full=Protein kinase A-anchoring protein 4;
DE Short=PRKA4;
DE AltName: Full=p82;
DE Flags: Precursor;
GN Name=Akap4; Synonyms=Akap82, Fsc1;
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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=CD-1; TISSUE=Sperm;
RX PubMed=8088444; DOI=10.1006/dbio.1994.1252;
RA Carrera A., Gerton G.L., Moss S.B.;
RT "The major fibrous sheath polypeptide of mouse sperm: structural and
RT functional similarities to the A-kinase anchoring proteins.";
RL Dev. Biol. 165:272-284(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=CD-1; TISSUE=Spermatid;
RX PubMed=7711182; DOI=10.1095/biolreprod52.1.41;
RA Fulcher K.D., Mori C., Welch J.E., O'Brien D.A., Klapper D.G., Eddy E.M.;
RT "Characterization of Fsc1 cDNA for a mouse sperm fibrous sheath
RT component.";
RL Biol. Reprod. 52:41-49(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC STRAIN=129/Sv;
RX PubMed=12606363; DOI=10.1095/biolreprod.102.013466;
RA Brown P.R., Miki K., Harper D.B., Eddy E.M.;
RT "A-kinase anchoring protein 4 binding proteins in the fibrous sheath of the
RT sperm flagellum.";
RL Biol. Reprod. 68:2241-2248(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP INTERACTION WITH PRKAR1A AND PRKAR2A, AND DOMAIN.
RX PubMed=9852104; DOI=10.1074/jbc.273.51.34384;
RA Miki K., Eddy E.M.;
RT "Identification of tethering domains for protein kinase A type Ialpha
RT regulatory subunits on sperm fibrous sheath protein FSC1.";
RL J. Biol. Chem. 273:34384-34390(1998).
RN [6]
RP FUNCTION.
RX PubMed=12167408; DOI=10.1006/dbio.2002.0728;
RA Miki K., Willis W.D., Brown P.R., Goulding E.H., Fulcher K.D., Eddy E.M.;
RT "Targeted disruption of the Akap4 gene causes defects in sperm flagellum
RT and motility.";
RL Dev. Biol. 248:331-342(2002).
RN [7]
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 [8]
RP INTERACTION WITH ENO4.
RX PubMed=23446454; DOI=10.1095/biolreprod.112.107128;
RA Nakamura N., Dai Q., Williams J., Goulding E.H., Willis W.D., Brown P.R.,
RA Eddy E.M.;
RT "Disruption of a spermatogenic cell-specific mouse enolase 4 (eno4) gene
RT causes sperm structural defects and male infertility.";
RL Biol. Reprod. 88:90-90(2013).
CC -!- FUNCTION: Major structural component of sperm fibrous sheath. Plays a
CC role in sperm motility (PubMed:12167408).
CC {ECO:0000269|PubMed:12167408}.
CC -!- SUBUNIT: Interacts with PRKAR1A and PRKAR2A (PubMed:9852104). Interacts
CC with ENO4 (PubMed:23446454). {ECO:0000269|PubMed:23446454,
CC ECO:0000269|PubMed:9852104}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q5JQC9}. Note=Localizes to the principle piece
CC of the sperm flagellum. {ECO:0000250|UniProtKB:Q5JQC9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60662-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60662-2; Sequence=VSP_004100;
CC -!- TISSUE SPECIFICITY: Spermatid.
CC -!- DEVELOPMENTAL STAGE: Post-meiotic phase of spermatogenesis.
CC -!- DOMAIN: RI-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer. {ECO:0000269|PubMed:9852104}.
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; U10341; AAA75597.1; -; mRNA.
DR EMBL; U07423; AAA53216.1; -; mRNA.
DR EMBL; AF448786; AAM18539.1; -; Genomic_DNA.
DR EMBL; AF448784; AAM18539.1; JOINED; Genomic_DNA.
DR EMBL; AF448785; AAM18539.1; JOINED; Genomic_DNA.
DR EMBL; AF448786; AAM18540.1; -; Genomic_DNA.
DR EMBL; AF448785; AAM18540.1; JOINED; Genomic_DNA.
DR EMBL; AL808124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40838.1; -. [Q60662-1]
DR CCDS; CCDS40839.1; -. [Q60662-2]
DR PIR; I49060; I49060.
DR RefSeq; NP_001036007.1; NM_001042542.2. [Q60662-2]
DR RefSeq; NP_033781.2; NM_009651.4. [Q60662-1]
DR AlphaFoldDB; Q60662; -.
DR STRING; 10090.ENSMUSP00000050962; -.
DR iPTMnet; Q60662; -.
DR PhosphoSitePlus; Q60662; -.
DR PaxDb; Q60662; -.
DR PRIDE; Q60662; -.
DR ProteomicsDB; 296389; -. [Q60662-1]
DR ProteomicsDB; 296390; -. [Q60662-2]
DR Antibodypedia; 470; 151 antibodies from 29 providers.
DR DNASU; 11643; -.
DR Ensembl; ENSMUST00000057101; ENSMUSP00000050962; ENSMUSG00000050089. [Q60662-1]
DR Ensembl; ENSMUST00000115750; ENSMUSP00000111416; ENSMUSG00000050089. [Q60662-2]
DR Ensembl; ENSMUST00000115751; ENSMUSP00000111417; ENSMUSG00000050089. [Q60662-2]
DR GeneID; 11643; -.
DR KEGG; mmu:11643; -.
DR UCSC; uc009slc.2; mouse. [Q60662-1]
DR CTD; 8852; -.
DR MGI; MGI:102794; Akap4.
DR VEuPathDB; HostDB:ENSMUSG00000050089; -.
DR eggNOG; ENOG502QQXJ; Eukaryota.
DR GeneTree; ENSGT00940000153313; -.
DR HOGENOM; CLU_016756_1_0_1; -.
DR InParanoid; Q60662; -.
DR OMA; KCGSGQS; -.
DR PhylomeDB; Q60662; -.
DR TreeFam; TF105403; -.
DR BioGRID-ORCS; 11643; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Akap4; mouse.
DR PRO; PR:Q60662; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q60662; protein.
DR Bgee; ENSMUSG00000050089; Expressed in seminiferous tubule of testis and 27 other tissues.
DR ExpressionAtlas; Q60662; baseline and differential.
DR Genevisible; Q60662; MM.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0097224; C:sperm connecting piece; ISO:MGI.
DR GO; GO:0097229; C:sperm end piece; ISO: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:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0120316; P:sperm flagellum assembly; 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; 3.
DR Pfam; PF10522; RII_binding_1; 1.
DR SMART; SM00807; AKAP_110; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Direct protein sequencing; Flagellum;
KW Phosphoprotein; Reference proteome.
FT PROPEP 1..188
FT /evidence="ECO:0000255"
FT /id="PRO_0000020659"
FT CHAIN 189..849
FT /note="A-kinase anchor protein 4"
FT /id="PRO_0000020660"
FT REGION 183..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..232
FT /note="PKA-RI and PKA-RII subunit binding domain"
FT REGION 335..344
FT /note="PKA-RI-alpha subunit binding domain"
FT COMPBIAS 183..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 301
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5JQC9"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JQC9"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 506
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35774"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004100"
FT CONFLICT 341
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="L -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="T -> P (in Ref. 1; AAA53216)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="K -> T (in Ref. 1; AAA53216)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="N -> T (in Ref. 1; AAA53216)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="I -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="S -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="G -> A (in Ref. 1; AAA53216)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="S -> R (in Ref. 1; AAA53216)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="A -> G (in Ref. 1; AAA53216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 849 AA; 93796 MW; 8DAC8939CF1CB81A CRC64;
MIAYCGTTTM SDDIDWLHSR RGVCKVDLYS PKGQQDQDRK VICFVDVSTL NVEDKDSKGA
AGSRSEGELN LETLEEKEII VIKDTEKQDQ SKTEGSVCLF KQAPSDPISV LNWLLNDLQK
YALGFQHALS PSASSCKHKV GDLEGDYSKI PSENCYSVYA DQVNFDYLNK GPQNLRLEMA
ASKNTNNNQS PSNPATKSPS NQRSVATPEG ECSMDDLSFY VNRLSSLVIQ MARKEIKDKL
EGGSKCLHHS MYTSGDKGKT SPRSAVSKIA SEMAHEAVEL TSSEMRGNGE DCRDGRKTFL
YSEMCNKNKC GEKQQMCPKD SKEFADSISK GLMVYANQVA SDMMVSVMKT LKVHSCGKPI
PACVVLKRVL LKHTKEIVSD LIDSCMKNLH NITGVLMTDS DFVSAVKRNL FNHGKQNAAD
IMEAMLKRLV SALLGEKKET KSQSLAYATL KAGTNDPKCK NQSLEFSAMK AEMKGKDKCK
SKADPCCKSL TSAERVSEHI LKESLTMWNN QKQGNQGKVT NKVCCTSKDE KREKISPSTD
SLAKDLIVSA LMLIQYHLTQ QAKGKDPCEE ECPGSSMGYM SQSAQYEKCG GGQSSKSLSM
KHFETRGAPG PSTCMKENQL ESQKMDMSNM VLSLIQKLLS ESPFSCDELT ESDNKRCCDP
RSSKAAPMAK RPEEQCQDNA ELDFISGMKQ MNRQFIDQLV ESVMKLCLIM AKYSNNGAAL
AELEEQAALV GSGSRCGRDA MMSQNYSETP GPEVIVNNQC STTNLQKQLQ AVLQWIAASQ
FNVPMLYFMG DDDGQLEKLP EVSAKAAEKG YSVGDLLQEV MKFAKERQLD EAVGNMARKQ
LLDWLLANL
