AKAP4_RAT
ID AKAP4_RAT Reviewed; 847 AA.
AC O35774;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=A-kinase anchor protein 4;
DE Short=AKAP-4;
DE AltName: Full=75 kDa fibrous sheath protein;
DE AltName: Full=Major sperm fibrous sheath protein;
DE AltName: Full=Protein kinase A-anchoring protein 4;
DE Short=PRKA4;
DE Flags: Precursor;
GN Name=Akap4 {ECO:0000312|RGD:620828};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAB62877.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAB62877.1};
RA El-Alfy M., Moshonas D., Morales C., Oko R.;
RT "Molecular cloning and developmental expression of the 75 kDa protein of
RT the rat fibrous sheath.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-129; SER-189;
RP SER-203; THR-206; SER-212; SER-225; SER-270; SER-301; SER-304; SER-340;
RP SER-430; SER-441; SER-443; SER-462; SER-491; SER-496; SER-503; THR-505;
RP SER-536; SER-626; SER-631; SER-648; SER-650; SER-674; SER-677; SER-700 AND
RP SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Major structural component of sperm fibrous sheath. May play
CC a role in sperm motility (By similarity).
CC {ECO:0000250|UniProtKB:Q5JQC9}.
CC -!- SUBUNIT: Interacts with PRKAR1A and PRKAR2A. Interacts with ENO4.
CC {ECO:0000250|UniProtKB:Q60662}.
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 -!- TISSUE SPECIFICITY: Expressed in flagella of epididymal sperm.
CC {ECO:0000269|PubMed:19423663}.
CC -!- DOMAIN: RI-alpha binding site, predicted to form an amphipathic helix
CC that is required for binding to Prkar1a.
CC {ECO:0000250|UniProtKB:Q60662}.
CC -!- SIMILARITY: Belongs to the AKAP110 family. {ECO:0000305}.
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DR EMBL; AF008114; AAB62877.1; -; mRNA.
DR RefSeq; NP_077378.1; NM_024402.1.
DR AlphaFoldDB; O35774; -.
DR STRING; 10116.ENSRNOP00000003939; -.
DR iPTMnet; O35774; -.
DR PhosphoSitePlus; O35774; -.
DR PaxDb; O35774; -.
DR PRIDE; O35774; -.
DR GeneID; 79254; -.
DR KEGG; rno:79254; -.
DR UCSC; RGD:620828; rat.
DR CTD; 8852; -.
DR RGD; 620828; Akap4.
DR eggNOG; ENOG502QQXJ; Eukaryota.
DR InParanoid; O35774; -.
DR OrthoDB; 221175at2759; -.
DR PhylomeDB; O35774; -.
DR PRO; PR:O35774; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0097224; C:sperm connecting piece; ISO:RGD.
DR GO; GO:0097229; C:sperm end piece; ISO:RGD.
DR GO; GO:0035686; C:sperm fibrous sheath; ISO:RGD.
DR GO; GO:0097225; C:sperm midpiece; ISO:RGD.
DR GO; GO:0097228; C:sperm principal piece; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0051018; F:protein kinase A binding; ISS:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:RGD.
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 Cell projection; Cilium; Cilium biogenesis/degradation; Flagellum;
KW Phosphoprotein; Reference proteome.
FT PROPEP 1..187
FT /evidence="ECO:0000255"
FT /id="PRO_0000248232"
FT CHAIN 188..847
FT /note="A-kinase anchor protein 4"
FT /evidence="ECO:0000250|UniProtKB:Q60662"
FT /id="PRO_0000248233"
FT REGION 182..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..231
FT /note="Interaction with Prkar1a and Prkar2a"
FT /evidence="ECO:0000250|UniProtKB:Q60662"
FT REGION 334..343
FT /note="PKA-RI subunit binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q60662"
FT REGION 511..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5JQC9"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 847 AA; 93494 MW; A8F3DB78EA2C3914 CRC64;
MIAYCGTTKM SDDIDWLHSR RGVCKVDLYS PEGQQDQDRK VICFVDVSTL NVEDDSKGAA
GPRSDGELNL ENLEEKEIIV IKDTEKQDQP KTEGSVCLFK QAPSDPISVL NWLLNDLQKY
ALGFQHALSP SASSCKHKVG DLEGDYHKIP SENCYSVYAD QVNLDYLNKG PQNLRLEMAA
SKNTNNNQSP SNPATKSPSN QRSVATPDGE CSMDDLSYYV NRLSSLVIQM ARKEIKDKLE
GGNKCLHHSM YTSGEKGKTS PRSAVSKIAS EMAHEAVELT SSEMRGNGEE GRDGRKTFLY
SELSNKNKCG EKQQMCPKDS KEFADSISKG LMVYANQVAS DMMVSVMKTL KVHSCGKPIP
ACVVLKRVLL KHTKEIVSDL IDSCMKNLHN ITGVLMTDSD FVSAVKRNLF NHGKQNAADI
MEAMLKRLVS ALLGEKKETK SQSLAYATLK AGTHDPKCKN QSLEFSAMKA EMKGKDKGKT
KGDPCCKSLT SAERVSEHIL KESLTMWNNQ KQGTQGRVPN KVCPSKDEKR EKISPSTDSL
AKDLIVSALM LIQYHLTQQA KGKDPCEEEC PGSSMGYMSQ SAQYEKSGGG QSSKSLSMKH
FESRGAPGPS TCAKENQLES QKMDMSNMVL SLIQKLLSES PFSCDELSES ENKRCCDSRS
KQAAPVAKRP EDQSQDSTEM DFISGMKQMN RQFIDQLVES VMKLCLIMAK YSNNGAALAE
LEEQAALASN GPRCGREAVM SQSYLETPGP EVIVNNQCST SNLQKQLQAV LQWIAASQFN
VPMLYFMGDD DGQLEKLPEV SAKAAEKGYS VGDLLQEVMK FAKERQLDEA VGNMARKQLL
DWLLANL
