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Database: UniProt
Entry: A0A3Q0CZ92_MESAU
LinkDB: A0A3Q0CZ92_MESAU
Original site: A0A3Q0CZ92_MESAU 
ID   A0A3Q0CZ92_MESAU        Unreviewed;       853 AA.
AC   A0A3Q0CZ92;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=A-kinase anchor protein 1, mitochondrial {ECO:0000313|RefSeq:XP_021086162.1};
GN   Name=Akap1 {ECO:0000313|RefSeq:XP_021086162.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021086162.1};
RN   [1] {ECO:0000313|RefSeq:XP_021086162.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26319212;
RA   Ying B., Toth K., Spencer J.F., Aurora R., Wold W.S.;
RT   "Transcriptome sequencing and development of an expression microarray
RT   platform for liver infection in adenovirus type 5-infected Syrian golden
RT   hamsters.";
RL   Virology 485:305-312(2015).
RN   [2] {ECO:0000313|RefSeq:XP_021086162.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_021086162.1; XM_021230503.1.
DR   AlphaFoldDB; A0A3Q0CZ92; -.
DR   STRING; 10036.ENSMAUP00000010080; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd22395; KH-I_AKAP1; 1.
DR   CDD; cd20407; Tudor_AKAP1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR047368; KH-I_AKAP1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR018459; RII-bd_1.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047367; Tudor_AKAP1.
DR   PANTHER; PTHR22948:SF65; A-KINASE ANCHOR PROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF10522; RII_binding_1; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          708..767
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
FT   REGION          61..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  91758 MW;  8D305AD1631740D6 CRC64;
     MAIQFRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ESLKVGSVIE DQLPREACPR
     VLSVPPSVTQ PPEMEQPAVG KSSPEPAALP RIRQVRRRSE SSGNLPSNVD TRSQPCRDDN
     SKVELSLMGD EAKSIPLGCP LLPKEVPFPC EAAEGCRQES ALGKTPGRGW LDQCAASGEK
     AREKSGVEGT GDAVLGENGP EEGLLSQECI SEVEKSEVPS LASCGDGGEK VSSGPPQVAE
     LAKKEEYVVG KLPSSFLEPV HSEMVKDEDA LVPQVRGGIT HDRDLAREQV KEETLPENDQ
     IEQAAFQIIS QVILNATEEM RASTTGKTVA QVYPPISATQ PQGLEESSVP ASQKTGLGQD
     IPHPASTTTG ATASPPAEAL PPKTYVSCLS SPLASPTKDQ KPKNSAHHIS LAPCPPPVTR
     LRQSLDGASS PGGDDTFVTC MSDSRQSVVS VTSSGQCSDS LSTSGLEDSC TETISSPGDK
     AVTPPLPDST EPFSNGVLKE EFSDVGTEDG WTMDAEADHS GGSDGNSMDS VDSCSGLPKP
     DSLQNVQASS NPKKVDLIIW EIEVPKHLVG RLIGKQGRYV SFLKQTSGAK IYISTLPYTQ
     NVQICHIEGS QHHVDKALNL IGKKFKELNL TNIYAPPLPS LALPSLPMTS WLMLPDGITV
     EVIVVNQVNA GHLFVQQHTH PTFHALRSLD QQMYLCYSQP GIPTLPTPVE ITVICAAPGA
     DGAWWRAQVV ASYEETNEVE IRYVDYGGYK RVKVDVLRQI RSDFVTLPFQ GAEVLLDSVV
     PLSDDDHFSP EADAAMSEMT GNTALLAQVT SYSATGLPLI QLWSVVGDEV VLINRSLVER
     GLAQWVDSYY ANL
//
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