AKAP1_CAEEL
ID AKAP1_CAEEL Reviewed; 867 AA.
AC Q09285; Q09286;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=KH domain-containing protein akap-1 {ECO:0000305};
GN Name=akap-1 {ECO:0000312|WormBase:C56G2.1a};
GN ORFNames=C56G2.1 {ECO:0000312|WormBase:C56G2.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q09285-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q09285-2; Sequence=VSP_002856, VSP_002857;
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DR EMBL; FO080744; CCD66341.1; -; Genomic_DNA.
DR EMBL; FO080744; CCD66342.1; -; Genomic_DNA.
DR RefSeq; NP_741190.1; NM_171163.5.
DR RefSeq; NP_741191.1; NM_171164.4. [Q09285-2]
DR AlphaFoldDB; Q09285; -.
DR SMR; Q09285; -.
DR STRING; 6239.C56G2.1a; -.
DR iPTMnet; Q09285; -.
DR EPD; Q09285; -.
DR PaxDb; Q09285; -.
DR PeptideAtlas; Q09285; -.
DR EnsemblMetazoa; C56G2.1a.1; C56G2.1a.1; WBGene00016977. [Q09285-1]
DR EnsemblMetazoa; C56G2.1b.1; C56G2.1b.1; WBGene00016977. [Q09285-2]
DR GeneID; 175898; -.
DR CTD; 175898; -.
DR WormBase; C56G2.1a; CE24866; WBGene00016977; akap-1. [Q09285-1]
DR WormBase; C56G2.1b; CE30637; WBGene00016977; akap-1. [Q09285-2]
DR eggNOG; KOG2279; Eukaryota.
DR GeneTree; ENSGT00390000001360; -.
DR HOGENOM; CLU_330699_0_0_1; -.
DR InParanoid; Q09285; -.
DR OMA; MIIRPHH; -.
DR OrthoDB; 378332at2759; -.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q09285; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016977; Expressed in larva and 5 other tissues.
DR ExpressionAtlas; Q09285; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IEA:InterPro.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR033104; Akap1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR22948:SF48; PTHR22948:SF48; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Membrane; Reference proteome; RNA-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..867
FT /note="KH domain-containing protein akap-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000050163"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 528..595
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 689..747
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 145..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..458
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_002856"
FT VAR_SEQ 459..500
FT /note="VLKHHENEAGDAAHAQIIESPHHENASYEKSDSPGLDSQNSE -> MKVYAK
FT VQEEVKTRRLRKNSTTSSGYGYSVPMTPNTEILFDT (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_002857"
SQ SEQUENCE 867 AA; 96430 MW; 1F3083DB0EBFE844 CRC64;
MVAAAAADAL AAGGDSSSPS DLYNKITGQQ SSTTTSLSYA ACDVITRHLI SMLLEISNWT
NDLAKYLAGS EQSSDDGHNE RCLLFSSIFF AIDPSLALAQ MSSVASKHAL LIALGGFSIA
ALFVWYINKK DKDGRKKKKV GDVISNGLPK TATASDVQTE NGNVKKANGH VNGDVQSSIG
VSQKQQQKDE DEKTQKKDAV QNEKPSIDKK QPKSQAPTEK KEEKTVEIHT ETEETDHVAA
GDSGVVSEHK EHDKKTKQKN DEPVSIDKKS EEIEVPKQAG VVNEEPKKQS EETVVEEQFV
KKEEPKLKSA PTPLLTMPSK KKVLENEQIP EEPTPTKMND ATSPLSLDIA AQMSPASFSW
SEEMEKSFNE EEFRLNESSD IDRSPASPLR HLQQQHNKNR SSQKRKGGRV NGRDGVHQPQ
QQHQQQKKEE QGQIKKGQRR LTKEKSVEET PEKSQKRVVL KHHENEAGDA AHAQIIESPH
HENASYEKSD SPGLDSQNSE ASSQDSGRAT GPLASPHEDG LTTEDDFLPM YEFEIPNSLV
GLIIGVKGKT IKELSVRTNV RMLIRQHHET DKVKTHQICQ VRGKRDEINH CLQMLRRRFP
PARFPELNLQ PVVPPVLPNS NFDMLSTQPT WLTLPEDIKC EVAVSSIISA SHFFIQQPTH
PSFASLRHLD MYMGSLYGEQ SNLPELPIPC QNGLLCAAPV GNAWFRAVTV QYFDETDEVF
VKFVDYGGYS KMARQDLRQI RTDLMSLPFQ STEVMLAHVR PVDGTTNWSD AAMQKFRAMC
IGKVINCKMV GQSHDTRIPM VELYMMSKDG KDAQEVRFDQ VLMNCGLART ADPSKMSRIT
VPAALDTESR MKRPSFSSQT SQTAVVC
