ID   ENKUR_MOUSE             Reviewed;         255 AA.
AC   Q6SP97;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Enkurin;
GN   Name=Enkur;
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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP   WITH TRPC1; TRPC2 AND TRPC5, AND TISSUE SPECIFICITY.
RC   STRAIN=CD-1;
RX   PubMed=15385169; DOI=10.1016/j.ydbio.2004.07.031;
RA   Sutton K.A., Jungnickel M.K., Wang Y., Cullen K., Lambert S., Florman H.M.;
RT   "Enkurin is a novel calmodulin and TRPC channel binding protein in sperm.";
RL   Dev. Biol. 274:426-435(2004).
CC   -!- FUNCTION: Adapter that functions to localize a calcium-sensitive signal
CC       transduction machinery in sperm to a calcium-permeable ion channel
CC       (PubMed:15385169). Microtubule inner protein (MIP) part of the dynein-
CC       decorated doublet microtubules (DMTs) in cilia axoneme, which is
CC       required for motile cilia beating (By similarity).
CC       {ECO:0000250|UniProtKB:E1B836, ECO:0000269|PubMed:15385169}.
CC   -!- SUBUNIT: Binds calmodulin via its IQ domain. Interacts with TRPC1,
CC       TRPC2, TRPC5, but not TRPC3 (PubMed:15385169). Interacts with CFAP45
CC       (By similarity). {ECO:0000250|UniProtKB:Q8TC29,
CC       ECO:0000269|PubMed:15385169}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:E1B836}. Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:15385169}. Note=Sperm acrosomal crescent and
CC       flagellar principal piece. {ECO:0000269|PubMed:15385169}.
CC   -!- TISSUE SPECIFICITY: High expression in testis and vomeronasal organ and
CC       lower expression in ovary, heart, lung, and brain. Not expressed in
CC       other tissues. {ECO:0000269|PubMed:15385169}.
CC   -!- DOMAIN: The IQ motif is involved in calmodulin binding.
CC       {ECO:0000269|PubMed:15385169}.
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DR   EMBL; AY454124; AAS45167.1; -; mRNA.
DR   CCDS; CCDS38055.1; -.
DR   RefSeq; NP_082004.1; NM_027728.2.
DR   AlphaFoldDB; Q6SP97; -.
DR   SMR; Q6SP97; -.
DR   BioGRID; 214568; 3.
DR   STRING; 10090.ENSMUSP00000027992; -.
DR   PhosphoSitePlus; Q6SP97; -.
DR   MaxQB; Q6SP97; -.
DR   PaxDb; Q6SP97; -.
DR   PRIDE; Q6SP97; -.
DR   ProteomicsDB; 275864; -.
DR   Antibodypedia; 25866; 225 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000027992; ENSMUSP00000027992; ENSMUSG00000026679.
DR   GeneID; 71233; -.
DR   KEGG; mmu:71233; -.
DR   UCSC; uc008ina.1; mouse.
DR   CTD; 219670; -.
DR   MGI; MGI:1918483; Enkur.
DR   VEuPathDB; HostDB:ENSMUSG00000026679; -.
DR   eggNOG; ENOG502QT8E; Eukaryota.
DR   GeneTree; ENSGT00940000153866; -.
DR   HOGENOM; CLU_088051_1_0_1; -.
DR   InParanoid; Q6SP97; -.
DR   OMA; YISTFRP; -.
DR   OrthoDB; 1449984at2759; -.
DR   PhylomeDB; Q6SP97; -.
DR   TreeFam; TF323892; -.
DR   BioGRID-ORCS; 71233; 2 hits in 73 CRISPR screens.
DR   PRO; PR:Q6SP97; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q6SP97; protein.
DR   Bgee; ENSMUSG00000026679; Expressed in seminiferous tubule of testis and 94 other tissues.
DR   ExpressionAtlas; Q6SP97; baseline and differential.
DR   Genevisible; Q6SP97; MM.
DR   GO; GO:0097728; C:9+0 motile cilium; IDA:MGI.
DR   GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; EXP:MGI.
DR   GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0061966; P:establishment of left/right asymmetry; IMP:MGI.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR   InterPro; IPR026150; Enkur.
DR   InterPro; IPR027012; Enkurin_dom.
DR   PANTHER; PTHR21490:SF0; PTHR21490:SF0; 1.
DR   Pfam; PF13864; Enkurin; 1.
DR   PROSITE; PS51665; ENKURIN; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW   Flagellum; Reference proteome; SH3-binding.
FT   CHAIN           1..255
FT                   /note="Enkurin"
FT                   /id="PRO_0000086976"
FT   DOMAIN          160..252
FT                   /note="Enkurin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01000"
FT   DOMAIN          176..187
FT                   /note="IQ"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..255
FT                   /note="Interaction with TRPC proteins"
FT                   /evidence="ECO:0000269|PubMed:15385169"
FT   MOTIF           83..89
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   255 AA;  29527 MW;  325389264E2701EC CRC64;
     MDSPCTSESI YNLIPSDLKE PPQHPRYTSL FRATIKNDMK KFKTAMKTMG PAKVEIPSPK
     DFLKKHSKEK TLPPKKKFNR CSPKKPAVPL RTDHPVMGIQ SGKNFINTNA ADVIMGVAKK
     PKPIYVDKRT GDKHDLETSG LFPKYINKKD YGITPEYICK RNEDVKKAQE EYDNYIQENL
     KKAAMKRLSD EEREAVLQGL KKNWEEVHKE FQSLSVFIDS VPKKIRKQKL EKEMKQLEHD
     ISVIEKHKII YIANK