ID   CFA36_RAT               Reviewed;         343 AA.
AC   Q4V8E4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cilia- and flagella-associated protein 36 {ECO:0000305};
DE   AltName: Full=Coiled-coil domain-containing protein 104 {ECO:0000312|RGD:1311732};
GN   Name=Cfap36 {ECO:0000305}; Synonyms=Ccdc104 {ECO:0000312|RGD:1311732};
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19680650; DOI=10.1007/s00262-009-0742-3;
RA   Totland C., Bredholt G., Haugen M., Haukanes B.I., Vedeler C.A.;
RT   "Antibody to CCDC104 is associated with a paraneoplastic antibody to CDR2
RT   (anti-Yo).";
RL   Cancer Immunol. Immunother. 59:231-237(2010).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP   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: May act as an effector for ARL3. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ARL3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96G28}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q96G28}. Cell projection, cilium, flagellum
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC       {ECO:0000303|PubMed:19680650}.
CC   -!- SIMILARITY: Belongs to the CFAP36 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; BC097425; AAH97425.1; -; mRNA.
DR   RefSeq; NP_001020037.1; NM_001024866.1.
DR   AlphaFoldDB; Q4V8E4; -.
DR   SMR; Q4V8E4; -.
DR   STRING; 10116.ENSRNOP00000005306; -.
DR   iPTMnet; Q4V8E4; -.
DR   PhosphoSitePlus; Q4V8E4; -.
DR   PaxDb; Q4V8E4; -.
DR   PRIDE; Q4V8E4; -.
DR   Ensembl; ENSRNOT00000005306; ENSRNOP00000005306; ENSRNOG00000003901.
DR   GeneID; 289859; -.
DR   KEGG; rno:289859; -.
DR   UCSC; RGD:1311732; rat.
DR   CTD; 112942; -.
DR   RGD; 1311732; Cfap36.
DR   eggNOG; KOG4511; Eukaryota.
DR   GeneTree; ENSGT00390000012785; -.
DR   HOGENOM; CLU_050059_0_0_1; -.
DR   InParanoid; Q4V8E4; -.
DR   OMA; LVDFMLG; -.
DR   OrthoDB; 1373952at2759; -.
DR   PhylomeDB; Q4V8E4; -.
DR   TreeFam; TF315143; -.
DR   PRO; PR:Q4V8E4; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000003901; Expressed in testis and 20 other tissues.
DR   Genevisible; Q4V8E4; RN.
DR   GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR   GO; GO:0097546; C:ciliary base; ISO:RGD.
DR   GO; GO:0035869; C:ciliary transition zone; ISO:RGD.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR   Gene3D; 1.20.1520.10; -; 1.
DR   InterPro; IPR023379; BART_dom.
DR   InterPro; IPR042541; BART_sf.
DR   InterPro; IPR038888; CFAP36.
DR   PANTHER; PTHR21532; PTHR21532; 1.
DR   Pfam; PF11527; ARL2_Bind_BART; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Flagellum; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..343
FT                   /note="Cilia- and flagella-associated protein 36"
FT                   /id="PRO_0000278640"
FT   REGION          165..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          147..181
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        165..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C6E0"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C6E0"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   343 AA;  39590 MW;  8F489FE5DDE8D741 CRC64;
     MAAEEEDEVE WVVESIAGFL RGPDWSIPIL DFVEQKCEVF DDEEESKLTY TEIHQEYKEL
     VEKLLESYLK EIGINEDQFQ EACTSPLAKT RTSQAILQPV LAAEDFTIFK AMMVQKNIEM
     QLQAIRIIQE RNGVLPDCLT DGADVVSDLE QEEMKILREV LRKSKEEYDQ EEERKRKKQS
     SEGKMEEPPI YTSETAKLTN SQGDGEHFVQ PSSEVKVHFT NQSVQPLARK MELLPETSSL
     TQKGLKIPGL EHASMEGPIA NLSALGTEEL RQREHYLKQK RDKLMSMRKD MRAKQIQNTE
     QKGKPTREAE EMTEKPEMTA EEKQTLLKRR LLAEKLKEEV INK