CFA53_HUMAN
ID CFA53_HUMAN Reviewed; 514 AA.
AC Q96M91; B4DXT1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cilia- and flagella-associated protein 53 {ECO:0000312|HGNC:HGNC:26530};
DE AltName: Full=Coiled-coil domain-containing protein 11 {ECO:0000312|HGNC:HGNC:26530};
GN Name=CFAP53 {ECO:0000312|HGNC:HGNC:26530};
GN Synonyms=CCDC11 {ECO:0000312|HGNC:HGNC:26530};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-294.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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 [3]
RP INVOLVEMENT IN HTX6, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22577226; DOI=10.1136/jmedgenet-2011-100457;
RA Perles Z., Cinnamon Y., Ta-Shma A., Shaag A., Einbinder T., Rein A.J.,
RA Elpeleg O.;
RT "A human laterality disorder associated with recessive CCDC11 mutation.";
RL J. Med. Genet. 49:386-390(2012).
RN [4]
RP VARIANT HTX6 GLY-158, AND FUNCTION.
RX PubMed=26531781; DOI=10.1002/humu.22928;
RA Noel E.S., Momenah T.S., Al-Dagriri K., Al-Suwaid A., Al-Shahrani S.,
RA Jiang H., Willekers S., Oostveen Y.Y., Chocron S., Postma A.V.,
RA Bhuiyan Z.A., Bakkers J.;
RT "A zebrafish loss-of-function model for human CFAP53 mutations reveals its
RT specific role in laterality organ function.";
RL Hum. Mutat. 37:194-200(2016).
CC -!- FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated
CC doublet microtubules (DMTs) in cilia axoneme, which is required for
CC motile cilia beating (By similarity). May play a role in the beating of
CC primary cilia and thereby be involved in the establishment of organ
CC laterality during embryogenesis (PubMed:26531781).
CC {ECO:0000250|UniProtKB:F1N7G5, ECO:0000269|PubMed:26531781}.
CC -!- SUBUNIT: Interacts with PIERCE1 and PIERCE2; the interactions link
CC outer dynein arms docking complex (ODA-DC) to the internal microtubule
CC inner proteins (MIP) in cilium axoneme. {ECO:0000250|UniProtKB:F1N7G5}.
CC -!- INTERACTION:
CC Q96M91; Q9Y3M2: CBY1; NbExp=4; IntAct=EBI-742422, EBI-947308;
CC Q96M91; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-742422, EBI-10961624;
CC Q96M91; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-742422, EBI-10175300;
CC Q96M91; P24863: CCNC; NbExp=3; IntAct=EBI-742422, EBI-395261;
CC Q96M91; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-742422, EBI-739624;
CC Q96M91; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-742422, EBI-5453285;
CC Q96M91; O95995: GAS8; NbExp=3; IntAct=EBI-742422, EBI-1052570;
CC Q96M91; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-742422, EBI-717919;
CC Q96M91; O00291: HIP1; NbExp=3; IntAct=EBI-742422, EBI-473886;
CC Q96M91; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-742422, EBI-740641;
CC Q96M91; Q15323: KRT31; NbExp=3; IntAct=EBI-742422, EBI-948001;
CC Q96M91; O76011: KRT34; NbExp=3; IntAct=EBI-742422, EBI-1047093;
CC Q96M91; O95751: LDOC1; NbExp=3; IntAct=EBI-742422, EBI-740738;
CC Q96M91; Q96PV6: LENG8; NbExp=3; IntAct=EBI-742422, EBI-739546;
CC Q96M91; P15173: MYOG; NbExp=3; IntAct=EBI-742422, EBI-3906629;
CC Q96M91; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-742422, EBI-3921217;
CC Q96M91; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-742422, EBI-14066006;
CC Q96M91; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-742422, EBI-302345;
CC Q96M91; Q15276: RABEP1; NbExp=3; IntAct=EBI-742422, EBI-447043;
CC Q96M91; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-742422, EBI-747035;
CC Q96M91; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-742422, EBI-12018146;
CC Q96M91; Q15025: TNIP1; NbExp=3; IntAct=EBI-742422, EBI-357849;
CC Q96M91; P36406: TRIM23; NbExp=3; IntAct=EBI-742422, EBI-740098;
CC Q96M91; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-742422, EBI-2130429;
CC Q96M91; P40222: TXLNA; NbExp=3; IntAct=EBI-742422, EBI-359793;
CC Q96M91; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-742422, EBI-6116822;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:F1N7G5}.
CC -!- TISSUE SPECIFICITY: Expressed in skin fibroblasts (at protein level).
CC {ECO:0000269|PubMed:22577226}.
CC -!- DISEASE: Heterotaxy, visceral, 6, autosomal (HTX6) [MIM:614779]: A form
CC of visceral heterotaxy, a complex disorder due to disruption of the
CC normal left-right asymmetry of the thoracoabdominal organs. Visceral
CC heterotaxy or situs ambiguus results in randomization of the placement
CC of visceral organs, including the heart, lungs, liver, spleen, and
CC stomach. The organs are oriented randomly with respect to the left-
CC right axis and with respect to one another. It can be associated with a
CC variety of congenital defects including cardiac malformations. HTX6
CC clinical features are situs inversus totalis and severe complex cardiac
CC malformations including unbalanced atrioventricular canal defects,
CC transposition of the great arteries with severe pulmonary stenosis,
CC right aortic arch, abnormal systemic venous return and total anomalous
CC pulmonary venous drainage. {ECO:0000269|PubMed:22577226,
CC ECO:0000269|PubMed:26531781}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CFAP53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71418.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK057305; BAB71418.1; ALT_INIT; mRNA.
DR EMBL; AK302114; BAG63493.1; -; mRNA.
DR EMBL; BC030606; AAH30606.2; -; mRNA.
DR CCDS; CCDS11940.2; -.
DR RefSeq; NP_659457.2; NM_145020.4.
DR AlphaFoldDB; Q96M91; -.
DR SMR; Q96M91; -.
DR BioGRID; 128633; 38.
DR IntAct; Q96M91; 28.
DR STRING; 9606.ENSP00000381553; -.
DR iPTMnet; Q96M91; -.
DR PhosphoSitePlus; Q96M91; -.
DR BioMuta; CFAP53; -.
DR DMDM; 118572626; -.
DR EPD; Q96M91; -.
DR jPOST; Q96M91; -.
DR MassIVE; Q96M91; -.
DR PaxDb; Q96M91; -.
DR PeptideAtlas; Q96M91; -.
DR PRIDE; Q96M91; -.
DR ProteomicsDB; 77314; -.
DR Antibodypedia; 22662; 77 antibodies from 14 providers.
DR DNASU; 220136; -.
DR Ensembl; ENST00000398545.5; ENSP00000381553.3; ENSG00000172361.6.
DR GeneID; 220136; -.
DR KEGG; hsa:220136; -.
DR MANE-Select; ENST00000398545.5; ENSP00000381553.3; NM_145020.5; NP_659457.2.
DR UCSC; uc002lee.4; human.
DR CTD; 220136; -.
DR DisGeNET; 220136; -.
DR GeneCards; CFAP53; -.
DR HGNC; HGNC:26530; CFAP53.
DR HPA; ENSG00000172361; Group enriched (fallopian tube, testis).
DR MalaCards; CFAP53; -.
DR MIM; 614759; gene.
DR MIM; 614779; phenotype.
DR neXtProt; NX_Q96M91; -.
DR OpenTargets; ENSG00000172361; -.
DR Orphanet; 157769; Situs ambiguus.
DR Orphanet; 101063; Situs inversus totalis.
DR PharmGKB; PA134960690; -.
DR VEuPathDB; HostDB:ENSG00000172361; -.
DR eggNOG; ENOG502QRDR; Eukaryota.
DR GeneTree; ENSGT01050000244995; -.
DR HOGENOM; CLU_036489_1_0_1; -.
DR InParanoid; Q96M91; -.
DR OMA; MQIAHQQ; -.
DR OrthoDB; 1167111at2759; -.
DR PhylomeDB; Q96M91; -.
DR TreeFam; TF329393; -.
DR PathwayCommons; Q96M91; -.
DR SignaLink; Q96M91; -.
DR SIGNOR; Q96M91; -.
DR BioGRID-ORCS; 220136; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; CFAP53; human.
DR GenomeRNAi; 220136; -.
DR Pharos; Q96M91; Tbio.
DR PRO; PR:Q96M91; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96M91; protein.
DR Bgee; ENSG00000172361; Expressed in bronchial epithelial cell and 128 other tissues.
DR Genevisible; Q96M91; HS.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0060271; P:cilium assembly; IEA:InterPro.
DR GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:UniProtKB.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; ISS:UniProtKB.
DR InterPro; IPR033365; CFAP53.
DR InterPro; IPR043596; CFAP53/TCHP.
DR InterPro; IPR043597; TPH_dom.
DR PANTHER; PTHR31183; PTHR31183; 1.
DR PANTHER; PTHR31183:SF1; PTHR31183:SF1; 1.
DR Pfam; PF13868; TPH; 1.
PE 1: Evidence at protein level;
KW Cell projection; Ciliopathy; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Disease variant; Heterotaxy; Reference proteome.
FT CHAIN 1..514
FT /note="Cilia- and flagella-associated protein 53"
FT /id="PRO_0000089407"
FT COILED 91..148
FT /evidence="ECO:0000255"
FT COILED 203..474
FT /evidence="ECO:0000255"
FT VARIANT 158
FT /note="R -> G (in HTX6; unknown pathological significance;
FT dbSNP:rs886037751)"
FT /evidence="ECO:0000269|PubMed:26531781"
FT /id="VAR_077590"
FT VARIANT 231
FT /note="R -> C (in dbSNP:rs12607385)"
FT /id="VAR_050746"
FT VARIANT 294
FT /note="E -> K (in dbSNP:rs35193847)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_050747"
SQ SEQUENCE 514 AA; 61835 MW; 50D8D72F26D227E3 CRC64;
MYSQRFGTVQ REVKGPTPKV VIVRSKPPKG QGAEHHLERI RRSHQKHNAI LASIKSSERD
RLKAEWDQHN DCKILDSLVR ARIKDAVQGF IINIEERRNK LRELLALEEN EYFTEMQLKK
ETIEEKKDRM REKTKLLKEK NEKERQDFVA EKLDQQFRER CEELRVELLS IHQKKVCEER
KAQIAFNEEL SRQKLVEEQM FSKLWEEDRL AKEKREAQEA RRQKELMENT RLGLNAQITS
IKAQRQATQL LKEEEARLVE SNNAQIKHEN EQDMLKKQKA KQETRTILQK ALQERIEHIQ
QEYRDEQDLN MKLVQRALQD LQEEADKKKQ KREDMIREQK IYHKYLAQRR EEEKAQEKEF
DRILEEDKAK KLAEKDKELR LEKEARRQLV DEVMCTRKLQ VQEKLQREAK EQEERAMEQK
HINESLKELN CEEKENFARR QRLAQEYRKQ LQMQIAYQQQ SQEAEKEEKR REFEAGVAAN
KMCLDKVQEV LSTHQVLPQN IHPMRKACPS KLPP
