CF157_MOUSE
ID CF157_MOUSE Reviewed; 523 AA.
AC Q0VFX2; Q9DA63;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cilia- and flagella-associated protein 157 {ECO:0000305};
GN Name=Cfap157 {ECO:0000312|MGI:MGI:2447809};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION
RP PHENOTYPE, AND INTERACTION WITH TUBB; TUBA4A AND CEP350.
RX PubMed=27965440; DOI=10.1242/dev.139626;
RA Weidemann M., Schuster-Gossler K., Stauber M., Wrede C., Hegermann J.,
RA Ott T., Boldt K., Beyer T., Serth K., Kremmer E., Blum M., Ueffing M.,
RA Gossler A.;
RT "CFAP157 is a murine downstream effector of FOXJ1 that is specifically
RT required for flagellum morphogenesis and sperm motility.";
RL Development 143:4736-4748(2016).
CC -!- FUNCTION: Specifically required during spermatogenesis for flagellum
CC morphogenesis and sperm motility (PubMed:27965440). May be required to
CC suppress the formation of supernumerary axonemes and ensure a correct
CC ultrastructure (PubMed:27965440). {ECO:0000269|PubMed:27965440}.
CC -!- SUBUNIT: Interacts with TUBB and TUBA4A (PubMed:27965440). Interacts
CC with CEP350 (PubMed:27965440). {ECO:0000269|PubMed:27965440}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:27965440}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in tissues containing motile
CC cilia. {ECO:0000269|PubMed:27965440}.
CC -!- INDUCTION: Expression is activated by FOXJ1.
CC {ECO:0000269|PubMed:27965440}.
CC -!- DISRUPTION PHENOTYPE: Mice were born at expected Mendelian ratios and
CC appear normal but homozygous males are infertile. Spermatozoa display
CC impaired motility due to defects in the axoneme. Sperm cells show an
CC axonemal loop of the midpiece, supernumerary axonemes and a disrupted
CC axonemal arrangement, as well as defective axonemes along the flagella.
CC {ECO:0000269|PubMed:27965440}.
CC -!- SIMILARITY: Belongs to the CFAP157 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24421.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK006127; BAB24421.1; ALT_FRAME; mRNA.
DR EMBL; AL772271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118617; AAI18618.1; -; mRNA.
DR EMBL; BC121825; AAI21826.1; -; mRNA.
DR CCDS; CCDS15932.1; -.
DR RefSeq; NP_079895.1; NM_025619.1.
DR AlphaFoldDB; Q0VFX2; -.
DR SMR; Q0VFX2; -.
DR STRING; 10090.ENSMUSP00000099877; -.
DR PhosphoSitePlus; Q0VFX2; -.
DR MaxQB; Q0VFX2; -.
DR PaxDb; Q0VFX2; -.
DR PeptideAtlas; Q0VFX2; -.
DR PRIDE; Q0VFX2; -.
DR ProteomicsDB; 283889; -.
DR Antibodypedia; 7779; 100 antibodies from 19 providers.
DR Ensembl; ENSMUST00000102813; ENSMUSP00000099877; ENSMUSG00000038987.
DR GeneID; 227736; -.
DR KEGG; mmu:227736; -.
DR UCSC; uc008jgz.1; mouse.
DR CTD; 286207; -.
DR MGI; MGI:2447809; Cfap157.
DR VEuPathDB; HostDB:ENSMUSG00000038987; -.
DR eggNOG; ENOG502QQK8; Eukaryota.
DR GeneTree; ENSGT00730000111240; -.
DR HOGENOM; CLU_025198_2_0_1; -.
DR InParanoid; Q0VFX2; -.
DR OMA; TFYELQI; -.
DR OrthoDB; 1171749at2759; -.
DR PhylomeDB; Q0VFX2; -.
DR TreeFam; TF329637; -.
DR BioGRID-ORCS; 227736; 0 hits in 41 CRISPR screens.
DR ChiTaRS; Cfap157; mouse.
DR PRO; PR:Q0VFX2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q0VFX2; protein.
DR Bgee; ENSMUSG00000038987; Expressed in spermatid and 58 other tissues.
DR Genevisible; Q0VFX2; MM.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:UniProtKB.
DR InterPro; IPR038844; CFAP157.
DR PANTHER; PTHR31954; PTHR31954; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..523
FT /note="Cilia- and flagella-associated protein 157"
FT /id="PRO_0000307225"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..191
FT /evidence="ECO:0000255"
FT COILED 248..274
FT /evidence="ECO:0000255"
FT COILED 302..371
FT /evidence="ECO:0000255"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4V7B0"
FT CONFLICT 224
FT /note="E -> D (in Ref. 1; BAB24421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 61048 MW; A3B32054ECA4527A CRC64;
MAPKKKPNKG GKEMQGKKIG GKKDASGTKT PELAMVEELK EFYHKQIQDL EDRLARYQRK
WDELAVREKL FHQEFEQLAN NKKEIVAFLK RTLNQKVDEI TDLNDQLQSL EVAKDMEKDA
FEAQLAQVRH EFQEIKDQLT TENIALGIKL SSLEEFRLQK EELTEKYLAL EEQLHRQEGE
YKEYVYNLEK KSVLDKDRLR KEIIQRVNLV ATEFRKMATN QMWETTRRAI LENNSVTLQL
NKVSKHGVQL LQENEQLKGT QNKLCQQLEM LENTQEIMAR KNIGHKKIIL MLTEKCRQQR
KGTEETEQLR LLLSQLEQNF QNVQRDNQTL RSEKDQLEAQ LKEKQAEANR LQEELTKEQK
IRANLKTVLI QATSMLQDIV HMQTEAEDGD FDVVFQLQRK ELLQQLLVLL SSGVVLKTQP
DMGSHQDKQP QGLSKESQRI TQTSKEGAVS LLQQLSTITT YKPGDLGLVP RRPVRIPLKP
QDLRPLSYIT RMGICQNTNE IYPSGALKRF RKFTLPRPFL HRK
