ID   ODF2L_MOUSE             Reviewed;         642 AA.
AC   Q9D478; Q8CD32; Q8VDY5; Q9D647;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Protein BCAP {ECO:0000305};
DE   AltName: Full=Basal body centriole-associated protein {ECO:0000303|PubMed:28775150};
DE   AltName: Full=Outer dense fiber protein 2-like;
GN   Name=Odf2l; Synonyms=Bcap {ECO:0000303|PubMed:28775150}, D3Ertd250e;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin, and 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 MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   FUNCTION.
RX   PubMed=28775150; DOI=10.1242/jcs.196642;
RA   de Saram P., Iqbal A., Murdoch J.N., Wilkinson C.J.;
RT   "BCAP is a centriolar satellite protein and inhibitor of ciliogenesis.";
RL   J. Cell Sci. 130:3360-3373(2017).
CC   -!- FUNCTION: Acts as a suppressor of ciliogenesis, specifically, the
CC       initiation of ciliogenesis. {ECO:0000269|PubMed:28775150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriolar satellite
CC       {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:Q9ULJ1}. Note=Localizes to centrioles in
CC       proliferative cells and basal bodies in ciliated cells. Disappears
CC       during ciliogenesis but reappears, albeit at a lower levels once
CC       ciliogenesis has completed. {ECO:0000250|UniProtKB:Q9ULJ1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D478-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D478-2; Sequence=VSP_029062;
CC       Name=3;
CC         IsoId=Q9D478-3; Sequence=VSP_029061, VSP_029062;
CC   -!- SIMILARITY: Belongs to the ODF2 family. {ECO:0000305}.
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DR   EMBL; AK014630; BAB29473.1; -; mRNA.
DR   EMBL; AK016726; BAB30400.1; -; mRNA.
DR   EMBL; AK031564; BAC27451.1; -; mRNA.
DR   EMBL; BC020075; AAH20075.1; -; mRNA.
DR   CCDS; CCDS17891.1; -. [Q9D478-2]
DR   CCDS; CCDS51087.1; -. [Q9D478-1]
DR   CCDS; CCDS51088.1; -. [Q9D478-3]
DR   RefSeq; NP_001156010.1; NM_001162538.1. [Q9D478-1]
DR   RefSeq; NP_001156011.1; NM_001162539.1. [Q9D478-3]
DR   RefSeq; NP_079990.2; NM_025714.4. [Q9D478-2]
DR   RefSeq; XP_011238462.1; XM_011240160.2.
DR   RefSeq; XP_011238463.1; XM_011240161.2. [Q9D478-3]
DR   RefSeq; XP_017175133.1; XM_017319644.1.
DR   AlphaFoldDB; Q9D478; -.
DR   SMR; Q9D478; -.
DR   BioGRID; 206436; 2.
DR   STRING; 10090.ENSMUSP00000096140; -.
DR   iPTMnet; Q9D478; -.
DR   PhosphoSitePlus; Q9D478; -.
DR   EPD; Q9D478; -.
DR   MaxQB; Q9D478; -.
DR   PaxDb; Q9D478; -.
DR   PRIDE; Q9D478; -.
DR   ProteomicsDB; 293922; -. [Q9D478-1]
DR   ProteomicsDB; 293923; -. [Q9D478-2]
DR   ProteomicsDB; 293924; -. [Q9D478-3]
DR   Antibodypedia; 33581; 114 antibodies from 23 providers.
DR   DNASU; 52184; -.
DR   Ensembl; ENSMUST00000029920; ENSMUSP00000029920; ENSMUSG00000028256. [Q9D478-3]
DR   Ensembl; ENSMUST00000098538; ENSMUSP00000096140; ENSMUSG00000028256. [Q9D478-1]
DR   Ensembl; ENSMUST00000098539; ENSMUSP00000096141; ENSMUSG00000028256. [Q9D478-2]
DR   Ensembl; ENSMUST00000106192; ENSMUSP00000101798; ENSMUSG00000028256. [Q9D478-2]
DR   GeneID; 52184; -.
DR   KEGG; mmu:52184; -.
DR   UCSC; uc008rqi.2; mouse. [Q9D478-1]
DR   UCSC; uc008rqj.2; mouse. [Q9D478-2]
DR   UCSC; uc008rql.2; mouse. [Q9D478-3]
DR   CTD; 57489; -.
DR   MGI; MGI:1098600; Odf2l.
DR   VEuPathDB; HostDB:ENSMUSG00000028256; -.
DR   eggNOG; ENOG502R83P; Eukaryota.
DR   GeneTree; ENSGT00530000063497; -.
DR   HOGENOM; CLU_018326_1_0_1; -.
DR   InParanoid; Q9D478; -.
DR   OMA; WKSRYEK; -.
DR   OrthoDB; 328077at2759; -.
DR   PhylomeDB; Q9D478; -.
DR   TreeFam; TF328605; -.
DR   BioGRID-ORCS; 52184; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Odf2l; mouse.
DR   PRO; PR:Q9D478; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9D478; protein.
DR   Bgee; ENSMUSG00000028256; Expressed in spermatocyte and 205 other tissues.
DR   ExpressionAtlas; Q9D478; baseline and differential.
DR   Genevisible; Q9D478; MM.
DR   GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR   GO; GO:1902017; P:regulation of cilium assembly; IBA:GO_Central.
DR   InterPro; IPR026102; BCAP.
DR   InterPro; IPR026099; Odf2-rel.
DR   PANTHER; PTHR23162; PTHR23162; 1.
DR   PANTHER; PTHR23162:SF7; PTHR23162:SF7; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..642
FT                   /note="Protein BCAP"
FT                   /id="PRO_0000308910"
FT   COILED          31..58
FT                   /evidence="ECO:0000255"
FT   COILED          128..226
FT                   /evidence="ECO:0000255"
FT   COILED          254..603
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         81..123
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029061"
FT   VAR_SEQ         423..475
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029062"
FT   CONFLICT        27
FT                   /note="Q -> R (in Ref. 1; BAB29473)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   642 AA;  74151 MW;  05E641CBA334CABC CRC64;
     MEMPTSDGSL SEGLISYLIR ERGSAPQCAP EKHLSRLKQD VANTKMELKA TLKEAQLASC
     SVELLLPLFK NTVEGISLEN ANLSASSLKK IFEQNDILSK ELDTFNRVKL ALEHLIKQTD
     YEQIGDSLLC LLKDLSDNES ENRNLEEKVL EKETYIRELS CLFQNEKESA LKANRLSQSV
     KVVHDRLQRQ IQKREAENEK LKEHVQSLET QIAKWNLQVK MNKQEAVAIK EASRQKAVAL
     KKASKVYRQR LRHFTGDIER LASQVRDQEA KLSETVSASS DWKSQFEKIA IEKTELEVQI
     ETMKKQIANL LEDLRKMETH GKNSCEEILR KLHSLEDENE ALNIENVKLK GTLDALKDEV
     ASVENELVEL QEVEKRQKTL VEGYRTQVQK LQEAAEMVKS RCKNLLHENN LIITNKNKKL
     EKMRGQVESN LKQVEQARSS FTSAEQRLQE CQEKLQRCKE KCAEQALTIR ELQGQVDGNQ
     SLLTKLSLEE ENHLIQLKCE NLKEKLEQMD AENKELEKKL ADQEECLKHS DLELKEKAAE
     YTALSRQLEA ALEEGRQKVS EEVEKMSSRE RALQIKILDL EAELRKKNEE QNQLVDKMNT
     KTQHQAICLK EIQHSLEKSE TRNESIKNYL QFLQISYVTM FR