TT21B_MOUSE
ID TT21B_MOUSE Reviewed; 1315 AA.
AC Q0HA38; Q3V1U7; Q69Z46;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Tetratricopeptide repeat protein 21B;
DE Short=TPR repeat protein 21B;
DE AltName: Full=Intraflagellar transport 139 homolog;
DE AltName: Full=Tetratricopeptide repeat-containing hedgehog modulator 1;
GN Name=Ttc21b; Synonyms=Ift139 {ECO:0000303|PubMed:25860617}, Kiaa1992, Thm1;
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, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=A/J;
RX PubMed=18327258; DOI=10.1038/ng.105;
RA Tran P.V., Haycraft C.J., Besschetnova T.Y., Turbe-Doan A., Stottmann R.W.,
RA Herron B.J., Chesebro A.L., Qiu H., Scherz P.J., Shah J.V., Yoder B.K.,
RA Beier D.R.;
RT "THM1 negatively modulates mouse sonic hedgehog signal transduction and
RT affects retrograde intraflagellar transport in cilia.";
RL Nat. Genet. 40:403-410(2008).
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] OF 667-1315.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 994-1315.
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH TTC25.
RX PubMed=25860617; DOI=10.1371/journal.pone.0124378;
RA Xu Y., Cao J., Huang S., Feng D., Zhang W., Zhu X., Yan X.;
RT "Characterization of tetratricopeptide repeat-containing proteins critical
RT for cilia formation and function.";
RL PLoS ONE 10:E0124378-E0124378(2015).
CC -!- FUNCTION: Component of the IFT complex A (IFT-A), a complex required
CC for retrograde ciliary transport and entry into cilia of G protein-
CC coupled receptors (GPCRs). Essential for retrograde trafficking of IFT-
CC 1, IFT-B and GPCRs (By similarity). Negatively modulates the SHH signal
CC transduction (PubMed:18327258). {ECO:0000250|UniProtKB:Q7Z4L5,
CC ECO:0000269|PubMed:18327258}.
CC -!- SUBUNIT: Component of the IFT complex A (IFT-A) complex. IFT-A complex
CC is divided into a core subcomplex composed of IFT122:IFT140:WDR19 which
CC is associated with TULP3 and a peripheral subcomplex composed of
CC IFT43:WDR35:TTC21B. Interacts directy with WDR35 and TTC21B (By
CC similarity). Interacts with TTC25 (PubMed:25860617).
CC {ECO:0000250|UniProtKB:Q7Z4L5, ECO:0000269|PubMed:25860617}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:18327258}. Note=In polarized epithelial inner
CC medullary collecting ducts cells and in the nodes of mice at 8.0 dpc,
CC colocalizes with alpha-tubulin in cilia. Expressed in a punctate manner
CC throughout the axoneme from the cilia base to the tip.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc, widely expressed with more intense
CC expression in the maxillary prominence, branchial arches, limb buds,
CC somites and spinal cord. {ECO:0000269|PubMed:18327258}.
CC -!- SIMILARITY: Belongs to the TTC21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32598.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32598.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; DQ011164; AAY79164.1; -; mRNA.
DR EMBL; AL844526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK132240; BAE21052.1; -; mRNA.
DR EMBL; AK173320; BAD32598.1; ALT_SEQ; mRNA.
DR CCDS; CCDS16076.1; -.
DR RefSeq; NP_001041069.1; NM_001047604.2.
DR AlphaFoldDB; Q0HA38; -.
DR BioGRID; 216179; 3.
DR ComplexPortal; CPX-5027; IFT-A complex.
DR STRING; 10090.ENSMUSP00000099779; -.
DR iPTMnet; Q0HA38; -.
DR PhosphoSitePlus; Q0HA38; -.
DR MaxQB; Q0HA38; -.
DR PaxDb; Q0HA38; -.
DR PRIDE; Q0HA38; -.
DR ProteomicsDB; 300145; -.
DR Antibodypedia; 47994; 48 antibodies from 9 providers.
DR Ensembl; ENSMUST00000102718; ENSMUSP00000099779; ENSMUSG00000034848.
DR GeneID; 73668; -.
DR KEGG; mmu:73668; -.
DR UCSC; uc008jwv.2; mouse.
DR CTD; 79809; -.
DR MGI; MGI:1920918; Ttc21b.
DR VEuPathDB; HostDB:ENSMUSG00000034848; -.
DR eggNOG; ENOG502QQAB; Eukaryota.
DR GeneTree; ENSGT00390000005979; -.
DR HOGENOM; CLU_006149_0_0_1; -.
DR InParanoid; Q0HA38; -.
DR OMA; PEWGQQA; -.
DR OrthoDB; 45918at2759; -.
DR PhylomeDB; Q0HA38; -.
DR TreeFam; TF314664; -.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 73668; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Ttc21b; mouse.
DR PRO; PR:Q0HA38; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q0HA38; protein.
DR Bgee; ENSMUSG00000034848; Expressed in spermatocyte and 218 other tissues.
DR ExpressionAtlas; Q0HA38; baseline and differential.
DR Genevisible; Q0HA38; MM.
DR GO; GO:0005929; C:cilium; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0030991; C:intraciliary transport particle A; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IMP:MGI.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IC:ComplexPortal.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0021798; P:forebrain dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:MGI.
DR GO; GO:1903999; P:negative regulation of eating behavior; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR GO; GO:0097499; P:protein localization to non-motile cilium; IMP:MGI.
DR GO; GO:1905799; P:regulation of intraciliary retrograde transport; ISS:UniProtKB.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 5.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR040364; TTC21A/TTC21B.
DR PANTHER; PTHR14699; PTHR14699; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 15.
DR SUPFAM; SSF48452; SSF48452; 4.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 4.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cytoplasm; Cytoskeleton; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..1315
FT /note="Tetratricopeptide repeat protein 21B"
FT /id="PRO_0000291918"
FT REPEAT 108..141
FT /note="TPR 1"
FT REPEAT 145..178
FT /note="TPR 2"
FT REPEAT 192..225
FT /note="TPR 3"
FT REPEAT 285..323
FT /note="TPR 4"
FT REPEAT 324..357
FT /note="TPR 5"
FT REPEAT 492..525
FT /note="TPR 6"
FT REPEAT 563..596
FT /note="TPR 7"
FT REPEAT 616..649
FT /note="TPR 8"
FT REPEAT 721..754
FT /note="TPR 9"
FT REPEAT 756..788
FT /note="TPR 10"
FT REPEAT 790..821
FT /note="TPR 11"
FT REPEAT 830..863
FT /note="TPR 12"
FT REPEAT 883..916
FT /note="TPR 13"
FT REPEAT 918..950
FT /note="TPR 14"
FT REPEAT 951..984
FT /note="TPR 15"
FT REPEAT 1022..1055
FT /note="TPR 16"
FT REPEAT 1196..1229
FT /note="TPR 17"
FT REPEAT 1231..1263
FT /note="TPR 18"
FT REPEAT 1265..1298
FT /note="TPR 19"
SQ SEQUENCE 1315 AA; 150795 MW; B4D73ACE5511268A CRC64;
MDSQGLKTLI NYYCQERYYH HVLLVASEGM KKYSSDPVFR FYHAYGTLME GKAQEALREF
EAIKNKQDVS LCSLMALMYV HKMSPNPDRE AILELDTKMK EQRKEAGRKA LYHAGLFLWH
IGRHDKAREY IDRMSKMPHD SNEGPILKAW LDITRGKEPY AKKALRYFEE GLQDGNDIFA
LLGKVLCLEI RQNYSGALET VSQIIVNFPS FLPAFEKKMK LQLALQDWDQ TVETAQRLLL
QDNHNVEALR MLALYYLCRE GDVEKAATKL ENLGNALDVM EPQNAQLFYK ITLAFSRTCG
RNQLILQKVQ SFLEKAFSLT PQQAEIATEL GYQMILQGKV KEAWKWYRTA MTLNESNISA
VTGLIRCQLI EGQLQDADQQ LEFFSEFQQS MGKSAELMYL HAVLATKKNN RQDEVINLLN
DVVNTHFSHL EDLPLGIQYF EKLNPDFLLE VVTEYLNLCP IQPAGPGQPL SPVLRRCSSV
LETIIRSVPG LPQAVFLMAK VKYLSGDTEA AYNNLQHCLE HSPSYAEAHL LMAQVYLSQD
KVKLCSQSLE LCLSYNFNVR EYPLYHLIKA QSQKKMGEVA EAIKTLHMAM NLPGMRRSRA
SSKSKHRTEV DASHRLSIFL ELVEVHRLNG EQHEAAKVLQ DAIHEFSGTC EELRVTIANA
DLALAQGDTD RALSMLRNVT TEQPYFIEAK EKMADIYLKH RKEKMLYITC YREIAERMPS
PRSFLLLGDA YMNIQEPEEA IVAYEQALNQ NPKDGTLARK IGKALVKTHN YSKAITYYEA
ALKSGQQNCL CYDLAELLLR LKLYEKAEKV LQHSLAHEPV SELSALMVDG RSQVLLAKVY
SKMERPSDAI AALQQARELQ ARILKRVQME QPDAVPSQKH FAAEICAEIA KHSAAQRDYE
KAITFYREAL VHCETDSKIM LELAQLYLAQ EDLDASLRHC ALLLQRDQDN EPATMLMADL
MFRKQDYEQA VYHLQQLLDR KPDNFMTLSR LIDLLRRCGK LEDVPRFFLM AEKHNSRTKL
EPGFQYCKGL HFWYTGEPND ALRHFNKARK DSDWGQNALY NMIEICLNPD NETIGGEVFE
NLNGDLGTSP EKQESVQLAV RTAEKLLKEL KPQTVQGRLQ LRIMENCCLM ATKQKSSVEQ
ALNTFTEIAA SEKDHIPALL GMATAYMILK QTPKARNQLK RIAKMPWNPI EAEDLEKSWL
LLADIYIQSA KYDMAEELLK RCLCHNRSCC KAYEYMGYIM EKEQAYTDAA FNYEMAWKHS
NQTNPAVGYK LAFNYLKAKR YVDAIDVCHQ VLEAHPTYPK IRKDILDKAR ASLRP
