TGRM1_MOUSE
ID TGRM1_MOUSE Reviewed; 1776 AA.
AC Q6A070; F8WJB2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=TOG array regulator of axonemal microtubules protein 1;
DE AltName: Full=Crescerin-1 {ECO:0000303|PubMed:26378256};
DE AltName: Full=Protein FAM179B;
GN Name=Togaram1; Synonyms=Fam179b, Kiaa0423;
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] (ISOFORM 2).
RC TISSUE=Brain;
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 [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 MUTAGENESIS OF ARG-367, AND FUNCTION.
RX PubMed=32747439; DOI=10.1136/jmedgenet-2020-106833;
RA Morbidoni V., Agolini E., Slep K.C., Pannone L., Zuccarello D., Cassina M.,
RA Grosso E., Gai G., Salviati L., Dallapiccola B., Novelli A., Martinelli S.,
RA Trevisson E.;
RT "Biallelic mutations in the TOGARAM1 gene cause a novel primary
RT ciliopathy.";
RL J. Med. Genet. 58:526-533(2021).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 332-620, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF TYR-364; TRP-1274 AND PHE-1559.
RX PubMed=26378256; DOI=10.1091/mbc.e15-08-0603;
RA Das A., Dickinson D.J., Wood C.C., Goldstein B., Slep K.C.;
RT "Crescerin uses a TOG domain array to regulate microtubules in the primary
RT cilium.";
RL Mol. Biol. Cell 26:4248-4264(2015).
CC -!- FUNCTION: Involved in ciliogenesis. It is required for appropriate
CC acetylation and polyglutamylation of ciliary microtubules, and
CC regulation of cilium length (By similarity). Interacts with
CC microtubules and promotes microtubule polymerization via its HEAT
CC repeat domains, especially those in TOG region 2 and 4
CC (PubMed:26378256, PubMed:32747439). {ECO:0000250|UniProtKB:Q17423,
CC ECO:0000269|PubMed:26378256, ECO:0000269|PubMed:32747439}.
CC -!- SUBUNIT: Interacts with ARMC9. Interacts with CCDC66, CEP104 and CSPP1.
CC {ECO:0000250|UniProtKB:Q9Y4F4}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:26378256}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:26378256}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q9Y4F4}. Note=Detected along the length of
CC primary cilia and at the basal body. Colocalization with the
CC cytoplasmic microtubule cytoskeleton upon heterologous expression is
CC most likely an artifact. {ECO:0000269|PubMed:26378256}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6A070-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6A070-2; Sequence=VSP_047942;
CC -!- DOMAIN: The TOG regions are composed of HEAT-type repeats that assemble
CC into a solenoid structure. They mediate interaction with microtubules.
CC {ECO:0000269|PubMed:26378256}.
CC -!- SIMILARITY: Belongs to the Crescerin family. {ECO:0000305}.
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DR EMBL; AK172948; BAD32226.1; -; Transcribed_RNA.
DR EMBL; AC159621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49075.1; -. [Q6A070-1]
DR RefSeq; NP_808473.2; NM_177805.3. [Q6A070-1]
DR PDB; 5DN7; X-ray; 2.20 A; A=332-620.
DR PDBsum; 5DN7; -.
DR AlphaFoldDB; Q6A070; -.
DR SMR; Q6A070; -.
DR BioGRID; 236543; 2.
DR STRING; 10090.ENSMUSP00000070382; -.
DR iPTMnet; Q6A070; -.
DR PhosphoSitePlus; Q6A070; -.
DR PaxDb; Q6A070; -.
DR PRIDE; Q6A070; -.
DR ProteomicsDB; 262904; -. [Q6A070-1]
DR ProteomicsDB; 262905; -. [Q6A070-2]
DR Antibodypedia; 23425; 13 antibodies from 6 providers.
DR DNASU; 328108; -.
DR Ensembl; ENSMUST00000066296; ENSMUSP00000070382; ENSMUSG00000035614. [Q6A070-1]
DR GeneID; 328108; -.
DR KEGG; mmu:328108; -.
DR UCSC; uc007nqs.2; mouse. [Q6A070-1]
DR CTD; 23116; -.
DR MGI; MGI:2684313; Togaram1.
DR VEuPathDB; HostDB:ENSMUSG00000035614; -.
DR eggNOG; KOG2933; Eukaryota.
DR GeneTree; ENSGT00940000158712; -.
DR HOGENOM; CLU_002584_1_0_1; -.
DR InParanoid; Q6A070; -.
DR OMA; HSSDELC; -.
DR OrthoDB; 476837at2759; -.
DR PhylomeDB; Q6A070; -.
DR TreeFam; TF315518; -.
DR BioGRID-ORCS; 328108; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Togaram1; mouse.
DR PRO; PR:Q6A070; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6A070; protein.
DR Bgee; ENSMUSG00000035614; Expressed in otolith organ and 225 other tissues.
DR ExpressionAtlas; Q6A070; baseline and differential.
DR Genevisible; Q6A070; MM.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
DR DisProt; DP02882; -.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028401; Crescerin-1.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR21567:SF6; PTHR21567:SF6; 2.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Reference proteome;
KW Repeat.
FT CHAIN 1..1776
FT /note="TOG array regulator of axonemal microtubules protein
FT 1"
FT /id="PRO_0000251953"
FT REPEAT 175..212
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 214..246
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 250..288
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 344..383
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 389..426
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 430..465
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 466..503
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 505..542
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 1297..1334
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1338..1375
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1541..1578
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1582..1619
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1623..1661
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REGION 94..311
FT /note="TOG 1"
FT /evidence="ECO:0000303|PubMed:26378256"
FT REGION 351..595
FT /note="TOG 2"
FT /evidence="ECO:0000303|PubMed:26378256"
FT REGION 655..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1481
FT /note="TOG 3"
FT /evidence="ECO:0000303|PubMed:26378256"
FT REGION 1493..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1776
FT /note="TOG 4"
FT /evidence="ECO:0000303|PubMed:26378256"
FT COMPBIAS 826..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1659..1675
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_047942"
FT MUTAGEN 364
FT /note="Y->E: Expected to disrupt microtubule binding.
FT Abolishes the ability to promote microtubule
FT polymerization."
FT /evidence="ECO:0000269|PubMed:26378256"
FT MUTAGEN 367
FT /note="R->W: Resulty in increased tubulin polymerization in
FT vitro."
FT /evidence="ECO:0000269|PubMed:32747439"
FT MUTAGEN 1274
FT /note="W->E: Abolishes association with microtubules."
FT /evidence="ECO:0000269|PubMed:26378256"
FT MUTAGEN 1559
FT /note="F->E: Abolishes association with microtubules and
FT the ability to promote microtubule polymerization."
FT /evidence="ECO:0000269|PubMed:26378256"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 407..424
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 425..431
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 432..441
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 448..465
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 467..475
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 483..499
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 507..514
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 515..519
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 523..540
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 546..553
FT /evidence="ECO:0007829|PDB:5DN7"
FT HELIX 564..573
FT /evidence="ECO:0007829|PDB:5DN7"
SQ SEQUENCE 1776 AA; 194910 MW; A7EA4B2D7B1DC5BC CRC64;
MAAAPSELLP LPPPATPGSY RLLSRCRPYA PGTDGRRSGG TMRGEKNYYC RGAAGDHGSC
PATPSPLAST LLLPAEAVST SWSGPGSGLS GGDEEETRLL QLLRTAPDPS EAFQALQAAL
PRRGGRLGFP RRKEALYRAL GRVLVEGGSE EKRLCLQLLS DVLRGQGEAG QLEEAFSLAL
LPQLVVSLRE DNPALRKDAL QILHICLRRS SGQVLRTLIQ GLESPDARLR ASTALLLPIL
FTPEDLLQGL DLTEVIISLA RKLGDQEMEE ESETAFSSLQ QIGERLGQER FHSYISRLPS
ALRRHYNRRL ESQYGSQVPY YLELEASGFS EDAAPCVVNL SSSNLKFEII PQELHARLLD
QEDYKNRTQA VEELKQLLGK FNPSSTPHAS LVGFISLLYN LLDDSNFKVV HGTLQVLHLL
VIRLGEQVQQ FLGPVIAASV KVLADNKLVI KQEYMKIFLK LMKEVGPQRV LSLLLENLKH
KHSRVREEVV NICICSLLTY PSEDFDLPKL SFDLAPALVD SKRRVRQAAL EAFAVLASSM
GSGKTNVLFK AVDTVELQDN GDGVMNAVQA RLARKTLPRL TEQGFVEYAI LMPSSAQGRS
SHLAHGADTD WLMSGNRTQS AHCYCGDHTR DSMQLYGSYS PTICTRRVLS AGKGKNKLPW
ENEQPGVMGE NQTSNSKDIK DTEQFSAHDL IPSPKLKPSQ GMPASDDLCF SKKRSSRNLF
QSSRDFNSES VPTCGAGNTA DLQTNLPGKC GQLGLSQIGC RTGSVGSDLQ FLGTANGHQD
KVYASIDFGS KTQQTFGSQS ERTSSYSGSN ASPGSFILPS YPLASPRTSP KHTSPLSVAP
KKSQDNSISF SNSWPLKSFE GLSKPSPQKK LANQKSSDPT GENFQEKTTA VQLTPALVRS
PSSRRGLNGT KPVPPIPRGI NLLPDKADLS TMGHMKKQPD DIWKSEKDNL TIDLSELNFR
DKDLDQEEMH SSLRSLRNSA AKKRAKLSGS SSTSDVDSPD SAMKLELTID SPSRASSPNI
SSYSESGVYS QESLTSSLST TPQGKRIMSD IFPTFGSKPC STRLSSAKKT SHAAEQSPSA
GFTRSSNLQQ ISSFDFTSTN TLSEDSVVIV GKGVFGNPNS APTTCSQPVI SSVESEDTFP
VKPSIEPPSG VYGRAVQHNA PLYPEVENDK DTKVSIAKST YEKMRQKRKE EKELLDAKDC
ERKETNPWER IKHLGSEKMT SENEPSSGVI PQYKERMSSV THSPEIMDSL ELRPFSKPDI
ALTEALRLLA DEDWEKKMEG LNFVRCLAAF HSDLLNTKLH ETTFAVVQEV KNLRSGVSRA
AVVCLGDLFT YLKKSMDQEL DSAVRALLHK AGESNTFIRE DVDKALKAMV NNVTPARAVT
SLINGGQSHL HIAVRRCTAQ HLADVVECMD PERISSGTKD MADRLLPAAA KFAQDSSQET
RYYGRKMLFL MMGHPNFEKL LEKYIPSKDL PYIKESVKNL RLKGLGEIPL DTASAKGRRS
HPGSVGNTRS SSVSRDAFSS SEREVTEVRE VPRKSAPRNS LESAEYIKVI TGLLNAKDFR
DRINGIKQLL SDTENNQELV VGNIVKIFDA FKSRLHDSNS KVNLVALETM HKMIPLLRDN
LSPIINMLIP AIVDNNLNSK NPGIYAAATN VVHALSQHVD NYLLLQPFCT KAQFLNGKAK
QDMTEKLADI VTELYQRKPH ATEQKVLVVL WHLLGNMTHS GSLPGAGGNI RTATAKLSKA
LFTQMGQNLL NQAASQPPHI KKSLEELLDV TVLSEL
