CREC_CAEEL
ID CREC_CAEEL Reviewed; 1282 AA.
AC Q17423; E9P869; E9P870; M1ZMI6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Crescerin-like protein che-12 {ECO:0000305};
GN Name=che-12 {ECO:0000303|PubMed:18245347, ECO:0000312|WormBase:B0024.8a};
GN ORFNames=B0024.8 {ECO:0000312|WormBase:B0024.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAA94880.3};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18245347; DOI=10.1534/genetics.107.082453;
RA Bacaj T., Lu Y., Shaham S.;
RT "The conserved proteins CHE-12 and DYF-11 are required for sensory cilium
RT function in Caenorhabditis elegans.";
RL Genetics 178:989-1002(2008).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF PHE-34; ALA-281; TRP-815 AND TRP-1073.
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).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF 645-TRP--ARG-1282.
RX PubMed=26976437; DOI=10.1534/g3.115.026450;
RA Neal S.J., Park J., DiTirro D., Yoon J., Shibuya M., Choi W.,
RA Schroeder F.C., Butcher R.A., Kim K., Sengupta P.;
RT "A Forward Genetic Screen for Molecules Involved in Pheromone-Induced Dauer
RT Formation in Caenorhabditis elegans.";
RL G3 (Bethesda) 6:1475-1487(2016).
CC -!- FUNCTION: Required for normal structure and function of sensory cilia
CC on amphid neurons, especially for the formation of distal ciliary
CC structures, but is less important for normal assembly of middle and
CC basal ciliary structures. Plays a role in the organization of axoneme
CC microtubule bundles in sensory cilia. Required for normal structure and
CC function of the ASER neuron that mediates attraction to NaCl. Required
CC for normal chemotaxis to NaCl (PubMed:18245347, PubMed:26378256).
CC Required for normal avoidance response to high osmolarity. In contrast,
CC is not required for normal chemotaxis to isoamyl alcohol. Does not play
CC a role in intraflagella transport (IFT) (PubMed:18245347). Promotes
CC dauer formation in response to pheromones such as the ascarosides
CC ascr#2, ascr#3, ascr#5, ascr#8 and icas#9 (PubMed:26976437).
CC {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256,
CC ECO:0000269|PubMed:26976437}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}. Perikaryon
CC {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}. Cell
CC projection, dendrite {ECO:0000269|PubMed:18245347,
CC ECO:0000269|PubMed:26378256}. Note=Detected in neuronal cell bodies,
CC and to a lesser extent in dendrites. Detected in ASER cilia
CC (PubMed:18245347, PubMed:26378256). Requires the intraflagella
CC transport (IFT) machinery for normal location in cilia, but does not
CC play a role in IFT itself (PubMed:18245347).
CC {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:B0024.8a};
CC IsoId=Q17423-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:B0024.8b};
CC IsoId=Q17423-2; Sequence=VSP_058558;
CC Name=c {ECO:0000312|WormBase:B0024.8c};
CC IsoId=Q17423-3; Sequence=VSP_058557;
CC Name=d {ECO:0000312|WormBase:B0024.8d};
CC IsoId=Q17423-4; Sequence=VSP_058556;
CC -!- TISSUE SPECIFICITY: Detected in a subset of amphid neurons that lack
CC wing- or finger-like ciliary extensions. Likewise, detected in phasmid
CC neurons. {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}.
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:0000250|UniProtKB:Q6A070}.
CC -!- DISRUPTION PHENOTYPE: Impaired structure and function of sensory cilia
CC on amphid neurons. Strongly reduced length of the sensory cilium on the
CC ASER neuron. Contrary to wild-type cilia that display the canonical
CC ring of nine doublet microtubule bundles surrounding central singlet
CC microtubules in the proximal and middle part, cilia from mutant
CC nematodes have poorly defined microtubule organization at the cilium
CC proximal end, and no visible microtubules at their distal ends.
CC {ECO:0000269|PubMed:26378256}.
CC -!- SIMILARITY: Belongs to the Crescerin family. {ECO:0000305}.
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DR EMBL; BX284605; CAA94880.3; -; Genomic_DNA.
DR EMBL; BX284605; CBZ01772.1; -; Genomic_DNA.
DR EMBL; BX284605; CBZ01773.1; -; Genomic_DNA.
DR EMBL; BX284605; CCU83323.1; -; Genomic_DNA.
DR RefSeq; NP_001256204.1; NM_001269275.1. [Q17423-1]
DR RefSeq; NP_001256205.1; NM_001269276.1. [Q17423-2]
DR RefSeq; NP_001256206.1; NM_001269277.1. [Q17423-2]
DR RefSeq; NP_001294732.1; NM_001307803.1. [Q17423-4]
DR AlphaFoldDB; Q17423; -.
DR SMR; Q17423; -.
DR STRING; 6239.B0024.8a; -.
DR EPD; Q17423; -.
DR PaxDb; Q17423; -.
DR EnsemblMetazoa; B0024.8a.1; B0024.8a.1; WBGene00000491. [Q17423-1]
DR EnsemblMetazoa; B0024.8b.1; B0024.8b.1; WBGene00000491. [Q17423-2]
DR EnsemblMetazoa; B0024.8c.1; B0024.8c.1; WBGene00000491. [Q17423-3]
DR EnsemblMetazoa; B0024.8d.1; B0024.8d.1; WBGene00000491. [Q17423-4]
DR GeneID; 179433; -.
DR KEGG; cel:CELE_B0024.8; -.
DR CTD; 179433; -.
DR WormBase; B0024.8a; CE42903; WBGene00000491; che-12. [Q17423-1]
DR WormBase; B0024.8b; CE45799; WBGene00000491; che-12. [Q17423-2]
DR WormBase; B0024.8c; CE45743; WBGene00000491; che-12. [Q17423-3]
DR WormBase; B0024.8d; CE48310; WBGene00000491; che-12. [Q17423-4]
DR eggNOG; KOG2933; Eukaryota.
DR GeneTree; ENSGT00940000167261; -.
DR HOGENOM; CLU_007936_0_0_1; -.
DR InParanoid; Q17423; -.
DR OMA; HSSDELC; -.
DR OrthoDB; 476837at2759; -.
DR PhylomeDB; Q17423; -.
DR PRO; PR:Q17423; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000491; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IMP:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IMP:WormBase.
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; IMP:UniProtKB.
DR GO; GO:0007600; P:sensory perception; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR034085; TOG.
DR Pfam; PF12348; CLASP_N; 1.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Chemotaxis;
KW Cilium biogenesis/degradation; Reference proteome; Repeat.
FT CHAIN 1..1282
FT /note="Crescerin-like protein che-12"
FT /id="PRO_0000437572"
FT REPEAT 59..96
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 100..137
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 162..209
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 261..300
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 308..345
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 349..386
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 388..421
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 424..461
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 838..875
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 879..917
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 919..953
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 961..998
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1095..1132
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1177..1214
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1219..1258
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REGION 33..240
FT /note="TOG 1"
FT /evidence="ECO:0000250|UniProtKB:Q6A070"
FT REGION 268..515
FT /note="TOG 2"
FT /evidence="ECO:0000250|UniProtKB:Q6A070"
FT REGION 566..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..1022
FT /note="TOG 3"
FT /evidence="ECO:0000250|UniProtKB:Q6A070"
FT REGION 1066..1282
FT /note="TOG 4"
FT /evidence="ECO:0000250|UniProtKB:Q6A070"
FT COMPBIAS 566..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..722
FT /note="MTSLFDALSRSNDRLPSPNFLPEDFLELLKSNDFDTKLTTLIRAATIAKREE
FT DWFHKFQKKGELFKCIDKIICDDRWELQHQCIKFLVEAMPTFGSATEYCMCFVMPNLIP
FT KLVSNKVTVRKITHQAIATFLRLKPEALQSFLKMLSNFMPNCNSKSELITELHHILIPE
FT LVKSNWTCLVENFTTESNIQGCEDQAGVLMKKLHYFIGNEFWQKIITNLSPEKREVLEQ
FT ITANVQVEHTESKAGSGVLRASAKPQSGGERRLRFGIVPSLVCALIAEDTDANQRISGL
FT EKMKQVVDQITPEEIARLVPHLHSYLLMLSNVLEDLNFKVVVLALDIVRATGHHLKGHM
FT EAHIQQFVNLVAKHFGNQKSVIKQIIMMTFMELFQNINPKTVGGCLRVFLENKNSRVRE
FT EVINIYTASLMTISPSKFNLQPLVNILVPMFHDVKKRVRLAAFEQLSVLAYLLNGKTEI
FT IMKPVRDFEQDQNSRGLTEAVTARIRRQVLPRIRYDGLIEYSTPPMMDSFDLAEAEMSL
FT PSNADLSWIVSNGGVEPDPFERTMSPISLAGNLATIRRNRVIQQQGQAEKPSFSLPQQP
FT AQQASHQAQRLPNGIEKSHETSENSSLDIGQRIVMTRMKSDDSFVRRQGSAASNPNSST
FT SSWEAPKRPPISPSEKSSISATKKEVNNNHIVKKGNLKSMRARSDTNLSEDHGEEEMEN
FT DPPRSFDDRPAKASGQYSFQD -> MYSQKMSAISSTHLPPIFAHKTQSWLKSDGREYL
FT WSSPN (in isoform d)"
FT /id="VSP_058556"
FT VAR_SEQ 1..681
FT /note="Missing (in isoform c)"
FT /id="VSP_058557"
FT VAR_SEQ 1..634
FT /note="MTSLFDALSRSNDRLPSPNFLPEDFLELLKSNDFDTKLTTLIRAATIAKREE
FT DWFHKFQKKGELFKCIDKIICDDRWELQHQCIKFLVEAMPTFGSATEYCMCFVMPNLIP
FT KLVSNKVTVRKITHQAIATFLRLKPEALQSFLKMLSNFMPNCNSKSELITELHHILIPE
FT LVKSNWTCLVENFTTESNIQGCEDQAGVLMKKLHYFIGNEFWQKIITNLSPEKREVLEQ
FT ITANVQVEHTESKAGSGVLRASAKPQSGGERRLRFGIVPSLVCALIAEDTDANQRISGL
FT EKMKQVVDQITPEEIARLVPHLHSYLLMLSNVLEDLNFKVVVLALDIVRATGHHLKGHM
FT EAHIQQFVNLVAKHFGNQKSVIKQIIMMTFMELFQNINPKTVGGCLRVFLENKNSRVRE
FT EVINIYTASLMTISPSKFNLQPLVNILVPMFHDVKKRVRLAAFEQLSVLAYLLNGKTEI
FT IMKPVRDFEQDQNSRGLTEAVTARIRRQVLPRIRYDGLIEYSTPPMMDSFDLAEAEMSL
FT PSNADLSWIVSNGGVEPDPFERTMSPISLAGNLATIRRNRVIQQQGQAEKPSFSLPQQP
FT AQQASHQAQRLPNGIEKSHETSENSSLDIGQRIVMTRMKSDDSFVRRQGSA -> MGTT
FT VSRAVSAPNRIYSSTVTPMPMSSNQNNMFMVVNRRMRP (in isoform b)"
FT /id="VSP_058558"
FT MUTAGEN 34
FT /note="F->E: Disrupts the predicted tubulin binding sites
FT and leads to strongly shortened sensory cilia on ASER
FT neurons; when associated with E-281; E-815 and E-1073."
FT /evidence="ECO:0000269|PubMed:26378256"
FT MUTAGEN 281
FT /note="A->E: Disrupts the predicted tubulin binding sites
FT and leads to strongly shortened sensory cilia on ASER
FT neurons; when associated with E-34; E-815 and E-1073."
FT /evidence="ECO:0000269|PubMed:26378256"
FT MUTAGEN 645..1282
FT /note="Missing: In oy106; shortens ASK and ASI cilia
FT length. Defects in pheromone-induced dauer formation in
FT response to the ascarosides ascr#2, ascr#3, ascr#5, ascr#8
FT and icas#9."
FT /evidence="ECO:0000269|PubMed:26976437"
FT MUTAGEN 815
FT /note="W->E: Disrupts the predicted tubulin binding sites
FT and leads to strongly shortened sensory cilia on ASER
FT neurons; when associated with E-34; E-281 and E-1073."
FT /evidence="ECO:0000269|PubMed:26378256"
FT MUTAGEN 1073
FT /note="W->E: Disrupts the predicted tubulin binding sites
FT and leads to strongly shortened sensory cilia on ASER
FT neurons; when associated with E-34; E-281 and E-815."
FT /evidence="ECO:0000269|PubMed:26378256"
SQ SEQUENCE 1282 AA; 142983 MW; C3EECA4F18FF06A8 CRC64;
MTSLFDALSR SNDRLPSPNF LPEDFLELLK SNDFDTKLTT LIRAATIAKR EEDWFHKFQK
KGELFKCIDK IICDDRWELQ HQCIKFLVEA MPTFGSATEY CMCFVMPNLI PKLVSNKVTV
RKITHQAIAT FLRLKPEALQ SFLKMLSNFM PNCNSKSELI TELHHILIPE LVKSNWTCLV
ENFTTESNIQ GCEDQAGVLM KKLHYFIGNE FWQKIITNLS PEKREVLEQI TANVQVEHTE
SKAGSGVLRA SAKPQSGGER RLRFGIVPSL VCALIAEDTD ANQRISGLEK MKQVVDQITP
EEIARLVPHL HSYLLMLSNV LEDLNFKVVV LALDIVRATG HHLKGHMEAH IQQFVNLVAK
HFGNQKSVIK QIIMMTFMEL FQNINPKTVG GCLRVFLENK NSRVREEVIN IYTASLMTIS
PSKFNLQPLV NILVPMFHDV KKRVRLAAFE QLSVLAYLLN GKTEIIMKPV RDFEQDQNSR
GLTEAVTARI RRQVLPRIRY DGLIEYSTPP MMDSFDLAEA EMSLPSNADL SWIVSNGGVE
PDPFERTMSP ISLAGNLATI RRNRVIQQQG QAEKPSFSLP QQPAQQASHQ AQRLPNGIEK
SHETSENSSL DIGQRIVMTR MKSDDSFVRR QGSAASNPNS STSSWEAPKR PPISPSEKSS
ISATKKEVNN NHIVKKGNLK SMRARSDTNL SEDHGEEEME NDPPRSFDDR PAKASGQYSF
QDFDAAIVPS SMGKKSISHH SLPITSHPPL KHAISQPQKR INNNGTFLRS GQGQRTKSVS
KPHRELTAVS KTYSLLDTSN MSVNQALKKM SSDEWADKVD GLNMISTLSE TQPRMVADNL
KEVIIAILNE CKNLRSSVSR VAIVTIGTVA QNLNSKIDSE MEKICAVLLS KSGDVSNAFI
RDDATDSLNK LVKAATAGKA LQGIILAGAK SKNNTIRSSC ANFVYDIITI QGSSAILNNQ
NALSNVLPVL LQFSRDQSPQ VRNPGKQSLC FLSKDPNFDR LMRKNALESE IKAVKDVLAN
VEKRGGVDSL ESTANLSGSL SRIGSTRRVQ KKLPDSLQLD LDEIRTELLA AGWERRLTGL
QRFEEMCGHA SKAVASDTRL IEAFISRLGD TNGKVASCAM ETYISTMGSM AKLYSTESNL
KAVMNQLAHA LTAHLSSKSE EHKHLARTCI QHTIRSIEPV SLLPAMTSAT KKSNVKQRPF
ILTQYCELSK LAYKSKPKQV EVMALPLLWD SVKNSAPDVD NKKATQYLAK TLAKLIGEKQ
LLDLATSELD PNRKKQLDAL IR
