OSM3_CAEEL
ID OSM3_CAEEL Reviewed; 699 AA.
AC P46873; Q8MPT7; Q8MPT8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Osmotic avoidance abnormal protein 3;
DE AltName: Full=Kinesin-like protein osm-3;
GN Name=osm-3 {ECO:0000312|WormBase:M02B7.3b};
GN ORFNames=M02B7.3 {ECO:0000312|WormBase:M02B7.3b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=7714894; DOI=10.1006/jmbi.1994.0146;
RA Tabish M., Siddiqui Z.K., Nishikawa K., Siddiqui S.S.;
RT "Exclusive expression of C. elegans osm-3 kinesin gene in chemosensory
RT neurons open to the external environment.";
RL J. Mol. Biol. 247:377-389(1995).
RN [2]
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 [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-397, FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=7690265; DOI=10.1097/00001756-199307000-00013;
RA Shakir M.A., Fukushige T., Yasuda H., Miwa J., Siddiqui S.S.;
RT "C. elegans osm-3 gene mediating osmotic avoidance behaviour encodes a
RT kinesin-like protein.";
RL NeuroReport 4:891-894(1993).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF GLY-444.
RX PubMed=17000880; DOI=10.1083/jcb.200606003;
RA Pan X., Ou G., Civelekoglu-Scholey G., Blacque O.E., Endres N.F., Tao L.,
RA Mogilner A., Leroux M.R., Vale R.D., Scholey J.M.;
RT "Mechanism of transport of IFT particles in C. elegans cilia by the
RT concerted action of kinesin-II and OSM-3 motors.";
RL J. Cell Biol. 174:1035-1045(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17420466; DOI=10.1073/pnas.0606974104;
RA Burghoorn J., Dekkers M.P., Rademakers S., de Jong T., Willemsen R.,
RA Jansen G.;
RT "Mutation of the MAP kinase DYF-5 affects docking and undocking of kinesin-
RT 2 motors and reduces their speed in the cilia of Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7157-7162(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=27623382; DOI=10.1016/j.devcel.2016.07.013;
RA Nechipurenko I.V., Olivier-Mason A., Kazatskaya A., Kennedy J.,
RA McLachlan I.G., Heiman M.G., Blacque O.E., Sengupta P.;
RT "A Conserved role for girdin in basal body positioning and ciliogenesis.";
RL Dev. Cell 38:493-506(2016).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=28479320; DOI=10.1016/j.cub.2017.04.015;
RA Yi P., Li W.J., Dong M.Q., Ou G.;
RT "Dynein-driven retrograde intraflagellar transport is triphasic in C.
RT elegans sensory cilia.";
RL Curr. Biol. 27:1448-1461(2017).
CC -!- FUNCTION: Kinesin motor protein which is required for the anterograde
CC intraflagellar transport (IFT) along the middle segment of the sensory
CC neuron cilia together with the kinesin II motor complex (composed of
CC klp-11, klp-20 and kap-1) and on its own, is required for IFT along the
CC distal segment (PubMed:17000880, PubMed:17420466). In addition,
CC regulates the length of cilia (PubMed:17420466). May have a role during
CC neurogenesis and axonal transport (PubMed:7714894, PubMed:7690265).
CC {ECO:0000269|PubMed:17000880, ECO:0000269|PubMed:17420466,
CC ECO:0000269|PubMed:7690265, ECO:0000269|PubMed:7714894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, cilium {ECO:0000269|PubMed:17420466,
CC ECO:0000269|PubMed:28479320}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:27623382}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:27623382}. Note=Localizes along the full
CC cilium length. {ECO:0000269|PubMed:17420466,
CC ECO:0000269|PubMed:27623382}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P46873-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P46873-2; Sequence=VSP_012172;
CC -!- TISSUE SPECIFICITY: Expressed in an exclusive set of 26 chemosensory
CC neurons whose dendritic endings are exposed to the external
CC environment; six IL2 neurons of the inner labial sensilla, 8 pairs of
CC amphid neurons in the head, and 2 pairs of phasmid neurons in the tail.
CC {ECO:0000269|PubMed:17420466, ECO:0000269|PubMed:7690265,
CC ECO:0000269|PubMed:7714894}.
CC -!- DISRUPTION PHENOTYPE: Worms are defective in osmotic avoidance,
CC chemotaxis and dauer formation. {ECO:0000269|PubMed:7690265,
CC ECO:0000269|PubMed:7714894}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin II subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA07612.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA20996.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA20996.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D38632; BAA07612.1; ALT_SEQ; Genomic_DNA.
DR EMBL; FO081251; CCD70203.1; -; Genomic_DNA.
DR EMBL; FO081251; CCD70204.1; -; Genomic_DNA.
DR EMBL; D14968; BAA20996.1; ALT_SEQ; Genomic_DNA.
DR PIR; S54351; S54351.
DR RefSeq; NP_001023308.1; NM_001028137.3.
DR RefSeq; NP_741362.1; NM_171308.4.
DR PDB; 7A3Z; X-ray; 2.10 A; A=2-362.
DR PDB; 7A40; X-ray; 2.30 A; A/B=2-337.
DR PDB; 7A5E; X-ray; 1.90 A; A/B=2-337.
DR PDBsum; 7A3Z; -.
DR PDBsum; 7A40; -.
DR PDBsum; 7A5E; -.
DR AlphaFoldDB; P46873; -.
DR SMR; P46873; -.
DR BioGRID; 42280; 7.
DR DIP; DIP-26512N; -.
DR STRING; 6239.M02B7.3b; -.
DR PaxDb; P46873; -.
DR EnsemblMetazoa; M02B7.3a.1; M02B7.3a.1; WBGene00003884. [P46873-2]
DR EnsemblMetazoa; M02B7.3a.2; M02B7.3a.2; WBGene00003884. [P46873-2]
DR EnsemblMetazoa; M02B7.3a.3; M02B7.3a.3; WBGene00003884. [P46873-2]
DR EnsemblMetazoa; M02B7.3b.1; M02B7.3b.1; WBGene00003884. [P46873-1]
DR UCSC; M02B7.3b; c. elegans. [P46873-1]
DR WormBase; M02B7.3a; CE31567; WBGene00003884; osm-3. [P46873-2]
DR WormBase; M02B7.3b; CE31568; WBGene00003884; osm-3. [P46873-1]
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000158776; -.
DR HOGENOM; CLU_001485_22_5_1; -.
DR InParanoid; P46873; -.
DR OMA; KKEAVWD; -.
DR OrthoDB; 862274at2759; -.
DR PhylomeDB; P46873; -.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:P46873; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003884; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; IDA:WormBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IDA:WormBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:WormBase.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IGI:UniProtKB.
DR GO; GO:0043053; P:dauer entry; IGI:UniProtKB.
DR GO; GO:0035720; P:intraciliary anterograde transport; IDA:WormBase.
DR GO; GO:0042073; P:intraciliary transport; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IGI:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IGI:WormBase.
DR GO; GO:0061066; P:positive regulation of dauer larval development; IMP:UniProtKB.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IGI:WormBase.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..699
FT /note="Osmotic avoidance abnormal protein 3"
FT /id="PRO_0000125402"
FT DOMAIN 4..327
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 339..523
FT /evidence="ECO:0000255"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT SITE 444
FT /note="Required for autoinhibition"
FT /evidence="ECO:0000269|PubMed:17000880"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_012172"
FT MUTAGEN 444
FT /note="G->E: Loss of autoinhibition."
FT /evidence="ECO:0000269|PubMed:17000880"
FT CONFLICT 57..59
FT /note="DST -> IRP (in Ref. 1; BAA07612 and 3; BAA20996)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="M -> I (in Ref. 1; BAA07612 and 3; BAA20996)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="L -> S (in Ref. 1; BAA07612)"
FT /evidence="ECO:0000305"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7A3Z"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 125..139
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:7A5E"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:7A40"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 206..218
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 246..270
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:7A5E"
FT TURN 288..293
FT /evidence="ECO:0007829|PDB:7A5E"
FT STRAND 294..304
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:7A5E"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:7A5E"
SQ SEQUENCE 699 AA; 78779 MW; 8A774E3EF3A07813 CRC64;
MAESVRVAVR CRPFNQREKD LNTTLCVGMT PNVGQVNLNA PDGAAKDFTF DGAYFMDSTG
EQIYNDIVFP LVENVIEGYN GTVFAYGQTG SGKTFSMQGI ETIPAQRGVI PRAFDHIFTA
TATTENVKFL VHCSYLEIYN EEVRDLLGAD NKQKLEIKEQ PDRGVYVAGL SMHVCHDVPA
CKELMTRGFN NRHVGATLMN KDSSRSHSIF TVYVEGMTET GSIRMGKLNL VDLAGSERQS
KTGATGDRLK EATKINLSLS ALGNVISALV DGKSKHIPYR DSKLTRLLQD SLGGNTKTIM
IACVSPSSDN YDETLSTLRY ANRAKNIKNK PTINEDPKDA LLREYQEEIA RLKSMVQPGA
VGVGAPAQDA FSIEEERKKL REEFEEAMND LRGEYEREQT SKAELQKDLE SLRADYERAN
ANLDNLNPEE AAKKIQQLQD QFIGGEEAGN TQLKQKRMKQ LKEAETKTQK LAAALNVHKD
DPLLQVYSTT QEKLDAVTSQ LEKEVKKSKG YEREIEDLHG EFELDRLDYL DTIRKQDQQL
KLLMQIMDKI QPIIKKDTNY SNVDRIKKEA VWNEDESRWI LPEMSMSRTI LPLANNGYMQ
EPARQENTLL RSNFDDKLRE RLAKSDSENL ANSYFKPVKQ INVINKYKSD QKLSTSKSLF
PSKTPTFDGL VNGVVYTDAL YERAQSAKRP PRLASLNPK
