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OSM1_CAEEL
ID   OSM1_CAEEL              Reviewed;        1737 AA.
AC   Q22830; Q1KYP6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 4.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Intraflagellar transport protein osm-1;
DE   AltName: Full=Osmotic avoidance abnormal protein 1;
GN   Name=osm-1 {ECO:0000312|WormBase:T27B1.1};
GN   ORFNames=T27B1.1 {ECO:0000312|WormBase:T27B1.1};
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 [MRNA].
RX   PubMed=16648645; DOI=10.1534/genetics.106.056721;
RA   Bell L.R., Stone S., Yochem J., Shaw J.E., Herman R.K.;
RT   "The molecular identities of the Caenorhabditis elegans intraflagellar
RT   transport genes dyf-6, daf-10 and osm-1.";
RL   Genetics 173:1275-1286(2006).
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   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10545497; DOI=10.1083/jcb.147.3.519;
RA   Signor D., Wedaman K.P., Orozco J.T., Dwyer N.D., Bargmann C.I., Rose L.S.,
RA   Scholey J.M.;
RT   "Role of a class DHC1b dynein in retrograde transport of IFT motors and IFT
RT   raft particles along cilia, but not dendrites, in chemosensory neurons of
RT   living Caenorhabditis elegans.";
RL   J. Cell Biol. 147:519-530(1999).
RN   [4]
RP   FUNCTION, IDENTIFICATION IN IFT COMPLEX B, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
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: Component of the intraflagellar transport (IFT) complex B
CC       required for transport of proteins in the motile cilium
CC       (PubMed:28479320). May be required for ciliary entrance and transport
CC       of specific ciliary cargo proteins such as che-3 which are related to
CC       motility (PubMed:28479320). Required for the maintenance and formation
CC       of chemosensory cilia that detect chemosensory cues (PubMed:10545497).
CC       {ECO:0000269|PubMed:10545497, ECO:0000269|PubMed:28479320}.
CC   -!- SUBUNIT: Component of the IFT complex B composed of at least che-2,
CC       che-13, dyf-1, dyf-3, dyf-6, dyf-11, dyf-13, ift-20, ift-74, ift-81,
CC       ifta-2, osm-1, osm-5 and osm-6. {ECO:0000269|PubMed:28479320}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000269|PubMed:10545497}. Note=Emerges from the transition zones
CC       and move in a bidirectional fashion along the sensory cilia, displaying
CC       anterograde movement from the transition zone toward the tip of the
CC       ciliary axoneme and retrograde movement from the cilium tip back toward
CC       the transition zone.
CC   -!- TISSUE SPECIFICITY: Expressed in amphid and phasmid chemosensory
CC       neurons, where it appears to concentrate at the base of the transition
CC       zones, which correspond to the basal bodies of motile and sensory
CC       cilia. Moves in the retrograde direction along cilia and dendrites,
CC       suggesting that it is retrieved from the distal endings of the cilia by
CC       a retrograde transport pathway that moves it along cilia and then
CC       dendrites, back to the neuronal cell body.
CC       {ECO:0000269|PubMed:10545497}.
CC   -!- DISRUPTION PHENOTYPE: Worms display defects in ciliary structure
CC       resulting in defects in ability and osmotic avoidance behavior.
CC       {ECO:0000269|PubMed:10545497}.
CC   -!- SIMILARITY: Belongs to the IFT172 family. {ECO:0000305}.
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DR   EMBL; DQ360811; ABC88648.1; -; mRNA.
DR   EMBL; FO081607; CCD72791.1; -; Genomic_DNA.
DR   RefSeq; NP_510681.4; NM_078280.6.
DR   AlphaFoldDB; Q22830; -.
DR   BioGRID; 46599; 8.
DR   ComplexPortal; CPX-1290; Intraflagellar transport complex B.
DR   STRING; 6239.T27B1.1; -.
DR   EPD; Q22830; -.
DR   PaxDb; Q22830; -.
DR   PeptideAtlas; Q22830; -.
DR   PRIDE; Q22830; -.
DR   EnsemblMetazoa; T27B1.1.1; T27B1.1.1; WBGene00003883.
DR   GeneID; 181715; -.
DR   KEGG; cel:CELE_T27B1.1; -.
DR   UCSC; T27B1.1; c. elegans.
DR   CTD; 181715; -.
DR   WormBase; T27B1.1; CE41845; WBGene00003883; osm-1.
DR   eggNOG; KOG3616; Eukaryota.
DR   GeneTree; ENSGT00940000153417; -.
DR   HOGENOM; CLU_002716_0_0_1; -.
DR   InParanoid; Q22830; -.
DR   OMA; YQQLGMW; -.
DR   OrthoDB; 30851at2759; -.
DR   PhylomeDB; Q22830; -.
DR   Reactome; R-CEL-5620924; Intraflagellar transport.
DR   PRO; PR:Q22830; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00003883; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR   GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR   GO; GO:0035869; C:ciliary transition zone; IDA:WormBase.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0030992; C:intraciliary transport particle B; IDA:WormBase.
DR   GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR   GO; GO:0060271; P:cilium assembly; IGI:UniProtKB.
DR   GO; GO:0043053; P:dauer entry; IGI:UniProtKB.
DR   GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR   GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Developmental protein; Reference proteome; Repeat;
KW   TPR repeat; WD repeat.
FT   CHAIN           1..1737
FT                   /note="Intraflagellar transport protein osm-1"
FT                   /id="PRO_0000328945"
FT   REPEAT          14..53
FT                   /note="WD 1"
FT   REPEAT          63..103
FT                   /note="WD 2"
FT   REPEAT          110..150
FT                   /note="WD 3"
FT   REPEAT          151..189
FT                   /note="WD 4"
FT   REPEAT          191..229
FT                   /note="WD 5"
FT   REPEAT          233..273
FT                   /note="WD 6"
FT   REPEAT          511..553
FT                   /note="WD 7"
FT   REPEAT          700..737
FT                   /note="TPR 1"
FT   REPEAT          803..836
FT                   /note="TPR 2"
FT   REPEAT          848..881
FT                   /note="TPR 3"
FT   REPEAT          907..940
FT                   /note="TPR 4"
FT   REPEAT          979..1012
FT                   /note="TPR 5"
FT   REPEAT          1037..1070
FT                   /note="TPR 6"
FT   REPEAT          1137..1170
FT                   /note="TPR 7"
SQ   SEQUENCE   1737 AA;  195702 MW;  EE96E0B3D871ADAA CRC64;
     MKLKYLSTIL PAQDGEAKIS NISCSPNGSR AAIACSDRSV ALLDENGVQK DRFTCKPIDA
     KYGKKSFTVL CMTFSPDSSR IAIGQSDNVL FIYKVGTSWN EKKVIVNKFV QPSAVTCLSW
     PFDDKILVGQ LDGKVRIGLI KTNKCSSLYK TDETVVSIQT HPKRTSFVSA HQDGSIILYN
     FSSRTQSKIC TLQVPPYNLV FTNHGLVVAT SDRRVLSYTE NGVVQQQFDY NDQSEKEFSS
     ISCDPTAQNV VVASYDRLRL FSWSARRGAW DEGAPLEIQN AYTIGALGWK MDGSTIYAGT
     VCGGVFSVDC CLRRGMLKSR FETTYVAPSH VILRDVTNDT RTNVISNKGL AIDELKIMGK
     DRYVIGYTSS SIIIADTESQ RFSELEWQSG GHEKFYFDFN NCCLIINAGE VTVVEYGVDG
     SLGWVRTELT SPHLLSVQVS GPDVEEHKKV KKLAYLVDPT TISIINLING QQESFINHTG
     AVDWIELNER ASKLLYRDKR SKVTLVDISS DQRSVLLSFC TYVQWVPMSD VIVAQSGDNL
     SIWYNPDLPE QVTNMKIKGE VEAVLRDADR TEVIVQEPTA KVAYELDNTQ IEFGAALEKR
     DFDRAVAFLE SNTSGTDAYS MWIRVAEMAL EHGNLFVAQR CYAAINDVAK VRKLHDILEI
     ADEASISIGG DGTHFYKVRA MLAIMGRKFK EAERIFLEQN DTESAIGMYT SLHKWDEALE
     LAKVLNYPEY EQLKTSYLRA LSDTGQDSKA AELKVSDGDT LSAIQLYIKS NKPLSALSAA
     NNDSVLSQDE NILRQIADSL VKSQLYDKAG DVYEKLKDFD KAVEYFKKGD AYGKAIQLAR
     FAFPEKVVTL EQEWGLHLEY IGQYDAAVNH FVEANDLKKA VEAAIRAKEW PKALSIVENI
     QDQKVRTGYY GEIADHYSNK GDFERAERLF VEAGLFNDAI MMYGKNNKWI DAFRLSEEFH
     GREATISSYL AKAEDLDEHG RFAEAEQLYI TIGMPHKAIQ MYDRVGRDDD VLRLVERYHG
     EHMHETRKRF ATQYEERGDL KAAEEQFLKA GDFRSAVNMY KDSEMWSDAY RIAKTEGGEN
     MEKQVLFMWA KSIGGDAAVK LLNKHGMLME GIDFACETGA FDLAFDLARI GAKDRMGTVH
     VRLATQLEEE GRLEDASKHY VEGNKPELAV EMFIRDNDWA DAERVAKDHC ESLLPDVYTG
     QARRAIEEGD HLRAETFLLR ANKPDIILRY FIENEMWPDA LRIAQNYLPH QAALIQEEYE
     KSELRNGARG VDSFVAQAKE WEQQGDWRKA VSALLKINRD STDNDALIKH STEKAADLVM
     KFLMGDEEYI GAALGALDEA NCNEKAAELL LLFGQSRQAI NALCRAKQWA KAKQVAQEYL
     PEMVPEIEKI YKESLKSEGR LGELIDVDVI TAIDMMIEND QWDKALDTAK SQNYRPLLDK
     YVAQYAAILV HRNDLSRVLA VLERYGASAN PANFSIYKLL MEETLAKPRF DYTEIARVRN
     VHLDVYNALQ KESSEHFEEF SRALWALHLI AMRTALEEIG DSVPEVQKLC LKQSLSLLRY
     TDILVADRIF YEAGAAAKDY GSEYESLGFL LLNHYLDLVD AIEEGNGELV DYSPFENSDI
     PTEVSLPTRQ WLESAKHEEM KEWVLASSVD DAHAKELVYD KRGVFEASLK DKRGTAEPCL
     VTGYPVIEST VRIGSMVAEK DNLNKFLVVI KSNQTENLLN VQNFVAKWAG SPLAISL
 
 
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