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CTR9_CAEEL
ID   CTR9_CAEEL              Reviewed;        1150 AA.
AC   Q03560; C0P268; C0P269; C0P270;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=RNA polymerase-associated protein CTR9 {ECO:0000250|UniProtKB:P89105};
GN   Name=ctr-9 {ECO:0000312|WormBase:B0464.2a};
GN   Synonyms=tpr-3 {ECO:0000312|WormBase:B0464.2a};
GN   ORFNames=B0464.2 {ECO:0000312|WormBase:B0464.2a};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
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, AND DISRUPTION PHENOTYPE.
RX   PubMed=24721716; DOI=10.1016/j.ydbio.2014.04.002;
RA   Kubota Y., Tsuyama K., Takabayashi Y., Haruta N., Maruyama R., Iida N.,
RA   Sugimoto A.;
RT   "The PAF1 complex is involved in embryonic epidermal morphogenesis in
RT   Caenorhabditis elegans.";
RL   Dev. Biol. 391:43-53(2014).
CC   -!- FUNCTION: Component of the PAF1 complex which is a multifunctional
CC       complex involved in transcription initiation via genetic interactions
CC       with TATA-binding proteins, elongation and transcription-coupled
CC       histone modification (By similarity). Ctr-9 is required for epidermal
CC       microtubule organization during morphogenesis (PubMed:24721716).
CC       {ECO:0000250|UniProtKB:P89105, ECO:0000269|PubMed:24721716}.
CC   -!- SUBUNIT: Component of the PAF1 complex which consists of at least cdc-
CC       73, ctr-9, leo-1, pafo-1 and rtfo-1. {ECO:0000250|UniProtKB:P89105}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24721716}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:B0464.2a};
CC         IsoId=Q03560-1; Sequence=Displayed;
CC       Name=d {ECO:0000312|WormBase:B0464.2d};
CC         IsoId=Q03560-4; Sequence=VSP_057316, VSP_057317;
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down is mostly embryonic
CC       lethal. Embryogenesis proceeds more slowly, with embryos displaying
CC       defects in the positioning and shape of epidermal cells. Randomly
CC       orientated microtubules are present in epidermal cells during the
CC       epidermal elongation process. F-actin accumulation is visible at the
CC       leading edge during ventral closure and circumferential actin bundles
CC       are present in epidermal cells. Decreased expression of pafo-1,
CC       increased cytoplasmic expression of leo-1 and increased nuclear
CC       expression of rtfo-1. {ECO:0000269|PubMed:24721716,
CC       ECO:0000303|PubMed:24721716}.
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DR   EMBL; BX284603; CAA79544.1; -; Genomic_DNA.
DR   EMBL; BX284603; CAX51623.1; -; Genomic_DNA.
DR   PIR; D88556; D88556.
DR   PIR; S28279; S28279.
DR   RefSeq; NP_001255000.1; NM_001268071.1. [Q03560-1]
DR   RefSeq; NP_001255001.1; NM_001268072.1. [Q03560-4]
DR   AlphaFoldDB; Q03560; -.
DR   SMR; Q03560; -.
DR   BioGRID; 41532; 3.
DR   ComplexPortal; CPX-966; PAF1 complex.
DR   STRING; 6239.B0464.2c; -.
DR   iPTMnet; Q03560; -.
DR   EPD; Q03560; -.
DR   PaxDb; Q03560; -.
DR   PeptideAtlas; Q03560; -.
DR   PRIDE; Q03560; -.
DR   EnsemblMetazoa; B0464.2a.1; B0464.2a.1; WBGene00007184. [Q03560-1]
DR   EnsemblMetazoa; B0464.2a.2; B0464.2a.2; WBGene00007184. [Q03560-1]
DR   EnsemblMetazoa; B0464.2d.1; B0464.2d.1; WBGene00007184. [Q03560-4]
DR   EnsemblMetazoa; B0464.2d.2; B0464.2d.2; WBGene00007184. [Q03560-4]
DR   GeneID; 176335; -.
DR   KEGG; cel:CELE_B0464.2; -.
DR   UCSC; B0464.2; c. elegans. [Q03560-1]
DR   CTD; 176335; -.
DR   WormBase; B0464.2a; CE20456; WBGene00007184; ctr-9. [Q03560-1]
DR   WormBase; B0464.2d; CE43518; WBGene00007184; ctr-9. [Q03560-4]
DR   eggNOG; KOG2002; Eukaryota.
DR   GeneTree; ENSGT00390000005097; -.
DR   HOGENOM; CLU_006386_0_0_1; -.
DR   InParanoid; Q03560; -.
DR   OMA; MSNCIEI; -.
DR   OrthoDB; 396755at2759; -.
DR   PhylomeDB; Q03560; -.
DR   Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR   PRO; PR:Q03560; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00007184; Expressed in embryo and 4 other tissues.
DR   GO; GO:0016593; C:Cdc73/Paf1 complex; IBA:GO_Central.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR   GO; GO:0016571; P:histone methylation; IC:ComplexPortal.
DR   GO; GO:0051569; P:regulation of histone H3-K4 methylation; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR031101; Ctr9.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR14027; PTHR14027; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00028; TPR; 10.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   PROSITE; PS50005; TPR; 9.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Coiled coil; Nucleus; Reference proteome; Repeat;
KW   TPR repeat.
FT   CHAIN           1..1150
FT                   /note="RNA polymerase-associated protein CTR9"
FT                   /id="PRO_0000106421"
FT   REPEAT          143..176
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          177..210
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          212..245
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          247..282
FT                   /note="TPR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          320..353
FT                   /note="TPR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          355..388
FT                   /note="TPR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          432..464
FT                   /note="TPR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          471..504
FT                   /note="TPR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          594..627
FT                   /note="TPR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          643..677
FT                   /note="TPR 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          679..711
FT                   /note="TPR 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          712..745
FT                   /note="TPR 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          748..781
FT                   /note="TPR 13"
FT                   /evidence="ECO:0000255"
FT   REGION          935..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          848..916
FT                   /evidence="ECO:0000255"
FT   COILED          972..1028
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        935..952
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1028
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1095
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         25..206
FT                   /note="EVIEINCSELPDGEEVLQILEAEEAKLSYWIEVALEYYRQDRVDLFMMILES
FT                   AGSRAGLEYEGVKQDQMRALDILAAYWMTQGYREKAKDKKSDFFSKATVLFNTADKIAM
FT                   YEWSHLTVRAWFYLFERDKSTNKYELADQQFNYVVKTNPKNVLPLIGKAVIAFNKKDYK
FT                   TAIYYFRKAIRQ -> GTHLKRLRRFSIEVWNLMQNWATASEKSVQYLESLVNSRLKLL
FT                   YSREVDVEESAKLTKDQSDRVLNEIVVMNSKLNQTMSDFEKVIGKFEVAQGRMSAWKQL
FT                   TEKSQNIEEKYIVETLDENLPLIITMLKKELKVKQDVLFDFAQNDSRDVFTLVLLTFKH
FT                   EPFVDVALLSKLFALVASEAQ (in isoform d)"
FT                   /id="VSP_057316"
FT   VAR_SEQ         207..1150
FT                   /note="Missing (in isoform d)"
FT                   /id="VSP_057317"
SQ   SEQUENCE   1150 AA;  132345 MW;  1A7054727FBC96B7 CRC64;
     MDESIDDVQE TRTIAIPLKD SHEDEVIEIN CSELPDGEEV LQILEAEEAK LSYWIEVALE
     YYRQDRVDLF MMILESAGSR AGLEYEGVKQ DQMRALDILA AYWMTQGYRE KAKDKKSDFF
     SKATVLFNTA DKIAMYEWSH LTVRAWFYLF ERDKSTNKYE LADQQFNYVV KTNPKNVLPL
     IGKAVIAFNK KDYKTAIYYF RKAIRQCRHT IADLRVGIGH CFAKMGMMDK AKTAFERAME
     IEPYNVSAMC GLGIILLNTY DHDSLKHAVS LFGRSYNLQT DHPVALIHLA NHFFFKKEIE
     RAWTLAWHAA TYNDCDSIKA EAFYQMGRCR HAQGQFDGAY KYYYQARQAN NGEHTLAHYG
     LGQMYIHRNE IEEAIKCFDT VHKRLPNNTD TMKILGSLYA HVQLNDPAQT AEARQKGRDV
     LGKYLAVEND DYEACIDLAQ LLEATDPKRS LELYENAIDL LVTNESIQPQ PEMLNNVGAL
     YMSMKQYEKA EHHFKRAKER LEEQLNTDEG SLLLERRSAP EKSHLLTIRY NLALCLEHLC
     RTVEAEQMYK DIVKECPGYI DGYLRLGCIT RDRHQVYESS LWLKQGVQFD QASPIVWTLI
     GNLHFAKNEW MPAQKKFEFI LSKIFNNKIP DPYSLVALGN VWFEQLLNPS RKKEDEKKYI
     DRALQMYQKA LKLQPKNMYA ANGIGCVLAY KRNWNDARDV FSQVRESTSE FYDVWLNIAH
     VCMEREQWMA AVQMYSSAMK KFRKENDSTL QHYLAKAYYR ANMLNEAKEA LECAMLDQLD
     NTQLKFNYAI VLKKSAKEVL RGHKMTSEQV TAAIDDLKFA DKIFQYISKN DDRQSSHTGM
     RISRTICAEE AKNCKDLLTQ AKHKLAAAQT QDEEERRLME KQEKEKIALQ NKMIEEARAK
     EEAEKQKLED MKNLRLSFIE MTKDVLRLPE IVEEKRRGGG GRKRRNDDGD EFVNDSSDAG
     NYDGEEGGED GERRERRKKD KAAKKASRKK RERRDSGGPD SNRRDEKKRK RKEERDRKLQ
     EKLSAKQSAK IKSRAFLSSS ESSDDDKPKP AADSSDDEVD PRPPVDEFDS PTRTDSDSDR
     ETTTKKKKKK AVVDSDEGSV SGSGSGSDND DKPIIGGSDD DDDDKPAGGN SRDSDGSDAP
     KKKVIESDSD
 
 
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