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TFP11_CAEEL
ID   TFP11_CAEEL             Reviewed;         830 AA.
AC   Q17784; A1XDB6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Septin and tuftelin-interacting protein 1 homolog;
DE            Short=STIP-1;
GN   Name=stip-1; Synonyms=stip; ORFNames=C07E3.1;
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], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=Bristol N2; TISSUE=Embryo;
RX   PubMed=17289020; DOI=10.1016/j.yexcr.2007.01.003;
RA   Ji Q., Huang C.-H., Peng J., Hashmi S., Ye T., Chen Y.;
RT   "Characterization of STIP, a multi-domain nuclear protein, highly conserved
RT   in metazoans, and essential for embryogenesis in Caenorhabditis elegans.";
RL   Exp. Cell Res. 313:1460-1472(2007).
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).
CC   -!- FUNCTION: May be involved in pre-mRNA splicing (By similarity).
CC       Required for embryonic development and survival. {ECO:0000250,
CC       ECO:0000269|PubMed:17289020}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex (By similarity). Can
CC       assemble into large rod-like polymers. {ECO:0000250,
CC       ECO:0000269|PubMed:17289020}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289020}.
CC   -!- TISSUE SPECIFICITY: Detected in muscle cells from body, pharynx and
CC       vulva, in neurons from head and tail, in pharyngeal gland and in tail
CC       hypodermal cells. {ECO:0000269|PubMed:17289020}.
CC   -!- DEVELOPMENTAL STAGE: Detected in oocyte, embryo, larval stage 1 to 4,
CC       and in adult. {ECO:0000269|PubMed:17289020}.
CC   -!- SIMILARITY: Belongs to the TFP11/STIP family. {ECO:0000305}.
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DR   EMBL; DQ342049; ABC69941.1; -; mRNA.
DR   EMBL; Z49908; CAA90093.2; -; Genomic_DNA.
DR   RefSeq; NP_496226.2; NM_063825.4.
DR   AlphaFoldDB; Q17784; -.
DR   SMR; Q17784; -.
DR   BioGRID; 39919; 3.
DR   DIP; DIP-25481N; -.
DR   IntAct; Q17784; 2.
DR   STRING; 6239.C07E3.1a; -.
DR   EPD; Q17784; -.
DR   PaxDb; Q17784; -.
DR   PeptideAtlas; Q17784; -.
DR   EnsemblMetazoa; C07E3.1a.1; C07E3.1a.1; WBGene00007412.
DR   GeneID; 174600; -.
DR   KEGG; cel:CELE_C07E3.1; -.
DR   UCSC; C07E3.1a; c. elegans.
DR   CTD; 174600; -.
DR   WormBase; C07E3.1a; CE41502; WBGene00007412; stip-1.
DR   eggNOG; KOG2184; Eukaryota.
DR   HOGENOM; CLU_007977_1_1_1; -.
DR   InParanoid; Q17784; -.
DR   OMA; EFFPKWH; -.
DR   OrthoDB; 1238995at2759; -.
DR   PhylomeDB; Q17784; -.
DR   PRO; PR:Q17784; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00007412; Expressed in embryo and 4 other tissues.
DR   ExpressionAtlas; Q17784; baseline and differential.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR022783; GCFC_dom.
DR   InterPro; IPR024933; STIP.
DR   InterPro; IPR022159; STIP/TFIP11_N.
DR   InterPro; IPR045211; TFP11/STIP/Ntr1.
DR   PANTHER; PTHR23329; PTHR23329; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF07842; GCFC; 1.
DR   Pfam; PF12457; TIP_N; 1.
DR   PIRSF; PIRSF017706; TFIP11; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   1: Evidence at protein level;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Spliceosome.
FT   CHAIN           1..830
FT                   /note="Septin and tuftelin-interacting protein 1 homolog"
FT                   /id="PRO_0000342283"
FT   DOMAIN          153..199
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   830 AA;  94313 MW;  C374A3301F6FF380 CRC64;
     MEDDDGRESF EINDMDLEYA MNPGGRRRFQ NKDQATYGVF APDSDDDDDE QGTSRGPYKK
     RSKISAPMSF VSGGIQQGNK IDKDDPASLN LNLGGEKKPK EDDEGSIQID FDKRTKKAPK
     QNGAQVFAGM RSSANHGAAD INQFGSWMRG DGNSNKIMKM MQAMGYKPGE GLGAQGQGIV
     EPVQAQLRKG RGAVGAYGKE STATGPKFGE SAADAQKRMA QEGTSSRPTN DDQEKSGLKI
     KGSWKKSQTV KTKYRTIEDV MEEGMSASRP ASHQQSQQYS NIKVIDMTGK QQKIYSGYDS
     FSMKTRSEYD TVDDEERTVF DVPELIHNLN LLVDLTEEGI RRSNQQLISL KDQTTALEYD
     LQQVQKSLGT EEQEAQHIKD VYELIDGFSS NRSPSMEECQ ELFRRLRSEF PHEYELYSLE
     TVAIPTVLPL IQKYFVAWKP LEDKNYGCEL ISTWRDILDD SKNGRKMTFG HNKTKGDEIR
     AYDRIIWEGI LPSIRRACLQ WDPSTQMHEM IELVEQWIPL LSAWITENIL EQLVVPKIAE
     RVNQWDPMTD EIPIHEWLVP WLVLLGDRIQ TVMPPIRQKL SKALKLWDPM DRSALETLRP
     WQNVWSAATF SAFIAQNIVP KLGVALDTME LNPTMNPEYP EWTACMEWLE FTHPDAIANI
     VTKYFFPRFY NCLCLWLDSP GVDYNEVKRW YGSWKARIPQ VLVNYPTVNE NLRRSMIAIG
     RSLQGEKVGG LQATPIAPMA PPPPMAPHFT QAAPVQKLSL KEIIEYTAGK NGFTYHPQKD
     RYKDGRQVFW FGALSIYLDS EMVYVMDPIE FVWRPSGLNE LIQMAQGAQG
 
 
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