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MIPT3_DANRE
ID   MIPT3_DANRE             Reviewed;         629 AA.
AC   Q6PGZ3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=TRAF3-interacting protein 1;
GN   Name=traf3ip1; ORFNames=zgc:63522;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=26487268; DOI=10.1038/ncomms9666;
RA   Bizet A.A., Becker-Heck A., Ryan R., Weber K., Filhol E., Krug P.,
RA   Halbritter J., Delous M., Lasbennes M.C., Linghu B., Oakeley E.J.,
RA   Zarhrate M., Nitschke P., Garfa-Traore M., Serluca F., Yang F.,
RA   Bouwmeester T., Pinson L., Cassuto E., Dubot P., Elshakhs N.A., Sahel J.A.,
RA   Salomon R., Drummond I.A., Gubler M.C., Antignac C., Chibout S.,
RA   Szustakowski J.D., Hildebrandt F., Lorentzen E., Sailer A.W., Benmerah A.,
RA   Saint-Mezard P., Saunier S.;
RT   "Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in
RT   microtubule stabilization.";
RL   Nat. Commun. 6:8666-8666(2015).
CC   -!- FUNCTION: Plays an inhibitory role on IL13 signaling by binding to
CC       IL13RA1 and recruits TRAF3 and DISC1 to the microtubules. Involved in
CC       the regulation of microtubule cytoskeleton organization. Is a negative
CC       regulator of microtubule stability, acting through the control of MAP4
CC       levels (PubMed:26487268). Involved in ciliogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q149C2, ECO:0000250|UniProtKB:Q8TDR0,
CC       ECO:0000269|PubMed:26487268}.
CC   -!- SUBUNIT: Component of the IFT complex B, at least composed of ift20,
CC       ift22, hspb11/ift25, ift27, ift46, ift52, traf3ip1/ift54, ift57, ift74,
CC       ift80, ift81, and ift88. Interacts with ift88 (By similarity).
CC       Interacts with il13ra1. Binds to microtubules, traf3 and disc1 (By
CC       similarity). Interacts with map4 (By similarity).
CC       {ECO:0000250|UniProtKB:Q149C2, ECO:0000250|UniProtKB:Q8TDR0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q8TDR0}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q8TDR0}. Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q149C2}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:Q149C2}. Note=Microtubules. In the cilium,
CC       it is observed at the ciliary base, ciliary transition zone and ciliary
CC       tip. {ECO:0000250|UniProtKB:Q8TDR0}.
CC   -!- SIMILARITY: Belongs to the TRAF3IP1 family. {ECO:0000305}.
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DR   EMBL; BC056776; AAH56776.1; -; mRNA.
DR   RefSeq; NP_956894.1; NM_200600.1.
DR   AlphaFoldDB; Q6PGZ3; -.
DR   SMR; Q6PGZ3; -.
DR   STRING; 7955.ENSDARP00000002437; -.
DR   PaxDb; Q6PGZ3; -.
DR   GeneID; 393572; -.
DR   KEGG; dre:393572; -.
DR   CTD; 26146; -.
DR   ZFIN; ZDB-GENE-040426-1146; traf3ip1.
DR   eggNOG; KOG3809; Eukaryota.
DR   InParanoid; Q6PGZ3; -.
DR   PhylomeDB; Q6PGZ3; -.
DR   Reactome; R-DRE-5620924; Intraflagellar transport.
DR   PRO; PR:Q6PGZ3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0030992; C:intraciliary transport particle B; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0043010; P:camera-type eye development; IMP:ZFIN.
DR   GO; GO:0090660; P:cerebrospinal fluid circulation; IMP:ZFIN.
DR   GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR   GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR   GO; GO:0048793; P:pronephros development; IMP:ZFIN.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0031113; P:regulation of microtubule polymerization; IMP:ZFIN.
DR   Gene3D; 1.10.418.50; -; 1.
DR   InterPro; IPR018799; TRAF3IP1.
DR   InterPro; IPR041476; TRAF3IP1_C.
DR   InterPro; IPR040468; TRAF3IP1_N.
DR   InterPro; IPR042576; TRAF3IP1_N_sf.
DR   PANTHER; PTHR31363; PTHR31363; 1.
DR   Pfam; PF10243; MIP-T3; 1.
DR   Pfam; PF17749; MIP-T3_C; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Reference proteome.
FT   CHAIN           1..629
FT                   /note="TRAF3-interacting protein 1"
FT                   /id="PRO_0000299547"
FT   REGION          130..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          220..282
FT                   /evidence="ECO:0000255"
FT   COILED          511..602
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        130..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  72010 MW;  02A3AF29AE5741E3 CRC64;
     MNESVAKKTQ ETLGKVIKKP PLTEKLLSKP PFRYLHDIFS EVIRTTGFMK GLYVEAEMKS
     DNVKDKDSKI AFLQKAIDVV MLVSGEPLAA KPARIVAGHE PEKTNELLQV IAKCCLNKLS
     SDEAVKRVLA GDKLDQKGKP STSRSQDKEN REGREHHRDR EERKGIKESS GSREQKDPDQ
     PKDQESKRDD KDRRRDAERS DKGRERERTK DRDRDKDKSR DREKDKTREK EREREKDRNR
     EKERERDKDR DKKKERESHK DRERDKDRER EKRREKEKDK ERPRETEEKL KDRGDRKIKA
     AEEISKSKPQ PEVASRTHQA ETEEAESPSR IPRPSSAKGQ RRKPKTGGQG TEQDETESEG
     EAEGPSAEKP IPLENGDVTD PAALQTTHSR RLPRPSSARP AAPRVKRQES YTDATPAERL
     GSGKTPASVI LDGKKLSEDE DDEDGQFVVE EAAPPPSDVP EVESNSLELQ GDDKHGGLVK
     KILETKKDYE SSPSSKSKEQ DRSLVSEASR KKERELVARE IERLRSSIQT VCRSALPLGK
     IMDYIQEDMD SMQNELQSWR KENKENAQAL LQEQRITDGV VEPLKVELAE LEQLIKDQQD
     KICAVKSNIL KNEEKIQKMV SSISFSSQT
 
 
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