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HRP65_CHITE
ID   HRP65_CHITE             Reviewed;         535 AA.
AC   Q9U1N0; Q95ZG9; Q95ZH0;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Hrp65 protein;
DE   AltName: Full=Ct-Hrp65;
GN   Name=HRP65;
OS   Chironomus tentans (Midge) (Camptochironomus tentans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Chironominae; Chironomus.
OX   NCBI_TaxID=7153 {ECO:0000312|EMBL:CAB64926.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 131-134;
RP   149-154; 216-223; 226-236; 329-341 AND 382-389, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Salivary gland;
RX   PubMed=10648560; DOI=10.1083/jcb.148.2.271;
RA   Miralles F., Oefverstedt L.-G., Sabri N., Aissouni Y., Hellman U.,
RA   Skoglund U., Visa N.;
RT   "Electron tomography reveals posttranscriptional binding of pre-mRNPs to
RT   specific fibers in the nucleoplasm.";
RL   J. Cell Biol. 148:271-282(2000).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2 AND 3), AND SUBCELLULAR LOCATION.
RC   TISSUE=Salivary gland;
RX   PubMed=11262185; DOI=10.1006/excr.2000.5127;
RA   Miralles F., Visa N.;
RT   "Molecular characterization of Ct-hrp65: identification of two novel
RT   isoforms originated by alternative splicing.";
RL   Exp. Cell Res. 264:284-295(2001).
CC   -!- FUNCTION: Component of nuclear connecting fibers associated with the
CC       transport of ribonucleoprotein particles from either the chromosome to
CC       the nuclear pore complex or their transient retention in the
CC       nucleoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:11262185};
CC         IsoId=Q9U1N0-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:11262185};
CC         IsoId=Q9U1N0-2; Sequence=VSP_050278;
CC       Name=3 {ECO:0000269|PubMed:11262185};
CC         IsoId=Q9U1N0-3; Sequence=VSP_050279;
CC   -!- DEVELOPMENTAL STAGE: Isoforms 1 and 2 are expressed in embryo, larva
CC       and adult while isoform 3 is expressed only in embryo.
CC       {ECO:0000269|PubMed:10648560, ECO:0000269|PubMed:11262185}.
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DR   EMBL; AJ243013; CAB64926.1; -; mRNA.
DR   EMBL; AJ404654; CAC42829.1; -; Genomic_DNA.
DR   EMBL; AJ404654; CAC42828.1; -; Genomic_DNA.
DR   EMBL; AJ404654; CAC42830.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U1N0; -.
DR   SMR; Q9U1N0; -.
DR   PRIDE; Q9U1N0; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; NAS:UniProtKB.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012975; NOPS.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF08075; NOPS; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Nucleus; Repeat; RNA-binding.
FT   CHAIN           1..535
FT                   /note="Hrp65 protein"
FT                   /id="PRO_0000081611"
FT   DOMAIN          113..185
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          187..268
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         500..535
FT                   /note="DQGNRFDGPPQRGNVRPWNNNDRGHRDDFQNKRRRY -> YYRPYVNQRPQK
FT                   ARYRNG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11262185"
FT                   /id="VSP_050278"
FT   VAR_SEQ         500..535
FT                   /note="DQGNRFDGPPQRGNVRPWNNNDRGHRDDFQNKRRRY -> KINNYKSTLKNL
FT                   I (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11262185"
FT                   /id="VSP_050279"
SQ   SEQUENCE   535 AA;  61891 MW;  B6D5BCF701099836 CRC64;
     MDVKAEAPNG PAPVKNENQN QPKPQRENMN MNKNQNQNQN NNMGGGGGPN KRNNMNMNKN
     FQNRGGKGGP GMGPRGPMKN EDFIVNSKLK NLAGPTHDLP ELVCEEIKFS GRNRLYIGNL
     TSDVTEEELK ELFSPYGEIS EAFINAEKNF AFLKIDYRAN AERAKKDLDG RMRKNKPIRI
     RFAPNATTIR VKNLTPFVSN ELLFKSFEVF GQVERAVIIV DDRGKTTGEG IVEFARKSGA
     MSALKYCSEK CYFLTSSLRP CVVETFDHID ETDGFPEKSL MRKSNDYYKA RQNGPRFAEM
     GSFEHEFGTK WKQMYDMYKQ KHDALKREMQ LEEEKLEAQM EYAKFEHETE SLREQLRKRE
     QDRDRQKKEW EDRERQADES RIRDEQQMRR QQDDMQMRMQ RQDEEMRRRQ QENSLFMQAQ
     QLSNMLDQQE MNHQGGGGGG GNGGNGNNQG GGGNQGGGRR NYNNDRNNDR NQNFDMMNQG
     GGNHGGNQYQ GNQHYQGNQD QGNRFDGPPQ RGNVRPWNNN DRGHRDDFQN KRRRY
 
 
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