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SIL1_RAT
ID   SIL1_RAT                Reviewed;         465 AA.
AC   Q6P6S4;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Nucleotide exchange factor SIL1;
DE   Flags: Precursor;
GN   Name=Sil1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for protein translocation and folding in the
CC       endoplasmic reticulum (ER). Functions as a nucleotide exchange factor
CC       for the ER lumenal chaperone HSPA5. {ECO:0000250|UniProtKB:Q9H173}.
CC   -!- SUBUNIT: Interacts with HSPA5. {ECO:0000250|UniProtKB:Q9H173}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:Q9H173}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9H173}.
CC   -!- PTM: Ubiquitinated by the CRL2(FEM1A) and CRL2(FEM1C) complexes, which
CC       recognize the -Lys-Xaa-Xaa-Arg C-degron at the C-terminus, leading to
CC       its degradation. {ECO:0000250|UniProtKB:Q9H173}.
CC   -!- SIMILARITY: Belongs to the SIL1 family. {ECO:0000305}.
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DR   EMBL; BC062050; AAH62050.1; -; mRNA.
DR   RefSeq; NP_955408.1; NM_199376.1.
DR   RefSeq; XP_008770247.1; XM_008772025.2.
DR   RefSeq; XP_017456394.1; XM_017600905.1.
DR   AlphaFoldDB; Q6P6S4; -.
DR   SMR; Q6P6S4; -.
DR   IntAct; Q6P6S4; 1.
DR   STRING; 10116.ENSRNOP00000026895; -.
DR   GlyGen; Q6P6S4; 2 sites.
DR   PaxDb; Q6P6S4; -.
DR   PRIDE; Q6P6S4; -.
DR   Ensembl; ENSRNOT00000026895; ENSRNOP00000026895; ENSRNOG00000019826.
DR   GeneID; 291673; -.
DR   KEGG; rno:291673; -.
DR   UCSC; RGD:735103; rat.
DR   CTD; 64374; -.
DR   RGD; 735103; Sil1.
DR   eggNOG; KOG2160; Eukaryota.
DR   GeneTree; ENSGT00940000153909; -.
DR   HOGENOM; CLU_046547_1_0_1; -.
DR   InParanoid; Q6P6S4; -.
DR   OMA; FQPTHEW; -.
DR   OrthoDB; 1501690at2759; -.
DR   PhylomeDB; Q6P6S4; -.
DR   TreeFam; TF324307; -.
DR   PRO; PR:Q6P6S4; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000019826; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q6P6S4; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Protein transport; Reference proteome;
KW   Signal; Translocation; Transport; Ubl conjugation.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..465
FT                   /note="Nucleotide exchange factor SIL1"
FT                   /id="PRO_0000223356"
FT   REGION          1..260
FT                   /note="Interaction with HSPA5 and localization to the
FT                   endoplasmic reticulum"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EPK6"
FT   REGION          39..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   465 AA;  52350 MW;  5645924C08F6A8FF CRC64;
     MAPQHLPSTR MAPQGMLLGL LLASCLTFCL SCQNSNNFAL TNPEKSTHED SDTKETRREE
     ELDAEVLEVL NPTQEWQALQ PGQAVPAGSH VRMNLQTGVN EVKLQQEDKF QSNWKGFKRG
     RRLDINTNTY TSQDLKSALA KFKEGTEMEN SKDELARQAT VKQLFRPIEE LKKEFDELNV
     VLETDMQIMV RLINKFNSSS SSLEEKVAAL FDLEYYVHQM DNAQDLLSFG GLQVVINGLN
     STEPLVKEYA AFVLGAAFSS NPKVQVEAIE GGALQKLLVI LATEQPLPAK KKVLFALCSL
     LRHFPYAQQQ FLKLGGLQVL RSLVQEKSAK VLAVRVVTLL YDLVTEKMFA EEEAELTQES
     SPEKLQQYRQ VQLLPGLREQ GWCEITAQLL ALPEHDAREK VLQTLGALLA TCRDRYRQDL
     ELSRTLGSLQ AEYQALASLE LQEGEDDGYF RELLASIDSL VKELR
 
 
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