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SEC20_MOUSE
ID   SEC20_MOUSE             Reviewed;         228 AA.
AC   Q6QD59; B0V2Q1; Q5M9M2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Vesicle transport protein SEC20;
GN   Name=Bnip1 {ECO:0000312|MGI:MGI:109328};
GN   Synonyms=Sec20 {ECO:0000312|EMBL:AAS55065.1}, Sec20l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:AAS55065.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Verrier S., Willmann M., Fischer von Mollard G., Soeling H.-D.;
RT   "SNARE proteins involved in Golgi-endoplasmic reticulum transport in
RT   mammalian cells.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000312|EMBL:AAH86888.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH86888.1};
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: As part of a SNARE complex may be involved in endoplasmic
CC       reticulum membranes fusion and be required for the maintenance of
CC       endoplasmic reticulum organization. Also plays a role in apoptosis. It
CC       is for instance required for endoplasmic reticulum stress-induced
CC       apoptosis. As a substrate of RNF185 interacting with SQSTM1, might also
CC       be involved in mitochondrial autophagy. {ECO:0000250|UniProtKB:Q12981}.
CC   -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC       BNIP1/SEC20L and SEC22B. Interacts directly with STX18, RINT1/TIP20L
CC       and NAPA. Interacts with ZW10 through RINT1. Interacts with BCL2.
CC       Interacts with RNF186. Interacts with RNF185. Interacts with SQSTM1;
CC       increased by 'Lys-63'-linked polyubiquitination of BNIP1.
CC       {ECO:0000250|UniProtKB:Q12981}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q12981}; Single-pass type IV membrane protein
CC       {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q12981};
CC       Single-pass type IV membrane protein {ECO:0000255}. Note=Localization
CC       to the mitochondrion is regulated by RNF186.
CC       {ECO:0000250|UniProtKB:Q12981}.
CC   -!- PTM: Polyubiquitinated. 'Lys-63'-linked polyubiquitination by RNF185
CC       increases the interaction with the autophagy receptor SQSTM1. Undergoes
CC       'Lys-29'- and 'Lys-63'-linked polyubiquitination by RNF186 that may
CC       regulate BNIP1 localization to the mitochondrion.
CC       {ECO:0000250|UniProtKB:Q12981}.
CC   -!- SIMILARITY: Belongs to the SEC20 family. {ECO:0000305}.
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DR   EMBL; AY547731; AAS55065.1; -; mRNA.
DR   EMBL; CT025550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC086888; AAH86888.1; -; mRNA.
DR   CCDS; CCDS28555.1; -.
DR   RefSeq; NP_742161.4; NM_172149.5.
DR   AlphaFoldDB; Q6QD59; -.
DR   SMR; Q6QD59; -.
DR   BioGRID; 230293; 2.
DR   STRING; 10090.ENSMUSP00000015725; -.
DR   iPTMnet; Q6QD59; -.
DR   PhosphoSitePlus; Q6QD59; -.
DR   EPD; Q6QD59; -.
DR   jPOST; Q6QD59; -.
DR   MaxQB; Q6QD59; -.
DR   PaxDb; Q6QD59; -.
DR   PeptideAtlas; Q6QD59; -.
DR   PRIDE; Q6QD59; -.
DR   ProteomicsDB; 256610; -.
DR   Antibodypedia; 2356; 546 antibodies from 35 providers.
DR   DNASU; 224630; -.
DR   Ensembl; ENSMUST00000015725; ENSMUSP00000015725; ENSMUSG00000024191.
DR   GeneID; 224630; -.
DR   KEGG; mmu:224630; -.
DR   UCSC; uc008ben.2; mouse.
DR   CTD; 662; -.
DR   MGI; MGI:109328; Bnip1.
DR   VEuPathDB; HostDB:ENSMUSG00000024191; -.
DR   eggNOG; ENOG502QUTT; Eukaryota.
DR   GeneTree; ENSGT00390000014412; -.
DR   InParanoid; Q6QD59; -.
DR   OMA; DDWARDT; -.
DR   OrthoDB; 1328108at2759; -.
DR   PhylomeDB; Q6QD59; -.
DR   TreeFam; TF324339; -.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 224630; 15 hits in 72 CRISPR screens.
DR   ChiTaRS; Bnip1; mouse.
DR   PRO; PR:Q6QD59; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q6QD59; protein.
DR   Bgee; ENSMUSG00000024191; Expressed in hindlimb stylopod muscle and 221 other tissues.
DR   ExpressionAtlas; Q6QD59; baseline and differential.
DR   Genevisible; Q6QD59; MM.
DR   GO; GO:0030137; C:COPI-coated vesicle; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0031201; C:SNARE complex; ISS:HGNC-UCL.
DR   GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR   GO; GO:0016320; P:endoplasmic reticulum membrane fusion; ISS:HGNC-UCL.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISS:HGNC-UCL.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   InterPro; IPR005606; Sec20.
DR   PANTHER; PTHR12825; PTHR12825; 1.
DR   Pfam; PF03908; Sec20; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Coiled coil; Endoplasmic reticulum; ER-Golgi transport;
KW   Membrane; Mitochondrion; Protein transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..228
FT                   /note="Vesicle transport protein SEC20"
FT                   /id="PRO_0000232417"
FT   TOPO_DOM        1..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..228
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   COILED          37..90
FT                   /evidence="ECO:0000255"
FT   CONFLICT        125
FT                   /note="K -> N (in Ref. 3; AAH86888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="S -> G (in Ref. 3; AAH86888)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   228 AA;  26175 MW;  FA7E3922DC1AF2E3 CRC64;
     MAAPQDVHVR ICNQEIVKFD LEVKALIQDI RDCSGPLSEL TELNTKVKEK FQQLKQRIQE
     LEQSAREQDK ESEKQLLLQE VENHKKQMLS NQTSWRKANL TCKLAIDNLE KAELLQGGDS
     LRQRKTTKES LAQTSSSITE SLMGISRMMS QQVQQSEEAM QTLVSSSRTL LDANEEFKSM
     SGTIQLGRKL ITKYNRRELT DKLLIFLALA LFLATVLYIV KKRLFPFL
 
 
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