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GOSR1_PONAB
ID   GOSR1_PONAB             Reviewed;         248 AA.
AC   Q5RBL6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Golgi SNAP receptor complex member 1;
DE   AltName: Full=28 kDa Golgi SNARE protein;
DE   AltName: Full=28 kDa cis-Golgi SNARE p28;
GN   Name=GOSR1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in transport from the ER to the Golgi apparatus as
CC       well as in intra-Golgi transport. It belongs to a super-family of
CC       proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive
CC       factor) attachment protein receptor. May play a protective role against
CC       hydrogen peroxide induced cytotoxicity under glutathione depleted
CC       conditions in neuronal cells by regulating the intracellular ROS levels
CC       via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14).
CC       Participates in docking and fusion stage of ER to cis-Golgi transport.
CC       Plays an important physiological role in VLDL-transport vesicle-Golgi
CC       fusion and thus in VLDL delivery to the hepatic cis-Golgi (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of several multiprotein Golgi SNARE complexes.
CC       Identified in a SNARE complex with BET1, STX5 and YKT6, in a SNARE
CC       complex with BET1L, STX5 and YKT6, in a SNARE complex with STX5, GOSR2,
CC       SEC22B and BET1, and in complex with STX5 and COG3. Interacts with
CC       GABARAPL2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type IV membrane protein {ECO:0000250}. Note=Localizes throughout
CC       the Golgi apparatus, with lowest levels in the trans-Golgi network.
CC       Enriched on vesicular components at the terminal rims of the Golgi.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}.
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DR   EMBL; CR858622; CAH90844.1; -; mRNA.
DR   RefSeq; NP_001125481.1; NM_001132009.1.
DR   AlphaFoldDB; Q5RBL6; -.
DR   SMR; Q5RBL6; -.
DR   STRING; 9601.ENSPPYP00000009145; -.
DR   GeneID; 100172390; -.
DR   KEGG; pon:100172390; -.
DR   CTD; 9527; -.
DR   eggNOG; KOG3208; Eukaryota.
DR   HOGENOM; CLU_078034_0_1_1; -.
DR   InParanoid; Q5RBL6; -.
DR   OMA; QAYAVND; -.
DR   TreeFam; TF105782; -.
DR   Proteomes; UP000001595; Chromosome 17.
DR   GO; GO:0005801; C:cis-Golgi network; IEA:InterPro.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR023601; Golgi_SNAP_su1.
DR   PANTHER; PTHR21094; PTHR21094; 1.
DR   PIRSF; PIRSF027109; Golgi_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; ER-Golgi transport; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95249"
FT   CHAIN           2..248
FT                   /note="Golgi SNAP receptor complex member 1"
FT                   /id="PRO_0000212544"
FT   TOPO_DOM        2..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   REGION          37..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          10..30
FT                   /evidence="ECO:0000255"
FT   COILED          68..92
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O95249"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95249"
SQ   SEQUENCE   248 AA;  28336 MW;  4D7352345FE00AC4 CRC64;
     MAAGTSNYWE DLRKQARQLE NELDLKLVSF SKLCTSYSHS STRDGRRDSS DTTPLLNGSS
     QDRMFETMAI EIEQLLARLT GVNDKMAEYT NSAGVPSLNA ALMHTLQRHR DILQDYTHEF
     HKTKANFMSI RERENLMGSV RKDIESYKSG SGVNNRRTEL FLKEHDHLRN SDRLIEETIS
     IAMATKENMT SQRGMLKSIH SKMNTLANRF PAVNSLIQRI NLRKRRDSLI LGGVIGICTI
     LLLLYAFH
 
 
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