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SCAM5_RAT
ID   SCAM5_RAT               Reviewed;         235 AA.
AC   Q9JKE3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Secretory carrier-associated membrane protein 5;
DE            Short=Secretory carrier membrane protein 5;
GN   Name=Scamp5;
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 [MRNA].
RX   PubMed=11050114; DOI=10.1523/jneurosci.20-21-07941.2000;
RA   Fernandez-Chacon R., Suedhof T.C.;
RT   "Novel SCAMPs lacking NPF repeats: ubiquitous and synaptic vesicle-specific
RT   forms implicate SCAMPs in multiple membrane-trafficking functions.";
RL   J. Neurosci. 20:7941-7950(2000).
CC   -!- FUNCTION: Required for the calcium-dependent exocytosis of signal
CC       sequence-containing cytokines such as CCL5. Probably acts in
CC       cooperation with the SNARE machinery (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via C-terminal part) with SYT1 and SYT2;
CC       interaction with synaptotagmins making a link with the SNARE molecules.
CC       Interacts with SLC9A7 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi
CC       network membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Note=Mainly localizes in Golgi apparatus membrane. Upon
CC       calcium-triggered exocytosis, it translocates to the cell membrane.
CC       Highly enriched in synaptic vesicles (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SCAMP family. SCAMP5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF240784; AAF64466.1; -; mRNA.
DR   RefSeq; NP_113914.1; NM_031726.1.
DR   AlphaFoldDB; Q9JKE3; -.
DR   SMR; Q9JKE3; -.
DR   BioGRID; 249284; 2.
DR   IntAct; Q9JKE3; 2.
DR   MINT; Q9JKE3; -.
DR   STRING; 10116.ENSRNOP00000033401; -.
DR   SwissPalm; Q9JKE3; -.
DR   jPOST; Q9JKE3; -.
DR   PaxDb; Q9JKE3; -.
DR   PRIDE; Q9JKE3; -.
DR   GeneID; 65171; -.
DR   KEGG; rno:65171; -.
DR   CTD; 192683; -.
DR   RGD; 68356; Scamp5.
DR   eggNOG; KOG3088; Eukaryota.
DR   InParanoid; Q9JKE3; -.
DR   PhylomeDB; Q9JKE3; -.
DR   PRO; PR:Q9JKE3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR   GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045806; P:negative regulation of endocytosis; ISO:RGD.
DR   GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IDA:SynGO.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR   InterPro; IPR007273; SCAMP.
DR   PANTHER; PTHR10687; PTHR10687; 1.
DR   Pfam; PF04144; SCAMP; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Endosome; Exocytosis; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..235
FT                   /note="Secretory carrier-associated membrane protein 5"
FT                   /id="PRO_0000191264"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..67
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..148
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   235 AA;  26098 MW;  5C2C35578FB1399F CRC64;
     MAEKVNNFPP LPKFIPLKPC FYQDFEADIP PQHLSLTKRL YYLWMLNSVT LAVNLVGCLA
     WLIGGGGATN FGLAFLWLIL FTPCSYVCWF RPIYKAFKTD SSFSFMAFFF TFMAQLVISI
     IQAVGIPGWG VCGWIATISF FGTNIGSAVV MLIPTVMFTV VAVFSFIALS MVHKFYRGSG
     GSFSKAQEEW TTGAWKNPHV QQAAQNAAMG AAQGAMNQPQ TQYSTTPNYT YSNEM
 
 
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