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