SCAM5_MOUSE
ID SCAM5_MOUSE Reviewed; 235 AA.
AC Q9JKD3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Secretory carrier-associated membrane protein 5;
DE Short=Secretory carrier membrane protein 5;
GN Name=Scamp5;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: 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:0000269|PubMed:11050114};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11050114}. Golgi
CC apparatus membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Recycling
CC endosome membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:11050114}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11050114}. Note=Mainly localizes in Golgi apparatus
CC membrane. Upon calcium-triggered exocytosis, it translocates to the
CC cell membrane. Highly enriched in synaptic vesicles (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:11050114}.
CC -!- DEVELOPMENTAL STAGE: Expressed late in development coincident with the
CC elaboration of mature synapses.
CC -!- SIMILARITY: Belongs to the SCAMP family. SCAMP5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF241833; AAF64491.1; -; mRNA.
DR EMBL; BC018613; AAH18613.1; -; mRNA.
DR CCDS; CCDS40649.1; -.
DR RefSeq; NP_001288563.1; NM_001301634.1.
DR RefSeq; NP_001288564.1; NM_001301635.1.
DR RefSeq; NP_064666.1; NM_020270.3.
DR RefSeq; XP_006511383.1; XM_006511320.3.
DR RefSeq; XP_017168984.1; XM_017313495.1.
DR AlphaFoldDB; Q9JKD3; -.
DR SMR; Q9JKD3; -.
DR BioGRID; 208182; 4.
DR STRING; 10090.ENSMUSP00000035898; -.
DR iPTMnet; Q9JKD3; -.
DR PhosphoSitePlus; Q9JKD3; -.
DR SwissPalm; Q9JKD3; -.
DR MaxQB; Q9JKD3; -.
DR PaxDb; Q9JKD3; -.
DR PeptideAtlas; Q9JKD3; -.
DR PRIDE; Q9JKD3; -.
DR ProteomicsDB; 255355; -.
DR Antibodypedia; 27182; 63 antibodies from 16 providers.
DR DNASU; 56807; -.
DR Ensembl; ENSMUST00000046587; ENSMUSP00000035898; ENSMUSG00000040722.
DR Ensembl; ENSMUST00000214256; ENSMUSP00000150867; ENSMUSG00000040722.
DR GeneID; 56807; -.
DR KEGG; mmu:56807; -.
DR UCSC; uc009puw.2; mouse.
DR CTD; 192683; -.
DR MGI; MGI:1928948; Scamp5.
DR VEuPathDB; HostDB:ENSMUSG00000040722; -.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000157577; -.
DR HOGENOM; CLU_066546_1_0_1; -.
DR InParanoid; Q9JKD3; -.
DR OMA; RHNDPNP; -.
DR OrthoDB; 995882at2759; -.
DR PhylomeDB; Q9JKD3; -.
DR TreeFam; TF313797; -.
DR BioGRID-ORCS; 56807; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Scamp5; mouse.
DR PRO; PR:Q9JKD3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JKD3; protein.
DR Bgee; ENSMUSG00000040722; Expressed in retinal neural layer and 204 other tissues.
DR ExpressionAtlas; Q9JKD3; baseline and differential.
DR Genevisible; Q9JKD3; MM.
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:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISS:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein 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_0000191263"
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; 26068 MW; 5C2C25568FB1399F CRC64;
MAEKVNNFPP LPKFIPLKPC FYQDFEADIP PQHLSLTKRL YYLWMLNSVT LAVNLVGCLA
WLIGGGGATN FGLAFLWLIL FTPCSYVCWF RPIYKAFKTD SSFSFMAFFF TFMAQLVISI
IQAVGIPGWG VCGWIATISF FGTNIGSAVV MLIPTVMFTV VAVFSFIALS MVHKFYRGSG
GSFSKAQEEW TTGAWKNPHV QQAAQNAAMG AAQGAMNQPQ TQYSATPNYT YSNEM
