SCAM1_MOUSE
ID SCAM1_MOUSE Reviewed; 338 AA.
AC Q8K021;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Secretory carrier-associated membrane protein 1;
DE Short=Secretory carrier membrane protein 1;
GN Name=Scamp1;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [2]
RP PROTEIN SEQUENCE OF 91-103 AND 299-334, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SYNRG, ITSN1 and SLC9A7. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: 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}.
CC -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
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DR EMBL; BC034283; AAH34283.1; -; mRNA.
DR CCDS; CCDS36750.1; -.
DR RefSeq; NP_083429.1; NM_029153.1.
DR AlphaFoldDB; Q8K021; -.
DR BioGRID; 223555; 7.
DR IntAct; Q8K021; 1.
DR STRING; 10090.ENSMUSP00000022197; -.
DR iPTMnet; Q8K021; -.
DR PhosphoSitePlus; Q8K021; -.
DR SwissPalm; Q8K021; -.
DR EPD; Q8K021; -.
DR jPOST; Q8K021; -.
DR MaxQB; Q8K021; -.
DR PaxDb; Q8K021; -.
DR PRIDE; Q8K021; -.
DR ProteomicsDB; 255479; -.
DR Antibodypedia; 24511; 161 antibodies from 25 providers.
DR DNASU; 107767; -.
DR Ensembl; ENSMUST00000022197; ENSMUSP00000022197; ENSMUSG00000021687.
DR GeneID; 107767; -.
DR KEGG; mmu:107767; -.
DR UCSC; uc007rlr.1; mouse.
DR CTD; 9522; -.
DR MGI; MGI:1349480; Scamp1.
DR VEuPathDB; HostDB:ENSMUSG00000021687; -.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000157310; -.
DR InParanoid; Q8K021; -.
DR OMA; NMVACIF; -.
DR OrthoDB; 995882at2759; -.
DR PhylomeDB; Q8K021; -.
DR TreeFam; TF313797; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 107767; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Scamp1; mouse.
DR PRO; PR:Q8K021; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8K021; protein.
DR Bgee; ENSMUSG00000021687; Expressed in ventral tegmental area and 248 other tissues.
DR ExpressionAtlas; Q8K021; baseline and differential.
DR Genevisible; Q8K021; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; TAS:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endosome; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15126"
FT CHAIN 2..338
FT /note="Secretory carrier-associated membrane protein 1"
FT /id="PRO_0000191251"
FT TOPO_DOM 2..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..261
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O15126"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56603"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15126"
SQ SEQUENCE 338 AA; 38029 MW; 7588A06064B23B9D CRC64;
MSDFDSNPFA DPDLNNPFKD PSVTQVTRNV PPGLDEYNPF SDSRTPPPGS VKMPNVPNTQ
PAIMKPTEEH PAYTQITKEH ALAQAELLKR QEELERKAAE LDRREREMQN LSQHGRKNNW
PPLPSNFPVG PCFYQDFSVD IPVEFQKTVK LMYYLWMFHA VTLFLNIFGC LAWFCVDSSR
AVDFGLSILW FLLFTPCSFV CWYRPLYGAF RSDSSFRFFV FFFVYICQFA VHVLQAAGFH
NWGNCGWISS LTGLNKNIPV GIMMIIIAAL FTASAVISLV MFKKVHGLYR TTGASFEKAQ
QEFATGVMSN KTVQTAAANA ASTAATSAAQ NAFKGNQM
