SCAM2_MOUSE
ID SCAM2_MOUSE Reviewed; 329 AA.
AC Q9ERN0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Secretory carrier-associated membrane protein 2;
DE Short=Secretory carrier membrane protein 2;
GN Name=Scamp2;
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].
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=Kidney;
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, 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 SLC6A4 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; AF295402; AAG22799.1; -; mRNA.
DR EMBL; BC014751; AAH14751.1; -; mRNA.
DR CCDS; CCDS23224.1; -.
DR RefSeq; NP_073724.1; NM_022813.3.
DR AlphaFoldDB; Q9ERN0; -.
DR SMR; Q9ERN0; -.
DR BioGRID; 204859; 2.
DR STRING; 10090.ENSMUSP00000038350; -.
DR iPTMnet; Q9ERN0; -.
DR PhosphoSitePlus; Q9ERN0; -.
DR SwissPalm; Q9ERN0; -.
DR EPD; Q9ERN0; -.
DR jPOST; Q9ERN0; -.
DR MaxQB; Q9ERN0; -.
DR PaxDb; Q9ERN0; -.
DR PRIDE; Q9ERN0; -.
DR ProteomicsDB; 253404; -.
DR Antibodypedia; 14704; 294 antibodies from 26 providers.
DR DNASU; 24044; -.
DR Ensembl; ENSMUST00000045791; ENSMUSP00000038350; ENSMUSG00000040188.
DR GeneID; 24044; -.
DR KEGG; mmu:24044; -.
DR UCSC; uc009pve.2; mouse.
DR CTD; 10066; -.
DR MGI; MGI:1346518; Scamp2.
DR VEuPathDB; HostDB:ENSMUSG00000040188; -.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000156476; -.
DR HOGENOM; CLU_066546_0_0_1; -.
DR InParanoid; Q9ERN0; -.
DR OMA; EPVDQYN; -.
DR OrthoDB; 995882at2759; -.
DR PhylomeDB; Q9ERN0; -.
DR TreeFam; TF313797; -.
DR BioGRID-ORCS; 24044; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Scamp2; mouse.
DR PRO; PR:Q9ERN0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ERN0; protein.
DR Bgee; ENSMUSG00000040188; Expressed in spermatid and 257 other tissues.
DR ExpressionAtlas; Q9ERN0; baseline and differential.
DR Genevisible; Q9ERN0; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; ISO: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 Endosome; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..329
FT /note="Secretory carrier-associated membrane protein 2"
FT /id="PRO_0000191255"
FT TOPO_DOM 1..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..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..262
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..218
FT /note="Interaction with SLC9A7"
FT /evidence="ECO:0000250"
FT COMPBIAS 18..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15127"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15127"
SQ SEQUENCE 329 AA; 36465 MW; EAA185E68E044D80 CRC64;
MSAFDTNPFA DPVDVNPFQD PSVTQLTNAP QSGLAEFNPF SETNAATTVP ATQAPGPSQP
AVLQPSVEPA QPTPQAVAAA AQAGLLRQQE ELDRKAAELE RKERELQNTA ANLHVRDNNW
PPLPSWCPVK PCFYQDFSTE IPADYQRICK MLYYLWMLHS VTLFLNLLAC LAWFTSDAAN
GTAFGLSILW FLIFTPCAFL CWYRPIYKAF RSDNSFSFFV FFFVFFCQIG IYFIQLIGLP
NLGTSGWLAA LSTMKNGPLA VTIIMMVVAG FFTLCAGLSL FLLQRVHAFY RRTGASFQQA
QEEFSQGIFS SRTFRGAASS AARGAFQGN
