SCAM1_RAT
ID SCAM1_RAT Reviewed; 338 AA.
AC P56603;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Secretory carrier-associated membrane protein 1;
DE Short=Secretory carrier membrane protein 1;
DE AltName: Full=SCAMP 37;
GN Name=Scamp1; Synonyms=Scamp;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8404846; DOI=10.1002/j.1460-2075.1993.tb06053.x;
RA Brand S.H., Castle J.D.;
RT "SCAMP 37, a new marker within the general cell surface recycling system.";
RL EMBO J. 12:3753-3761(1993).
RN [2]
RP INTERACTION WITH SYNRG AND ITSN1, AND FUNCTION.
RX PubMed=10777571; DOI=10.1074/jbc.275.17.12752;
RA Fernandez-Chacon R., Achiriloaie M., Janz R., Albanesi J.P., Suedhof T.C.;
RT "SCAMP1 function in endocytosis.";
RL J. Biol. Chem. 275:12752-12756(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface. {ECO:0000269|PubMed:10777571}.
CC -!- SUBUNIT: Interacts with SLC9A7 (By similarity). Interacts with SYNRG
CC and ITSN1. {ECO:0000250, ECO:0000269|PubMed:10777571}.
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; L22079; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S37395; S37395.
DR RefSeq; NP_001094106.1; NM_001100636.1.
DR AlphaFoldDB; P56603; -.
DR SMR; P56603; -.
DR BioGRID; 248159; 2.
DR ELM; P56603; -.
DR IntAct; P56603; 3.
DR MINT; P56603; -.
DR STRING; 10116.ENSRNOP00000014602; -.
DR iPTMnet; P56603; -.
DR PhosphoSitePlus; P56603; -.
DR SwissPalm; P56603; -.
DR jPOST; P56603; -.
DR PaxDb; P56603; -.
DR PRIDE; P56603; -.
DR Ensembl; ENSRNOT00000084044; ENSRNOP00000070553; ENSRNOG00000061582.
DR GeneID; 29521; -.
DR KEGG; rno:29521; -.
DR UCSC; RGD:3625; rat.
DR CTD; 9522; -.
DR RGD; 3625; Scamp1.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000157310; -.
DR InParanoid; P56603; -.
DR OrthoDB; 995882at2759; -.
DR PhylomeDB; P56603; -.
DR TreeFam; TF313797; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P56603; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
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; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0006897; P:endocytosis; IDA:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; ISO:RGD.
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_0000191253"
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..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..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:0007744|PubMed:22673903"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15126"
SQ SEQUENCE 338 AA; 37999 MW; 72E3BAD6A8FEBF59 CRC64;
MSDFDSNPFA DPDLNNPFKD PSVTQVTRNV PPGLDEYNPF SDSRTPPPGG 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
