SCAM1_PIG
ID SCAM1_PIG Reviewed; 338 AA.
AC O77735;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Secretory carrier-associated membrane protein 1;
DE Short=Secretory carrier membrane protein 1;
GN Name=SCAMP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=German Landrace; TISSUE=Brain, and Liver;
RX PubMed=9657850; DOI=10.1007/s003359900814;
RA Wen G., Leeb T., Hui D., Baumgartner B.G., Robic A., Hameister H.,
RA Brenig B.;
RT "Structural and functional analysis of the porcine secretory carrier
RT membrane protein 1 gene (SCAMP1).";
RL Mamm. Genome 9:536-539(1998).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface.
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; AJ223734; CAA11536.1; -; Genomic_DNA.
DR EMBL; AJ223735; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; AJ223736; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; AJ223737; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; AJ223738; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; AJ223739; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; AJ223740; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; AJ223741; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; AJ223742; CAA11536.1; JOINED; Genomic_DNA.
DR EMBL; Y15710; CAA75731.1; -; mRNA.
DR RefSeq; NP_999410.1; NM_214245.1.
DR RefSeq; XP_013842293.1; XM_013986839.1.
DR AlphaFoldDB; O77735; -.
DR SMR; O77735; -.
DR STRING; 9823.ENSSSCP00000014995; -.
DR PaxDb; O77735; -.
DR PeptideAtlas; O77735; -.
DR PRIDE; O77735; -.
DR Ensembl; ENSSSCT00005025505; ENSSSCP00005015441; ENSSSCG00005016123.
DR Ensembl; ENSSSCT00055038469; ENSSSCP00055030564; ENSSSCG00055019570.
DR Ensembl; ENSSSCT00070010296; ENSSSCP00070008446; ENSSSCG00070005425.
DR GeneID; 397477; -.
DR KEGG; ssc:397477; -.
DR CTD; 9522; -.
DR eggNOG; KOG3088; Eukaryota.
DR InParanoid; O77735; -.
DR OMA; NMVACIF; -.
DR OrthoDB; 995882at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW 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_0000191252"
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..63
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; 37919 MW; 82FA42B1ED9115EF CRC64;
MSDFDSNPFA DPDLNNPFKD PSVTQVTRNV PPGLDEYNPF SDSRTPPPGN VKMPNVPSTQ
PAIMKPTEEH PAYTQIAKEH ALAQAELLKR QEELERKAAE LDRREREMQN LSQHGRKNNW
PPLPGNFPVG PCFYQDFSVD IPVEFQKTVK IMYYLWMFHA VTLFLNIFGC LAWFCVDPSR
GVDFGLSILW FLLFTPCSFV CWYRPLYGAF RSDSSFRFFV FFFVYICQFA VHVLQAAGFH
NWGNCGWISS LTGLNQSIPV GIMMIIIAAL FTASAVISLV MFKKVHGLYR TTGASFEKAQ
QEFATGVMSN KTVQTAAANA ASTAATSAAQ NAFKGNQI
