Slc31a1
entrez
171135
canonical
uniprot
Q9JK41
canonical
genesymbol
Slc31a1
resolver
genesymbol_syn
Copt1
resolver
genesymbol_syn
Ctr1
resolver
uniprot
Q53YN6
resolver
uniprot_entry
COPT1_RAT
resolver
uniprot_sec
Q53YN6
resolver
activity_regulation
ACTIVITY REGULATION: Copper uptake is inhibited by cold temperature, silver and zinc ions (PubMed:23123662). Platinum-containing chemotherapeutic agents uptake is inhibited by cold temperature and copper (PubMed:23123662). {ECO:0000269|PubMed:23123662}.
uniprot
proteins
amino_acid_sequence
MRMNHMEMHHMGMNHTDDNITMPPHQHPTTSASHSHEMMMPMTFYFGFKNVDLLFSSLVINTPGEMAGAFVAVFLLAMFYEGLKIAREGLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH
uniprot
proteins
function
FUNCTION: [High affinity copper uptake protein 1]: Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane (PubMed:23123662). Then, delivers directly copper(1+) to specific chaperone such as ATOX1, via a copper(1+)- mediated transient interaction between the C-terminal domain and a copper(1+) chaperone, thus controlling intracellular copper(1+) levels (By similarity). May function in copper(1+) import from the apical membrane thus may drive intestinal copper absorption (By similarity). The copper(1+) transport mechanism is sodium-independent, saturable and of high-affinity (PubMed:23123662). Also mediates the uptake of silver(1+) (By similarity). May function in the influx of the platinum-containing chemotherapeutic agents (PubMed:23123662). The platinum-containing chemotherapeutic agents uptake is saturable (PubMed:23123662). Also participates in the first step of copper(2+) acquisition by cells through a direct transfer of copper(2+) from copper(2+) carriers in blood, such as ALB to the N-terminal domain of SLC31A1, leading to copper(2+) reduction and probably followed by copper(1+) stabilization (By similarity). In addition, functions as a redox sensor to promote angiogenesis in endothelial cells, in a copper(1+) transport independent manner, by transmitting the VEGF-induced ROS signal through a sulfenylation at Cys-189 leading to a subsequent disulfide bond formation between SLC31A1 and KDR (By similarity). The SLC31A1-KDR complex is then co-internalized to early endosomes, driving a sustained VEGFR2 signaling (By similarity). {ECO:0000250|UniProtKB:O15431, ECO:0000250|UniProtKB:Q8K211, ECO:0000269|PubMed:23123662}.; FUNCTION: [Truncated CTR1 form]: Mobilizes copper(1+) out of the endosomal compartment, making copper(1+) available for export out of the cells. {ECO:0000250|UniProtKB:Q8K211}.
uniprot
proteins
mass_dalton
21129
uniprot
proteins
post_translational_modification
PTM: O-Glycosylation at Thr-30 protects from proteolytic cleavage in the N-terminal extracellular domain. {ECO:0000250|UniProtKB:O15431}.; PTM: Proteolytic cleavage, leading to a truncated form, is facilitated by SLC31A2 and initiated preferentially by CTSL and to a minor extend by CTSB in endolysosomal compartments. A post-CTSL/cathepsin L processing occurs to yield to the fully truncated form. {ECO:0000250|UniProtKB:O15431}.; PTM: Sulfenylated at Cys-186 after stimulation with VEGFA, which induces SLC31A1-KDR disulfide bond formation and their co-internalization to early endosomes, driving to a sustained VEGFR2 signaling. {ECO:0000250|UniProtKB:O15431}.
uniprot
proteins
protein_family
Copper transporter (Ctr) (TC 1.A.56) family
uniprot
proteins
protein_family
SLC31A subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20699218
uniprot
proteins
pubmed
23123662
uniprot
proteins
sequence_length
187
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23123662}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O15431}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:O15431}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:20699218}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q8K211}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8K211}; Multi-pass membrane protein {ECO:0000255}. Note=The localization is controlled by the intra and extra-cellular copper concentration. Under conditions of elevated extracellular copper concentrations, it is rapidly internalized by endocytosis from the plasma membrane by a clathrin- and dynamin-mediated process and degradated in order to prevent intracellular copper accumulation and to reduce the transport of the copper across the membrane. The internalized SLC31A1 is then localized in early endosomes, and, upon a low extracellular copper concentrations, it is transported back to the plasma membrane in a RAB11A-dependent recycling pathway (By similarity). Localizes to the apical membrane in intestinal epithelial cells (PubMed:20699218). Localizes to the neuronal cell body plasma membranes (PubMed:23123662). Mainly localized on the basolateral side of renal tubular cells (By similarity). {ECO:0000250|UniProtKB:O15431, ECO:0000250|UniProtKB:Q8K211, ECO:0000269|PubMed:20699218, ECO:0000269|PubMed:23123662}.
uniprot
proteins
transmembrane_region
TRANSMEM 66..86; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 130..150; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 154..174; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins